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Небесная энциклопедия

Космические корабли и станции, автоматические КА и методы их проектирования, бортовые комплексы управления, системы и средства жизнеобеспечения, особенности технологии производства ракетно-космических систем

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Мониторинг СМИ

Мониторинг СМИ и социальных сетей. Сканирование интернета, новостных сайтов, специализированных контентных площадок на базе мессенджеров. Гибкие настройки фильтров и первоначальных источников.

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Применить Всего найдено 3294. Отображено 100.

31-05-2012 дата публикации

Pharmaceutical composition containing nuclear factor involved in proliferation and differentiation of central neuronal cells

Номер: US20120134969A1

Автор: Hideki Ando, Hiroshi Handa, Kentaro Hotta, Takumi Itoh

Принадлежит: Tokyo Institute of Technology NUC

With an aim to provide a novel factor inducing proliferation of neural stem cells and differentiation of these cells into nerve cells, a pharmaceutical composition comprising 1) CRBN, 2) a nucleic acid encoding CRBN, or 3) a stem cell or a neural progenitor cell in which CRBN is expressed, a method including administering the pharmaceutical composition to a non-human animal and inducing proliferation of neural stem cells or neural progenitor cells of the non-human animal and differentiation of these cells into nerve cells, and a method for screening for a therapeutic drug for a disease of cerebral cortex or a surgical injury of cerebral cortex, using CRBN, are provided.

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Номер записи: 1

16-08-2012 дата публикации

Endoglucanase variants

Номер: US20120208235A1

Автор: Ish Kumar Dhawan, Jie Yang, Sachin Patil, Xiyun Zhang

Принадлежит: Codexis Inc

The present invention relates to variant endoglucanases having improved thermoactivity, improved thermostability, and improved viscosity reduction activity over wild-type M. thermophila endoglucanase.

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Номер записи: 2

01-11-2012 дата публикации

Accelerated fungal growth

Номер: US20120276246A1

Автор: Natalja Alekseevna Cyplenkova, Robert John Bromley Savage, Van Rutger Jan Rooijen

Принадлежит: DSM IP ASSETS BV

The present invention relates to a process for the preparation of fermented food wherein a carboxypeptidase preparation is used to obtain accelerated fungal growth.

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Номер записи: 3

07-02-2013 дата публикации

Collagen mixture and method of making the same

Номер: US20130035473A1

Автор: Dana Summers, Robert Den Hoed

Принадлежит: Individual

A collagen mixture having a portion of unhydrolyzed eggshell membrane collagen and Avian collagen.

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Номер записи: 4

28-03-2013 дата публикации

Method for protein production in filamentous fungi

Номер: US20130078674A1

Автор: Hakkinen Mari, Pakula Tiina, Penttilä Merja, Saloheimo Markku, Vitikainen Marika, Westerholm-Parvinen Ann

Принадлежит: TEKNOLOGIAN TUTKIMUSKESKUS VTT

The present invention relates to a method for genetically modifying a filamentous fungus host for improved protein production. The method comprises that a filamentous fungus host is genetically modified to overexpress or to be deficient of specific genes. The invention relates also to the modified hosts. Furthermore, the invention relates to a method for improved production or for producing an improved composition of proteins, such as cellulases, hemicellulases, other proteins involved in the degradation of lignocellulosic material, or other proteins, in a filamentous fungus host. 1. A method to genetically modify a filamentous fungus host for improved protein production , said method comprising:{'i': Trichoderma, Aspergillus, Fusarium, Neurospora, Talaromyces, Phanerochaete, Chrysosporium', 'Penicillium, 'genetically modifying a filamentous fungus host to overexpress with increased amount or activity, or to be deficient with reduced or lacking amount or activity, of one or more genes selected from the group consisting of genes tre77513 (SEQ ID NO:1), tre80291 (SEQ ID NO:2), tre41573 (SEQ ID NO:3), tre74765 (SEQ ID NO:4), and tre64608 (SEQ ID NO:5); or of the closest homologue of at least one of said genes in or ; or of a fragment or derivative of any of said genes or other nucleotide sequence hybridizing under stringent conditions to at least one of said genes or said homologues, said host being capable of increased or decreased production of cellulase, hemicellulase, other proteins involved in degradation of lignocellulosic material and/or other proteins as compared to the parental strain.'}2Trichoderma, Aspergillus, Fusarium, Neurospora, Talaromyces, Phanerochaete, ChrysosporiumPenicillium. The method according to claim 1 , wherein the filamentous fungus host is genetically modified to overexpress one or more genes selected from the group consisting of genes tre77513 (SEQ ID NO:1) claim 1 , tre80291 (SEQ ID NO:2) claim 1 , tre41573 (SEQ ID NO:3) claim 1 , ...

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Номер записи: 5

28-03-2013 дата публикации

Protozoan Glycosidases and Related Methods

Номер: US20130078678A1

Автор: Findley Seth D., Mormile Melanie, Stacey Gary

Принадлежит: The Curators of the University of Missouri

Nucleic acids encoding glycosidases useful for the hydrolysis of cellulose and hemicellulose obtained from ciliates residing in a bovine rumen are provided. Also provided recombinant nucleic acids encoding the glycosidases, transformed cells comprising the same and related methods of using the transformed cells and glycosidases to degrade cellulose and/or hemicellulose. 1. A recombinant nucleic acid comprising a heterologous promoter that is operably linked to a gene encoding a protein having at least 85% identity to SEQ ID NO: 6 and glycosidase activity.2. The recombinant nucleic acid of claim 1 , wherein nucleic acid is DNA.3. The recombinant nucleic acid of claim 2 , said promoter provides for expression of the glycosidase in a bacterial cell claim 2 , a yeast cell claim 2 , a plant cell claim 2 , a fungal cell claim 2 , an algal cell claim 2 , a protozoan cell claim 2 , or a mammalian cell.4. The recombinant nucleic acid of claim 1 , wherein said glycosidase comprises at least one GH5 domain.5. The recombinant nucleic acid of claim 1 , wherein said glycosidase activity comprises a xyloglucanase activity.6. The recombinant nucleic acid of claim 1 , wherein said protein has at least 90% claim 1 , 95% claim 1 , 98% claim 1 , 99% claim 1 , or 100% sequence identity to SEQ ID NO:6.7. A transformed cell comprising the recombinant nucleic acid of .8. The transformed cell of claim 7 , wherein said cell is a bacterial cell claim 7 , a yeast cell claim 7 , an algal cell claim 7 , a protozoan cell claim 7 , a plant cell claim 7 , a fungal cell claim 7 , or a mammalian cell.9. The transformed cell of claim 7 , wherein said promoter provides for constitutive and/or inducible expression of the protein in the cell.10. A method of making a glycosidase comprising the steps of:{'claim-ref': {'@idref': 'CLM-00007', 'claim 7'}, 'c. culturing the transformed cell of under conditions that provide for accumulation of the protein in the cell or in the cell culture medium; and,'}d. ...

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Номер записи: 6

28-03-2013 дата публикации

Polypeptides Having Cellobiohydrolase 1 Activity and Polynucleotides Encoding Same

Номер: US20130078679A1

Автор: Aubert Dominique, Clausen Ib Groth, Landvik Sara, Lange Lene, Schnorr Kirk Matthew, Wu Wenping

Принадлежит: NOVOZYMES A/S

The present invention relates to polypeptides having cellobiohydrolase I activity and polynucleotides having a nucleotide sequence which encodes for the polypeptides. The invention also relates to nucleic acid constructs, vectors, and host cells comprising the nucleic acid constructs as well as methods for producing and using the polypeptides. 129-. (canceled)30. An isolated polypeptide having cellobiohydrolase I activity , which has at least 80% identity with the sequence of amino acids 1 to 529 of SEQ ID NO:4.31. The polypeptide of claim 30 , which has at least 85% identity with amino acids 1 to 529 of SEQ ID NO:4.32. The polypeptide of claim 30 , which has at least 90% identity with amino acids 1 to 529 of SEQ ID NO:4.33. The polypeptide of claim 30 , which has at least 95% identity with amino acids 1 to 529 of SEQ ID NO:4.34. The polypeptide of claim 30 , which has at least 97% identity with amino acids 1 to 529 of SEQ ID NO:4.35. The polypeptide of claim 30 , which has at least 98% identity with amino acids 1 to 529 of SEQ ID NO:4.36. The polypeptide of claim 30 , which has at least 99% identity with amino acids 1 to 529 of SEQ ID NO:4.37. The polypeptide of claim 30 , comprising the sequence of amino acids 1 to 529 of SEQ ID NO:4.38. The polypeptide of claim 30 , which is a fragment of the sequence of amino acids 1 to 529 of SEQ ID NO:4.39. A detergent composition comprising a surfactant and the polypeptide of .40. A method for producing ethanol from biomass claim 30 , comprising{'claim-ref': {'@idref': 'CLM-00030', 'claim 30'}, '(a) contacting the biomass with the polypeptide of , an endo-1,4-beta-glucanase, and a beta-D-glucosidase to produce sugar; and'}(b) fermenting the sugar to produce ethanol. This application is a divisional of U.S. application Ser. No. 13/646,980 filed on Oct. 8, 2012, now pending, which is a divisional of U.S. application Ser. No. 13/483,389 filed on May 30, 2012, now pending, which is a divisional of U.S. application Ser. No. 12/818 ...

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Номер записи: 7

11-04-2013 дата публикации

Polypeptides Having Isoamylase Activity and Polynucleotides Encoding Same

Номер: US20130089897A1

Автор: Hoff Tine, Norman Barrie Edmund, Sjoeholm Carsten

Принадлежит: NOVOZYMES A/S

The present invention relates to isolated polypeptides having isoamylase activity derived from and isolated polynucleotides encoding the polypeptides. The invention also relates to nucleic acid constructs, vectors, and host cells comprising the polynucleotides as well as methods of producing and using the polypeptides. The invention also relates to the use of said polypeptide having isoamylase activity for producing glucose syrup, fructose syrup, maltose syrup or maltitol. 1. An isolated polypeptide having isoamylase activity , selected from the group consisting of:(a1) a polypeptide comprising an amino acid sequence having at least 93%, more preferably at least 94%, more preferably at least 95%, more preferably at least 96%, more preferably at least 97%, more preferably at least 98%, even more preferably at least 99% identity to the mature polypeptide of SEQ ID NO: 2;(a2) a polypeptide comprising an amino acid sequence having at least 94%, more preferably at least 95%, more preferably at least 96%, more preferably at least 97%, more preferably at least 98%, even more preferably at least 99% identity to the mature polypeptide of SEQ ID NO: 4;(a3) a polypeptide comprising an amino acid sequence having at least 93%, more preferably at least 94%, more preferably at least 95%, more preferably at least 96%, more preferably at least 97%, more preferably at least 98%, even more preferably at least 99% identity to the mature polypeptide of SEQ ID NO: 6;(a4) a polypeptide comprising an amino acid sequence having at least 90%, preferably at least 91%, more preferably at least 92%, more preferably at least 93%, more preferably at least 94%, more preferably at least 95%, more preferably at least 96%, more preferably at least 97%, more preferably at least 98%, even more preferably at least 99% identity to the mature polypeptide of SEQ ID NO: 8;(b) a polypeptide encoded by a polynucleotide that hybridizes under at least high stringency conditions with (i) the mature polypeptide ...

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Номер записи: 8

18-04-2013 дата публикации

BETA-GLUCOSIDASE VARIANT ENZYMES AND RELATED POLYNUCLEOTIDES

Номер: US20130095530A1

Автор: Cho Catherine M., Clark Louis, Postlethwaite Sally Rhiannon

Принадлежит: CODEXIS, INC.

The invention provides variants of the CelA β-glucosidase that have improve β-glucosidase activity, particularly improved thermoactivity, compared to the wild type enzyme. The invention further provides related polynucleotides, vectors, host cell, and methods for making and using the variants. 1. A method of converting a biomass substrate to a fermentable sugar , the method comprising contacting the biomass substrate with a β-glucosidase polypeptide variant wherein the β-glucosidase polypeptide variant comprises:{'i': 'Azospirillum irakense', '(a) an amino acid sequence that is at least about 70% identical to wild type β-glucosidase (SEQ ID NO:4) and comprising at least one substitution or deletion of an amino acid residue at a position selected from the group consisting of T2, A3, I4, A5, Q6, E7, G8, A9, A10, P11, A12, A13, I14, L15, P17, E18, K19, W20, P21, P23, A24, T25, Q26, I29, D30, E34, K35, A39, L41, K42, Q43, L44, E47, V46, G51, Q52, V53, G56, G59, T60, I61, E64, L66, R67, K68, P70, S73, N79, N83, G84, D85, R87, A88, P89, K91, E92, A97, A98, L105, K107, P109, G110, H111, T112, P113, I114, F118, I120, G127, N128, I134, F135, L141, A143, T144, H145, D146, P147, E148, L150, R151, R152, I153, G154, E155, A158, V159, M161, A162, A163, G165, I166, W168, T169, A173, V177, D180, G188, S190, I195, A197, A198, A201, A202, I203, V204, E205, G206, V207, F211, G212, S213, K214, D215, F216, M217, A218, P219, G220, I222, S225, A226, F229, G233, D236, Q237, G238, D243, R245, I246, S247, E248, E250, R253, N256, A257, D264, A272, F274, Q278, I280, H282, H285, Q287, G295, M297, G298, F299, N300, V304, D311, Q312, P314, G315, F319, N320, T323, S324, I326, M331, A335, K339, Q340, Y342, E343, T345, A347, V349, K350, V351, T353, I354, M356, A357, R358, D360, A362, I366, V369, V371, L372, A373, E377, K378, P379, P381, K382, D383, G386, L387, L390, S395, P396, A400, G402, R403, K408, K417, S423, A426, D433, Q418, T419, R425, A426, D436, G439, K440, G444, T452, G453, R455, D456, ...

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Номер записи: 9

18-04-2013 дата публикации

POLYPEPTIDE HAVING BETA-GLUCOSIDASE ACTIVITY AND USES THEREOF

Номер: US20130095531A1

Автор: Damveld Robbertus Antonius, De Jong Rene Marcel, Heijne Wilbert Herman Marie, SCHOONEVELD-BERGMANS Margot Elisabeth Francoise

Принадлежит: DSM IP ASSETS B.V.

The invention relates to a polypeptide comprising the amino acid sequence set out in SEQ ID NO: 2 or an amino acid sequence encoded by the nucleotide sequence of SEQ ID NO: 1, or a variant polypeptide or variant polynucleotide thereof, wherein the variant polypeptide has at least 70% sequence identity with the sequence set out in SEQ ID NO: 2 or the variant polynucleotide encodes a polypeptide that has at least 70% sequence identity with the sequence set out in SEQ ID NO: 2. The invention features the full length coding sequence of the novel gene as well as the amino acid sequence of the full-length functional polypeptide and functional equivalents of the gene or the amino acid sequence. The invention also relates to methods for using the polypeptide in industrial processes. Also included in the invention are cells transformed with a polynucleotide according to the invention suitable for producing these proteins. 1. A polypeptide which comprises the amino acid sequence set out in SEQ ID NO: 2 or an amino acid sequence encoded by the nucleotide sequence of SEQ ID NO:1 , or a variant polypeptide or variant polynucleotide thereof , wherein the variant polypeptide has at least 70% sequence identity with the sequence set out in SEQ ID NO: 2 or the variant polynucleotide encodes a polypeptide that has at least 70% sequence identity with the sequence set out in SEQ ID NO: 2.2. A polypeptide according to claim 1 , wherein the polypeptide has beta-glucosidase activity.3. A polynucleotide which comprises:(a) the nucleotide sequence set out in SEQ ID NO: 1 ; or(b) a nucleotide sequence which hybridizes selectively with a polynucleotide being a reverse complement of SEQ ID NO: 1; or(c) a nucleotide sequence having at least 75% sequence identity with the nucleotide sequence of SEQ ID NO: 1; or(d) a fragment which is at least about 100 nucleotides in length of a nucleotide sequence as defined in (a), (b) or (c) which is at least about 100 nucleotides in length; or(e) a sequence ...

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Номер записи: 10

18-04-2013 дата публикации

Polypeptide having or assisting in carbohydrate material degrading activity and uses thereof

Номер: US20130095553A1

Автор: Alrik Pieter Los, Margot Elisabeth Francoise Schooneveld-Bergmans, Wilbert Herman Marie Heijne

Принадлежит: DSM IP ASSETS BV

The invention relates to a polypeptide which comprises the amino acid sequence set out in SEQ ID NO: 2 or an amino acid sequence encoded by the nucleotide sequence of SEQ ID NO: 1, or a variant polypeptide or variant polynucleotide thereof, wherein the variant polypeptide has at least 76% sequence identity with the sequence set out in SEQ ID NO: 2 or the variant polynucleotide encodes a polypeptide that has at least 76% sequence identity with the sequence set out in SEQ ID NO: 2. The invention features the full length coding sequence of the novel gene as well as the amino acid sequence of the full-length functional polypeptide and functional equivalents of the gene or the amino acid sequence. The invention also relates to methods for using the polypeptide in industrial processes. Also included in the invention are cells transformed with a polynucleotide according to the invention suitable for producing these proteins.

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Номер записи: 11

18-04-2013 дата публикации

MODIFIED FAMILY 5 CELLULASES AND USES THEREOF

Номер: US20130095554A1

Автор: Hill Christopher M.D., Masri Nabil, Mortimer Sandra, St-Pierre Patrick

Принадлежит: IOGEN BIO-PRODUCTS CORPORATION

The present invention relates to a modified Family 5 cellulase comprising a substitution of an amino acid at position 363 with a non-native alanine, serine or threonine, said position determined from alignment of the modified Family 5 cellulase with amino acids 71-397 of a Cel5A amino acid sequence as set forth in SEQ ID NO:1 and enzyme mixtures comprising same. Additionally provided is a genetic construct comprising a nucleic acid sequence encoding the modified Family 5 cellulase and a genetically modified microbe comprising the genetic construct. The invention also provides a process for producing the modified Family 5 cellulase. 1. A modified Family 5 cellulase comprising a substitution of an amino acid at position 363 with a non-native alanine , or serine or threonine , said position determined from alignment of the modified Family 5 cellulase amino acid sequence with amino acids 71 to 397 of SEQ ID NO:1 , wherein the modified Family 5 cellulase contains no more than 20 other amino acid substitutions relative to a corresponding wild-type Family 5 cellulase , and wherein the modified Family 5 cellulase is derived from a fungal parental Family 5 cellulase which does not naturally possess an alanine , serine , or threonine at position 363.2. The modified Family 5 cellulase of claim 1 , wherein said modified Family 5 cellulase exhibits an increase in specific activity of at least about 1.2 fold relative to a parental Family 5 cellulase or a corresponding wild-type Family 5 cellulase.3Trichoderma, Hypocrea, Penicillium, Botryotinia, Macrophomina, Aspergillus, Orpinomyces, Pestalotiopsis, MyceliopthoraChrysosporium.. The modified Family 5 cellulase of claim 1 , wherein said fungal parental Family 5 cellulase is a Family 5 cellulase from a species of claim 1 , or4. The modified Family 5 cellulase of claim 1 , wherein the substituted amino acid at position 363 is an alanine.5. An enzyme mixture comprising the modified Family 5 cellulase of .6. A process for bio-stoning ...

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Номер записи: 12

25-04-2013 дата публикации

POLYPEPTIDE HAVING BETA-GLUCOSIDASE ACTIVITY AND USES THEREOF

Номер: US20130104264A1

Автор: Damveld Robbertus Antonius, De Jong Rene Marcel, Heijne Wilbert Herman Marie, Schoonneveld-Bergmans Margot Elisabeth Francoise

Принадлежит: DSM IP ASSETS B.V.

The invention relates to a polypeptide comprising the amino acid sequence set out in SEQ ID NO: 2 or an amino acid sequence encoded by the nucleotide sequence of SEQ ID NO: 1, or a variant polypeptide or variant polynucleotide thereof, wherein the variant polypeptide has at least 96% sequence identity with the sequence set out in SEQ ID NO: 2 or the variant polynucleotide encodes a polypeptide that has at least 96% sequence identity with the sequence set out in SEQ ID NO: 2. The invention features the full length coding sequence of the novel gene as well as the amino acid sequence of the full-length functional polypeptide and functional equivalents of the gene or the amino acid sequence. The invention also relates to methods for using the polypeptide in industrial processes. Also included in the invention are cells transformed with a polynucleotide according to the invention suitable for producing these proteins. 1. A polypeptide which comprises the amino acid sequence set out in SEQ ID NO: 2 or an amino acid sequence encoded by the nucleotide sequence of SEQ ID NO:1 , or a variant polypeptide or variant polynucleotide thereof , wherein the variant polypeptide has at least 96% sequence identity with the sequence set out in SEQ ID NO: 2 or the variant polynucleotide encodes a polypeptide that has at least 96% sequence identity with the sequence set out in SEQ ID NO: 2.2. The polypeptide according to claim 1 , wherein said polypeptide has beta-glucosidase activity.3. A polynucleotide which comprises:(a) the nucleotide sequence set out in SEQ ID NO: 1; or(b) a nucleotide sequence which hybridizes selectively with a polynucleotide being the reverse complement of SEQ ID NO: 1; or(c) a nucleotide sequence having at least 83% sequence identity with the nucleotide sequence of SEQ ID NO: 1; or(d) a fragment which is at least about 100 nucleotides in length of a nucleotide sequence as defined in (a), (b) or (c) which is at least about 100 nucleotides in length; or(e) a ...

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Номер записи: 13

16-05-2013 дата публикации

OPTIMIZED CELLULASE ENZYMES

Номер: US20130123115A1

Автор: Brück Thomas, Claren Jörg, Gerlach Jochen, Kettling Ulrich, Kohl Andreas, Koltermann Andre, Pieck Jan Carsten, Rarbach Markus, Reisinger Christoph, Röcher Lutz, Schlosser Dominik, Unterstrasser Isabel

Принадлежит: SUD-CHEMIE IP GMBH & CO. KG

The invention discloses cellulase enzymes with optimized properties for processing of cellulose- and lignocellulose-containing substrates. In particular, cellobiohydrolase enzymes with preferred characteristics are disclosed. The present invention provides fusion, insertion, deletion and/or substitution variants of such enzymes. Enzyme variants have enhanced thermostability, proteolytic stability, specific activity and/or stability at extreme pH. Nucleic acid molecules encoding said enzymes, a composition comprising said enzymes, a method for preparation, and the use for cellulose processing and/or for the production of biofuels are disclosed. 1. A polypeptide having cellobiohydrolase activity , wherein the polypeptide comprises an amino acid sequence having at least 60% sequence identity to SEQ ID NO: 5 over a sequence length of 437 positions , and wherein the polypeptide maintains 50% of its maximum substrate conversion capacity when the conversion is done for 60 minutes at a temperature of 62° C. or higher.2. The polypeptide according to claim 1 , wherein the polypeptide comprises an amino acid sequence having at least 80% sequence identity to SEQ ID NO:5 over a sequence length of 437 amino acid residues.3. The polypeptide according to claim 1 , wherein one or more of the amino acid residues of the sequence defined by SEQ ID NO: 5 are modified by substitution or deletion at one or more positions preferably selected fromQ1, Q2, G4, A6, T7, A8, N10, P12, T15, A21, G23, S24, T26, T27, Q28, N29, G30, A31, V32, N37, W40, V41, G46, Y47, T48, N49, C50, T52, N54, D57, T59, Y60, D64, E65, A68, Q69, A72, V84, S86, S89, S90, K92, S99, Q109, D110, D111, I116, F117, K118, L119, L120, D129, V130, G139, A145, M146, V152, K154, Y155, N157, N158, K159, K163, G167, Q172, F179, I180, D181, E183, E187, G188, Q190, S192, S193, N194, I200, D202, H203, D211, V212, A221, P224, D228, T229, G231, T233, M234, S236, T243, Y244, S245, N246, D247, G251, F260, G266, K275, I276, I277, T280, ...

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Номер записи: 14

23-05-2013 дата публикации

Polypeptides Having Beta-Glucosidase Activity, Beta-Xylosidase Activity, or Beta-Glucosidase and Beta-Xylosidase Activity and Polynucleotides Encoding Same

Номер: US20130130325A1

Автор: Morant Marc Dominique

Принадлежит:

The present invention relates to isolated polypeptides having beta-glucosidase activity, beta-xylosidase activity, or beta-glucosidase and beta-xylosidase activity and isolated polynucleotides encoding the polypeptides. The invention also relates to nucleic acid constructs, vectors, and host cells comprising the polynucleotides as well as methods of producing and using the polypeptides. 1. An isolated polypeptide having beta-glucosidase activity , beta-xylosidase activity , or beta-glucosidase and beta-xylosidase activity , selected from the group consisting of:(a) a polypeptide having at least 76% sequence identity to the mature polypeptide of SEQ ID NO: 2, SEQ ID NO: 4, SEQ ID NO: 6, SEQ ID NO: 8, SEQ ID NO: 10, or SEQ ID NO: 12;(b) a polypeptide encoded by a polynucleotide that hybridizes under at least midium stringency conditions with (i) the mature polypeptide coding sequence of SEQ ID NO: 1 or the cDNA sequence thereof, the mature polypeptide coding sequence of SEQ ID NO: 3 or the cDNA sequence thereof, the mature polypeptide coding sequence of SEQ ID NO: 5 or the cDNA sequence thereof, the mature polypeptide coding sequence of SEQ ID NO: 7 or the cDNA sequence thereof, the mature polypeptide coding sequence of SEQ ID NO: 9 or the cDNA sequence thereof, or the mature polypeptide coding sequence of SEQ ID NO: 11 or the cDNA sequence thereof, or (ii) the full-length complement of (i);(c) a polypeptide encoded by a polynucleotide having at least 76% sequence identity to the mature polypeptide coding sequence of SEQ ID NO: 1 or the cDNA sequence thereof, the mature polypeptide coding sequence of SEQ ID NO: 3 or the cDNA sequence thereof, the mature polypeptide coding sequence of SEQ ID NO: 5 or the cDNA sequence thereof, the mature polypeptide coding sequence of SEQ ID NO: 7 or the cDNA sequence thereof, the mature polypeptide coding sequence of SEQ ID NO: 9 or the cDNA sequence thereof, or the mature polypeptide coding sequence of SEQ ID NO: 11 or the cDNA ...

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Номер записи: 15

23-05-2013 дата публикации

Polypeptides Having Beta-Glucosidase Activity, Beta-Xylosidase Activity, or Beta-Glucosidase and Beta-Xylosidase Activity and Polynucleotides Encoding Same

Номер: US20130130326A1

Автор: Morant Marc Dominique

Принадлежит:

The present invention relates to isolated polypeptides having beta-glucosidase activity, beta-xylosidase activity, or beta-glucosidase and beta-xylosidase activity and isolated polynucleotides encoding the polypeptides. The invention also relates to nucleic acid constructs, vectors, and host cells comprising the polynucleotides as well as methods of producing and using the polypeptides. 1. An isolated polypeptide having beta-glucosidase activity , beta-xylosidase activity , or beta-glucosidase and beta-xylosidase activity , selected from the group consisting of:(a) a polypeptide having at least 80% sequence identity to the mature polypeptide of SEQ ID NO: 2, or the mature polypeptide of SEQ ID NO: 4;(b) a polypeptide encoded by a polynucleotide that hybridizes under at least high stringency conditions with (i) the mature polypeptide coding sequence of SEQ ID NO: 1 or the cDNA sequence thereof, or the mature polypeptide coding sequence of SEQ ID NO: 3 or the cDNA sequence thereof, or (ii) the full-length complement of (i);(c) a polypeptide encoded by a polynucleotide having at least 80% sequence identity to the mature polypeptide coding sequence of SEQ ID NO: 1 or the cDNA sequence thereof, or the mature polypeptide coding sequence of SEQ ID NO: 3 or the cDNA sequence thereof;(d) a variant of the mature polypeptide of SEQ ID NO: 2, SEQ ID NO: 4 comprising a substitution, deletion, and/or insertion at one or more (e.g., several) positions; and(e) a fragment of the polypeptide of (a), (b), (c), or (d) that has beta-glucosidase activity, beta-xylosidase activity, or beta-glucosidase and beta-xylosidase activity.2. An isolated polynucleotide encoding the polypeptide of .3. A recombinant host cell comprising the polynucleotide of operably linked to one or more control sequences that direct the production of the polypeptide.4. A method of producing the polypeptide of claim 1 , comprising:(a) cultivating a cell, which in its wild-type form produces the polypeptide, under ...

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Номер записи: 16

30-05-2013 дата публикации

Protein Fusion Constructs Possessing Thrombolytic and Anticoagulant Properties

Номер: US20130136731A1

Автор: Maheshwari Neeraj, SAHNI Girish

Принадлежит: COUNCIL OF SCIENTIFIC & INDUSTRIAL RESEARCH

The present invention discloses novel hybrid proteins that have both plasminogen activator and anti-thrombotic properties, including clot specific action, that renders these as highly advantageous for the treatment of circulatory disorders involving fibrin clot formation due to underlying tissue damage in the blood vessels leading to myocardial infarction, strokes etc. Also disclosed are new proteins, and methods of obtaining the same, that help to dissolve blood clots by activating plasminogen in a plasmin or thrombin dependent manner and also inhibit both the activity and generation of thrombin through the intrinsic pathway of blood coagulation. 1. A chimeric protein construct comprising the 4 , 5 , and 6 epidermal growth factor-like domains (EGF 4 ,5 ,6) of thrombomodulin fused to a thrombolytic protein selected from the group consisting of a streptokinase , a tissue plasminogen activator , a staphylokinase , a urokinase , and derivatives and analogs thereof.2. The chimeric protein construct according to claim 1 , where said thrombomodulin EGF 4 claim 1 ,5 claim 1 ,6 domains are fused to said thrombolytic protein claim 1 , or derivative or analog thereof at the N-terminus claim 1 , C-terminus claim 1 , or both N- and C-termini of said thrombolytic protein claim 1 , or derivative or analog thereof.3. The chimeric protein construct according to claim 1 , wherein said thrombolytic protein comprises a streptokinase with one or more amino acid substitutions claim 1 , insertions claim 1 , deletions claim 1 , or truncations claim 1 , and wherein the construct possesses plasminogen activation claim 1 , thrombin inhibition claim 1 , and anticoagulant protein C pathway activation activity.4. The chimeric protein construct according to claim 1 , where the thrombomodulin EGF 4 claim 1 ,5 claim 1 ,6 domains are fused between the alpha and beta or beta and gamma domains of said streptokinase or between the alpha and beta or beta and gamma domains of a streptokinase derivative ...

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Номер записи: 17

20-06-2013 дата публикации

Compositions Comprising A Polypeptide Having Cellulolytic Enhancing Activity And A Dioxy Compound And Uses Thereof

Номер: US20130157317A1

Автор: Quinlan Jason, Sweeney Matthew, Xu Feng

Принадлежит: NOVOZYMES, INC.

The present invention relates to compositions comprising: a polypeptide having cellulolytic enhancing activity and a dioxy compound. The present invention also relates to methods of using the compositions. 1. A composition comprising: (a) a polypeptide having cellulolytic enhancing activity and (b) a dioxy compound , wherein the combination of the polypeptide having cellulolytic enhancing activity and the dioxy compound enhances hydrolysis of a cellulosic material by a cellulolytic enzyme.9. The composition of claim 2 , wherein the dioxy compound is selected from the group consisting of: (I-1): pyrocatechol or catechol; (I-2): caffeic acid; (I-3): 3 claim 2 ,4-dihydroxybenzoic acid; (I-4): 4-tert-butyl-5-methoxy-1 claim 2 ,2-benzenediol; (I-5): pyrogallol; (I-6): gallic acid; (I-7): Methyl-3 claim 2 ,4 claim 2 ,5-trihydroxybenzoate; (I-8): 2 claim 2 ,3 claim 2 ,4-trihydroxybenzophenone; (I-9): 2 claim 2 ,6-dimethoxyphenol; (I-10): sinapinic acid; (I-12): 3 claim 2 ,5-dihydroxybenzoic acid; (I-12): 4-chloro-1 claim 2 ,2-benzenediol; (I-13): 4-nitro-1 claim 2 ,2-benzenediol; (I-14): tannic acid; (I-15): ethyl gallate; (I-16): methyl glycolate; (I-17): dihydroxyfumaric acid; (I-18): 2-butyne-1 claim 2 ,4-diol; (I-19): croconic acid; (I-20): 1 claim 2 ,3-propanediol; (I-21): tartaric acid; (I-22): 2 claim 2 ,4-pentanediol; (I-23): 3-ethyoxy-1 claim 2 ,2-propanediol; (I-24): 2 claim 2 ,4 claim 2 ,4′-trihydroxybenzophenone; (I-25): cis-2-butene-1 claim 2 ,4-diol; (I-26): 3 claim 2 ,4-dihydroxy-3-cyclobutene-1 claim 2 ,2-dione; (I-27): dihydroxyacetone; (I-28): acrolein acetal; (I-29): methyl-4-hydroxybenzoate; (I-30): 4-hydroxybenzoic acid; (I-31): methyl-3 claim 2 ,5-dimethoxy-4-hydroxybenzoate; and (I-32): and pyrocatechol violet; or a salt or solvate thereof.10. The composition of claim 1 , which further comprises (c) one or more enzymes selected from the group consisting of a cellulase claim 1 , a hemicellulase claim 1 , an esterase claim 1 , an expansin claim 1 , a ...

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Номер записи: 18

11-07-2013 дата публикации

BGL7 Beta-Glucosidase and Nucleic Acids Encoding the Same

Номер: US20130177965A1

Автор: Dunn-Coleman Nigel, Ward Michael

Принадлежит: DANISCO US INC.

The present invention provides a novel β-glucosidase nucleic acid sequence, designated bgl7, and the corresponding BGL7 amino acid sequence. The invention also provides expression vectors and host cells comprising a nucleic acid sequence encoding BGL7, recombinant BGL7 proteins and methods for producing the same. 117-. (canceled)18. A substantially purified BGL7 polypeptide with the biological activity of a β-glucosidase , comprising a sequence selected from the group consisting of:(a) an amino acid sequence having at least 85% sequence identity to the amino acid sequence of SEQ ID NO:2;(b) an amino acid sequence having at least 90% sequence identity to the amino acid sequence of SEQ ID NO:2;(c) an amino acid sequence having at least 95% sequence identity to the amino acid sequence of SEQ ID NO:2;(d) an amino acid sequence of SEQ ID NO:2; and(e) a substantially purified biologically active fragment of the amino acid sequence of SEQ ID NO:2.1924-. (canceled)25. A detergent composition , said composition comprising a polypeptide selected from the group consisting of:(a) an amino acid sequence having at least 85% sequence identity to the amino acid sequence of SEQ ID NO:2;(b) an amino acid sequence having at least 90% sequence identity to the amino acid sequence of SEQ ID NO:2;(c) an amino acid sequence having at least 95% sequence identity to the amino acid sequence of SEQ ID NO:2;(d) an amino acid sequence of SEQ ID NO:2; and(e) a substantially purified biologically active fragment of the amino acid sequence of SEQ ID NO:2.2638-. (canceled)39. The BGL7 polypeptide of claim 18 , wherein said fragment is about 50-100 amino acids in length.40. The BGL7 polypeptide of claim 18 , wherein said fragment is about 50-200 amino acids in length.41. The BGL7 polypeptide of claim 18 , wherein said fragment is about 100-200 amino acids in length.42. The BGL7 polypeptide of claim 18 , wherein said fragment corresponds to the N-terminal domain of BGL7 or the C-terminal domain of ...

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Номер записи: 19

18-07-2013 дата публикации

Compositions Comprising A Polypeptide Having Cellulolytic Enhancing Activity And A Nitrogen-Contaning Compound And Uses Thereof

Номер: US20130183722A1

Автор: Quinlan Jason, Sweeney Matthew, Xu Feng

Принадлежит: NOVOZYMES, INC.

The present invention relates to compositions comprising: a polypeptide having cellulolytic enhancing activity and a nitrogen-containing compound. The present invention also relates to methods of using the compositions. 1. A composition comprising: (a) a polypeptide having cellulolytic enhancing activity and (b) a nitrogen-containing compound , wherein the combination of the polypeptide having cellulolytic enhancing activity and the nitrogen-containing compound enhances hydrolysis of a cellulosic material by a cellulolytic enzyme.2. The composition of claim 1 , wherein the nitrogen-containing compound comprises an amine claim 1 , imine claim 1 , hydroxylamine claim 1 , or nitroxide moiety.5. The composition of claim 1 , wherein the nitrogen-containing compound is selected from the group consisting of: (I-1): acetone oxime; (1-2): violuric acid; (1-3): pyridine-2-aldoxime; (II-1): 2-aminophenol; (II-2): 1 claim 1 ,2-benzenediamine; (II-3):2 claim 1 ,2 claim 1 ,6 claim 1 ,6-tetramethyl-1-piperidinyloxy; (II-4): 5 claim 1 ,6 claim 1 ,7 claim 1 ,8-tetrahydrobiopterin; (II-5): 6 claim 1 ,7-dimethyl-5 claim 1 ,6 claim 1 ,7 claim 1 ,8-tetrahydropterine; and (II-6): maleamic acid; or a salt or solvate thereof.6. The composition of claim 1 , which further comprises (c) one or more enzymes selected from the group consisting of a cellulase claim 1 , a hemicellulase claim 1 , an esterase claim 1 , an expansin claim 1 , a laccase claim 1 , a ligninolytic enzyme claim 1 , a pectinase claim 1 , a peroxidase claim 1 , a protease claim 1 , and a swollenin.7. A method for degrading or converting a cellulosic material claim 1 , comprising: treating the cellulosic material with an enzyme composition in the presence of a polypeptide having cellulolytic enhancing activity and a nitrogen-containing compound claim 1 , wherein the combination of the polypeptide having cellulolytic enhancing activity and the nitrogen-containing compound enhances hydrolysis of the cellulosic material by the ...

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Номер записи: 20

25-07-2013 дата публикации

Protease Variants

Номер: US20130189732A1

Автор: Andersen Carsten, Christensen Lars Lehmann Hylling, De Maria Leonardo, Lassen Soren Flensted, Ostergaard Peter Rahbek

Принадлежит: NOVOZYMES A/S

The invention relates to a novel 3D structure encoding a as well as to variants of parent protease homologous to proteases, preferably of improved thermostability and/or with an amended temperature activity profile. The invention also relates to DNA sequences encoding such variants, their production in a recombinant host cell, as well as methods of using the variants, in particular within the field of animal feed and detergents. The invention furthermore relates to methods of generating and preparing protease variants of amended properties. 134-. (canceled)35. A variant of a parent protease , comprising a substitution in at least one position of at least one region selected from the group of regions consisting of:6-18; 22-28; 32-39; 42-58; 62-63; 66-76; 78-100; 103-106; 111-114; 118-131; 134-136; 139-141; 144-151; 155-156; 160-176; 179-181; and 184-188; (a) the variant has protease activity; and', '(b) each position corresponds to a position of amino acids 1 to 188 of SEQ ID NO: 2; and', '(c) the variant has a percentage of identity to amino acids 1 to 188 of SEQ ID NO: 2 of at least 60%., 'wherein'}36. An animal feed additive comprising at least one protease variant of claim 35 , and(a) at least one fat soluble vitamin;(b) at least one water soluble vitamin; and/or(c) at least one trace mineral.37. An animal feed composition having a crude protein content of 50 to 800 g/kg and comprising the protease variant of .38. A method for improving the nutritional value of an animal feed claim 35 , comprising adding a protease variant of to the feed.39. A method for the treatment of proteins claim 35 , comprising the step of adding the protease variant of to at least one protein or protein source. This application is a divisional of U.S. application Ser. No. 12/984,826 filed on Jan. 5, 2011, now allowed, which is a divisional of U.S. application Ser. No. 10/574,554 filed on Apr. 3, 2006, now U.S. Pat. No. 7,892,808, which is a 35 U.S.C. 371 national application of PCT/DK2004 ...

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Номер записи: 21

25-07-2013 дата публикации

METHOD FOR PRODUCING GLUCOSIDASE, ENZYME COMPOSITION, AND METHOD FOR HYDROLYZING BIOMASS

Номер: US20130189761A1

Автор: Ishikawa Kazuhiko, Kado Yuji, Kurihara Hiroyuki, Wada Yasunobu, Watanabe Shiomi, Yamada Katsushige

Принадлежит: Toray Industries, Inc.

A method for producing a mutant glucosidase includes introducing DNA encoding a secretion signal sequence and DNA encoding Asn-X-Ser or Asn-X-Thr into DNA encoding a glucosidase derived from a thermophile, and introducing the resulting DNA into a eukaryotic microorganism and expressing it as a secretory protein. An enzyme composition contains the mutant glucosidase. 1. A method of producing a mutant glucosidase derived from a thermophile selectively attached thereto a sugar chain and having a glucosidase activity , comprising:(i) preparing DNA encoding a mutant glucosidase derived from a thermophile by introducing a DNA sequence encoding Asn-X-Ser or Asn-X-Thr (wherein, X is any amino acid except proline) into DNA encoding a glucosidase derived from a thermophile originally devoid of a glycosylation sequence and adding a DNA sequence encoding a secretion signal sequence to the DNA encoding a mutant glucosidase,(ii) introducing the DNA encoding a mutant glucosidase to which the DNA sequence encoding the secretion signal sequence has been added into an eukaryotic microorganism so that a mutant glucosidase encoded by the DNA of the mutant glucosidase is expressed as a secretory protein, and(iii) isolating and purifying the mutant glucosidase thus expressed as a secretory protein.2. The method according to claim 1 , wherein the sugar chain is a high mannose type sugar chain.3SulfolobusThermoplasmaCaldirivgaThermosphaeraPyrococcusPicrophilusCaldivirgaFervidobacterium.. The method according to claim 1 , wherein the glucosidase derived from a thermophile is a glucosidase derived from a thermophile selected from the group consisting of genus claim 1 , genus claim 1 , genus claim 1 , genus claim 1 , genus claim 1 , genus claim 1 , genus claim 1 , and genus5Pichia pastoris.. The method according to claim 1 , wherein the eukaryotic microorganism is6. The method according to claim 1 , wherein the secretion signal sequence is an α factor secretion signal sequence.7. The method ...

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Номер записи: 22

01-08-2013 дата публикации

Polypeptides Having Cellobiohydrolase Activity And Polynucleotides Encoding Same

Номер: US20130198910A1

Автор: Spodsberg Nikolaj

Принадлежит:

The present invention relates to isolated polypeptides having cellobiohydrolase activity and isolated polynucleotides encoding the polypeptides. The invention also relates to nucleic acid constructs, vectors, and host cells comprising the polynucleotides as well as methods of producing and using the polypeptides. 1. An isolated polypeptide having cellobiohydrolase activity , selected from the group consisting of:(a) a polypeptide having at least 85% sequence identity to the mature polypeptide of SEQ ID NO: 2;(b) a polypeptide encoded by a polynucleotide that hybridizes under at least high stringency conditions with (i) the mature polypeptide coding sequence of SEQ ID NO: 1, (ii) the cDNA thereof, or (iii) the full-length complement of (i) or (ii);(c) a polypeptide encoded by a polynucleotide having at least 85% sequence identity to the mature polypeptide coding sequence of SEQ ID NO: 1, or the cDNA sequence thereof;and(d) a fragment of the polypeptide of (a), (b), (c), or (d) that has cellobiohydrolase activity.2. An isolated polynucleotide encoding the polypeptide of .3. A recombinant host cell comprising the polynucleotide of operably linked to one or more control sequences that direct the production of the polypeptide.4. A method of producing the polypeptide of claim 1 , comprising:(a) cultivating a cell, which in its wild-type form produces the polypeptide, under conditions conducive for production of the polypeptide; and(b) recovering the polypeptide.5. A method of producing a polypeptide having cellobiohydrolase activity claim 1 , comprising:{'claim-ref': {'@idref': 'CLM-00003', 'claim 3'}, '(a) cultivating the host cell of under conditions conducive for production of the polypeptide; and'}(b) recovering the polypeptide.6. A transgenic plant claim 1 , plant part or plant cell transformed with a polynucleotide encoding the polypeptide of .7. A method of producing a polypeptide having cellobiohydrolase activity claim 1 , comprising:{'claim-ref': {'@idref': 'CLM- ...

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Номер записи: 23

08-08-2013 дата публикации

VARIANT CBH I POLYPEPTIDES

Номер: US20130203128A1

Автор: Healey Shaun, LUGINBUHL PETER, Lyon Chris S., Poland John, Stege Justin T., Varvak Alexander

Принадлежит: BP Corporation North America Inc,

In alternative embodiments, the invention provides polypeptides having a lignocellulolytic (lignocellulosic) activity, e.g., a ligninolytic and cellulolytic activity, including, e.g., a glycosyl hydrolase, a cellulase, an endoglucanase, a cellobiohydrolase (cbhl) (e.g., an exo-cellobiohydrolase, e.g., having an “exo” activity that can processively release cellobiose units β-1,4 glucose-glucose disaccharide), a beta-glucosidase, a xylanase, a mannanse, a xylosidase (e.g., a (β-xylosidase) and/or an arabinofuranosidase activity, polynucleotides encoding these polypeptides, and methods of making and using these polynucleotides and polypeptides. In one embodiment, the invention provides thermostable and thermotolerant forms of polypeptides of the invention. The polypeptides and nucleic acids of the invention are used in a variety of pharmaceutical, agricultural and industrial contexts; for example, as enzymes for the bioconversion of a biomass, e.g., lignocellulosic residues, into fermentable sugars, where in one aspect these sugars are used as a chemical feedstock for the production of ethanol and fuels, e.g., biofuels, e.g., synthetic liquid or gas fuels, including ethanol, methanol and the like. 1. A polypeptide comprising the amino acid sequence of a variant cellobiohydrolase I (“CBH I”) catalytic domain , said variant CBH I catalytic domain having at least 90% sequence identity to a reference catalytic domain corresponding to amino acid positions 26-455 of SEQ ID NO:134 , and which comprises one or more amino acid substitutions that result in increased activity or improved thermotolerance as compared to the reference catalytic domain.2. The polypeptide of claim 1 , which has one or more substitutions that result in increased activity as compared to the reference catalytic domain.3. The polypeptide of claim 2 , which has one or more of the following substitutions or combinations of substitutions: (a) N222H; (b) N222E; (c) S217K; (d) L225Y; (e) L225V; (f) D87L; (g) ...

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Номер записи: 24

15-08-2013 дата публикации

METHOD FOR PRODUCING CELLULOLYTIC AND/OR HEMICELLULOLYTIC ENZYMES

Номер: US20130210119A1

Автор: Ben Chaabane Fadhel, Monot Frederic

Принадлежит: IFP ENERGIES NOUVELLES

The process for the production of cellulolytic and/or hemicellulolytic enzymes by a cellulolytic and/or hemicellulolytic microorganism according to the present invention comprises at least one phase for growth in the presence of a source of carbon and at least one phase for production in the presence of an inducing substrate, in which said inducing substrate is a mixture comprising 40% to 65% by weight of glucose or cellulosic hydrolysates, 21% to 25% by weight of lactose and 10% to 39% by weight of xylose or a solution of a lignocellulosic hemicellulosic hydrolysate, the sum of these three constituents being equal to 100%. 2Trichoderma reesei. A process according to claim 1 , in which the microorganism belongs to the species and is deleted for catabolic repression by glucose.3. A process according to claim 1 , in which the inducing substrate is supplied in solution claim 1 , the concentration of inducing substrate in the supply solution used during the production phase being 350 to 600 g/L.4. A process according to claim 3 , in which the concentration is in the range 450 to 550 g/L.5. A process according to claim 1 , in which the mixture constituting the inducing substrate comprises 50% to 65% by weight of glucose or cellulosic hydrolysates claim 1 , 22% to 24% by weight of lactose and 15% to 25% by weight of xylose or a solution of hemicellulosic hydrolysates claim 1 , the sum of the constituents being equal to 100%.6. A process according to claim 5 , in which the inducing substrate is a mixture constituted by 60% by weight of glucose or cellulosic hydrolysates claim 5 , 23% by weight of lactose and 17% by weight of xylose or hemicellulosic hydrolysates.7. A process according to claim 1 , in which the carbonaceous substrate used during the growth phase is selected from glucose claim 1 , xylose claim 1 , lactose claim 1 , residues obtained after ethanolic fermentation of monomeric sugars of the enzymatic hydrolysates of cellulosic biomass and/or an unrefined ...

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Номер записи: 25

22-08-2013 дата публикации

POLYPEPTIDE FOR INHIBITING METASTASIS, USES THEREOF, AND PHARMACEUTICAL COMPOSITIONS CONTAINING THE SAME

Номер: US20130216604A1

Автор: CHEN CHIEN-SHENG, CHEN Hung-Chi, Cheng Chin-Yun, Lin Yu-Chuan

Принадлежит: NATIONAL CHENG KUNG UNIVERSITY

A polypeptide for inhibiting, treating or diagnosing metastasis and an use thereof are disclosed, wherein the polypeptide is a polypeptide, a derivative polypeptide, or a mutated polypeptide of a fibronectin-binding domain of dipeptidyl peptidase IV. In addition, a pharmaceutical composition treating or diagnosing metastasis is also disclosed, which comprises the aforementioned polypeptide, and a pharmaceutically acceptable carrier. 1. A polypeptide for inhibiting , treating or diagnosing metastasis , which is a polypeptide , a derivative polypeptide , or a mutated polypeptide of a fibronectin-binding domain of dipeptidyl peptidase IV.2. The polypeptide as claimed in claim 1 , wherein the fibronectin-binding domain of dipeptidyl peptidase IV has a sequence with 70-100% similarity to a sequence represented by SEQ ID NO: 1.3. The polypeptide as claimed in claim 1 , wherein the fibronectin-binding domain of dipeptidyl peptidase IV has a sequence with 70-100% identity to a sequence represented by SEQ ID NO: 1.4. The polypeptide as claimed in claim 1 , wherein the fibronectin-binding domain of dipeptidyl peptidase IV has a sequence represented by SEQ ID NO: 1.5. The polypeptide as claimed in claim 1 , wherein the fibronectin-binding domain of dipeptidyl peptidase IV is a binding domain A of dipeptidyl peptidase IV.6. The polypeptide as claimed in claim 1 , wherein an N-terminal of the polypeptide is fused with a maltose-binding protein (MBP).7. An use of a polypeptide to prepare a pharmaceutical composition for inhibiting claim 1 , treating or diagnosing metastasis claim 1 , wherein the polypeptide is a polypeptide claim 1 , a derivative polypeptide claim 1 , or a mutated polypeptide of a fibronectin-binding domain of dipeptidyl peptidase IV.8. The use as claimed in claim 7 , wherein the fibronectin-binding domain of dipeptidyl peptidase IV has a sequence with 70-100% similarity to a sequence represented by SEQ ID NO: 1.9. The use as claimed in claim 7 , wherein the ...

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Номер записи: 26

17-10-2013 дата публикации

MUTANT PROTEASES AND METHODS OF USE THEREOF

Номер: US20130273027A1

Автор: Eddins Michael, Leach Craig, Nicholson Benjamin, Stemer David

Принадлежит:

Mutant enzymes and methods of use thereof are provided. 1. A method for screening for modulators of an enzyme , said method comprisinga) contacting at least one mutant of said enzyme with at least one compound, wherein said mutant comprises at least one mutation in at least one blocking loop;b) measuring the activity of the mutant enzyme in the presence of said compound,wherein a modulation in the activity of the mutant enzyme in the presence of the compound compared to the activity of the mutant enzyme in the absence of the compound indicates that the compound is a modulator of the wild-type enzyme.2. The method of claim 1 , wherein said modulator is an inhibitor.3. The method of claim 1 , wherein said blocking loop is identified by protein structure.4. The method of claim 1 , wherein said mutation is in a tetra serine motif in said blocking loop.5. The method of claim 1 , wherein said enzyme is an isopeptidase.6. The method of claim 5 , wherein said isopeptidase is a deubiquitinating enzyme or ubiquitin-like protein (Ubl)-specific protease (Ulp).7. The method of claim 6 , wherein said enzyme is selected from the group consisting of ubiquitin specific protease 14 (USP14) claim 6 , USP24 claim 6 , USP42 claim 6 , USP36 claim 6 , USP53 claim 6 , USP26 claim 6 , USP10 claim 6 , USP51 claim 6 , SUMO1/sentrin specific protease 7 (SENP7) claim 6 , SENP1 claim 6 , and COP9 signalsome complex subunit 5 (CSN5).8. The method of claim 7 , wherein said enzyme is USP14.9. The method of claim 8 , wherein said mutant enzyme comprises an amino acid sequence having at least 80% homology with SEQ ID NO: 1 or 2 claim 8 , wherein at least one amino acid of the tetra serine motif is not a serine.10. The method of claim 9 , wherein said mutant enzyme comprises SEQ ID NO: 2.11. The method of claim 8 , wherein said wherein said mutant enzyme comprises an amino acid sequence having at least 80% homology with SEQ ID NO: 1 or 2 claim 8 , wherein at least one amino acid of the sequence ...

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Номер записи: 27

24-10-2013 дата публикации

ENZYMES AND USES THEREOF

Номер: US20130280786A1

Автор: CLAVERIE JEAN-MICHEL, Joseph Pascale, Leonetti Jean-Paul, Roux Lucie

Принадлежит: DEINOVE

The present invention relates to novel enzymes and the uses thereof. The invention also relates to methods of producing such enzymes, coding nucleic acid molecules, recombinant cells and methods of transforming biomass from such materials. The invention is particularly suited to degrade biomass and/or to improve biomass degradation, and to produce bioenergy products or recombinant proteins. This invention also relates to various applications of the enzymes in the field of paper industry, textile industry as well as in the chemical and medical fields. 118-. (canceled)19. An isolated enzyme or polypeptide selected from:{'i': 'Deinococcus', 'a) an enzyme, wherein said enzyme is derived from a or a related bacterium and is involved in energetic metabolism; or'}b) a polypeptide comprising an amino acid sequence selected from SEQ ID NOs: 1-12, 27-41, 58, 60, 62, 64, 66, 68, 70 or 72 or a fragment thereof comprising at least 15 contiguous residues thereof.20. The isolated enzyme of claim 19 , which is active at a temperature of 30° C. or more.21. The isolated enzyme of claim 19 , wherein said enzyme catalyses biomass modification.22. The isolated enzyme of claim 21 , wherein said enzyme is selected from amylases claim 21 , glucosidases claim 21 , cellulases claim 21 , xylanases claim 21 , pectinases claim 21 , esterases claim 21 , acetyl xylan esterases claim 21 , or glucuronidases.23. The isolated enzyme of claim 22 , which comprises all or an active part of an amino acid sequence selected from SEQ ID NOs: 1-12 claim 22 , 58 claim 22 , 60 claim 22 , 62 claim 22 , 64 claim 22 , 66 claim 22 , 68 claim 22 , 70 or 72.24. The isolated enzyme of claim 21 , wherein said enzyme is involved in biofuel production by fermentation.25. The isolated enzyme of claim 24 , wherein said enzyme is selected from acetaldehyde dehydrogenases claim 24 , alcohol dehydrogenases or pyruvate dehydrogenases.26. The isolated enzyme of claim 24 , which comprises all or an active part of an amino acid ...

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Номер записи: 28

31-10-2013 дата публикации

Polypeptides Having Endoglucanase Activity And Polynucleotides Encoding Same

Номер: US20130291230A1

Автор: Lopez de Leon Alfredo, Rey Michael

Принадлежит:

The present invention relates to isolated polypeptides having endoglucanase activity and isolated polynucleotides encoding the polypeptides. The invention also relates to nucleic acid constructs, vectors, and host cells comprising the polynucleotides as well as methods of producing and using the polypeptides. 1. An isolated polynucleotide encoding a polypeptide having endoglucanase activity , selected from the group consisting of:(a) a polynucleotide encoding a polypeptide comprising an amino acid sequence having at least 90% sequence identity to the mature polypeptide of SEQ ID NO: 4;(b) a polynucleotide encoding a polypeptide which hybridizes under at least high stringency conditions with (i) the mature polypeptide coding sequence of SEQ ID NO: 3, (ii) the genomic DNA sequence of the mature polypeptide coding sequence of SEQ ID NO: 3, or (iii) the full-length complement of (i) or (ii), wherein high stringency conditions are defined as prehybridization and hybridization at 42° C. in 5×SSPE, 0.3% SDS, 200 μg/ml sheared and denatured salmon sperm DNA, and 50% formamide and washing three times each for 15 minutes using 2×SSC, 0.2% SDS at 65° C.; and(c) a polynucleotide encoding a polypeptide comprising a nucleotide sequence having at least 90% sequence identity to the mature polypeptide coding sequence of SEQ ID NO: 3.2. The polynucleotide of claim 1 , wherein the polypeptide having endoglucanase activity comprises an amino acid sequence having at least 90% sequence identity to the mature polypeptide of SEQ ID NO: 4.3. The polynucleotide of claim 2 , wherein the polypeptide having endoglucanase activity comprises an amino acid sequence having at least 95% sequence identity to the mature polypeptide of SEQ ID NO: 4.4. The polynucleotide of claim 3 , wherein the polypeptide having endoglucanase activity comprises an amino acid sequence having at least 97% sequence identity to the mature polypeptide of SEQ ID NO: 4.5. The polynucleotide of claim 1 , which hybridizes ...

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Номер записи: 29

28-11-2013 дата публикации

THERMOPHILIC AND THERMOACIDOPHILIC BIOPOLYMER-DEGRADING GENES AND ENZYMES FROM ALICYCLOBACILLUS ACIDOCALDARIUS AND RELATED ORGANISMS, METHODS

Номер: US20130316406A1

Автор: Apel William A., Henriksen Emily D., Lacey Jeffrey A., Reed David W., Thompson David N., Thompson Vicki S.

Принадлежит: BATTELLE ENERGY ALLIANCE, LLC

Isolated and/or purified polypeptides and nucleic acid sequences encoding polypeptides from are provided. Further provided are methods of at least partially degrading, cleaving, or removing polysaccharides, lignocellulose, cellulose, hemicellulose, lignin, starch, chitin, polyhydroxybutyrate, heteroxylans, glycosides, xylan-, glucan-, galactan-, or mannan-decorating groups using isolated and/or purified polypeptides and nucleic acid sequences encoding polypeptides from 1. An isolated or purified nucleic acid sequence comprising a nucleic acid sequence encoding a polypeptide selected from the group consisting of polypeptides having at least 90% sequence identity to SEQ ID No. 2 , 19 , 52 , 69 , 86 , 102 , 119 , 136 , 153 , 168 , 185 , 202 , 219 , 236 , 253 , 270 , 287 , 304 , 321 , 337 , 354 , 371 , 388 , 405 , 422 , and 439; at least 93% sequence identity to SEQ ID No. 462; at least 94% sequence identity to SEQ ID No. 36; at least 96% sequence identity to SEQ ID No. 460; at least 99% sequence identity to SEQ ID No. 464; at least 99.6% sequence identity to SEQ ID No. 458; and at least 99.7% sequence identity to SEQ ID No. 456.2. The isolated or purified nucleic acid sequence of claim 1 , wherein the polypeptide has enzymatic activity at or below about pH 7.3. The isolated or purified nucleic acid sequence of claim 1 , wherein the polypeptide has enzymatic activity at a temperature at or above about 50 degrees Celsius.4. The isolated or purified nucleic acid sequence of claim 1 , wherein the nucleic acid sequence is present in a vector.5. An isolated or purified polypeptide comprising a polypeptide selected from the group consisting of polypeptide having at least 90% sequence identity to SEQ ID No. 2 claim 1 , 19 claim 1 , 52 claim 1 , 69 claim 1 , 86 claim 1 , 102 claim 1 , 119 claim 1 , 136 claim 1 , 153 claim 1 , 168 claim 1 , 185 claim 1 , 202 claim 1 , 219 claim 1 , 236 claim 1 , 253 claim 1 , 270 claim 1 , 287 claim 1 , 304 claim 1 , 321 claim 1 , 337 claim 1 , ...

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Номер записи: 30

05-12-2013 дата публикации

METHODS AND COMPOSITIONS FOR THE PRODUCTION OF EXTREMOPHILE ENZYMES FROM GREEN MICROALGAE AND CYANOBACTERIA

Номер: US20130323803A1

Автор: Grunden Amy Michele, Sederoff Heike Inge Ada

Принадлежит: North Carolina State University

The present invention relates to compositions and methods for stable transformation of green microalgae and for production of transgenic green microalgae and/or cyanobacteria that produce extremophile enzymes as co-products during the growth of the green microalgae and/or cyanobacteria for lipid biofuel production. Thus, the present invention provides nucleic acid constructs and methods of transformation useful in the production of stably transformed green microalgae and/or cyanobacteria expressing extremophile enzymes in combination with lipid production for biofuel. 123-. (canceled)24. A method for producing one or more extremophile enzymes , the method comprising:(a) culturing a green microalgae cell, wherein the green microalgae cell is stably transformed with a heterologous nucleotide sequence encoding one or more extremophile enzymes and expresses the one or more extremophile enzymes; and(b) collecting the one or more extremophile enzymes from the green microalgae cell culture of (a), thereby producing one or more extremophile enzymes.25. The method of claim 24 , wherein the green microalgae cell is stably transformed with the heterologous nucleotide sequence encoding one or more extremophile enzymes claim 24 , bypropelling the heterologous nucleotide sequence at a green microalgae cell embedded in a gel at a velocity sufficient to pierce the cell wall, cell membrane and chloroplast membrane and deposit the heterologous nucleotide sequence within a chloroplast of the green microalgae cell;wherein the heterologous nucleotide sequence is incorporated into the chloroplast genome of the green microalgae cell, thereby producing a stably transformed green microalgae cell, andfurther wherein the heterologous nucleotide sequence is carried by a microprojectile and the heterologous nucleotide sequence is propelled at the green microalgae cell by propelling the microprojectile at the green microalgae cell.26. The method of claim 24 , wherein the heterologous nucleotide ...

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Номер записи: 31

12-12-2013 дата публикации

METHOD FOR USING AN ENZYME RESISTANT TO HIGH PRESSURES

Номер: US20130330758A1

Автор: Cho Yong-Jin, Kim Chong-Tai, Kim Chul-Jin, Kim Nam-Soo, Kwon Soo-Jin, Maeng Jin-Soo

Принадлежит: KOREA FOOD RESEARCH INSTITUTE

At least at least one embodiment of the present invention relates to a method for using a high pressure-resistant enzyme in a high pressure condition; a method for promoting the activity of the high pressure-resistant enzyme by means of a high pressure treatment; a composition, which contains the high pressure-resistant enzyme, for decomposing proteins under a high pressure condition; a composition, which contains the composition for decomposing proteins, for preparing natural flavoring substances; a container for high pressure treatment, which contains the composition for decomposing proteins; and a method for measuring the activity of the high pressure-resistant enzyme, which comprises a step of decomposing an azocasein solution serving as a substrate by using the high pressure-resistant enzyme treated under a high pressure condition. 1. A method for using an enzyme under a high pressure condition , wherein the enzyme is at least one selected from the group consisting of α-chymotrypsin , pepsin , trypsin , trypsin acetylated , flavourzyme , protease E and alcalase.2. A method for promoting the activity of at least one enzyme selected from the group consisting of α-chymotrypsin , pepsin , trypsin , trypsin acetylated , flavourzyme , protease E and alcalase , wherein the enzyme is treated at high pressure when heating.3. The method according to claim 1 , wherein the high pressure is 100 to 400 MPa.4. The method according to claim 1 , which is at least one selected from the group consisting of a method decomposing proteins claim 1 , carbohydrates or lipids claim 1 , a method for extracting bioactive compounds claim 1 , a method for modifying protein enzymes claim 1 , and a method for synthesizing functional ingredients with enzymes.5. The method according to claim 1 , wherein the high pressure is kept for 60 to 300 min.6. The method according to claim 1 , wherein the heating is conducted at 40° C. or higher for 2 min or longer.7. The method according to claim 2 , ...

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Номер записи: 32

19-12-2013 дата публикации

Polypeptides having endoglucanase activity and polynucleotides encoding same

Номер: US20130340122A1

Автор: Harris Paul, Krogh Kristian, Lassen Soren Flensted, Vlasenko Elena

Принадлежит:

The present invention relates to isolated polypeptides having endoglucanase activity and isolated polynucleotides encoding the polypeptides. The invention also relates to nucleic acid constructs, vectors, and host cells comprising the polynucleotides as well as methods for producing and using the polypeptides. 1. An isolated polypeptide having endoglucanase activity , selected from the group consisting of:(a) a polypeptide comprising an amino acid sequence which has at least 80% sequence identity with the mature polypeptide of SEQ ID NO: 10;(b) a polypeptide which is encoded by a polynucleotide which hybridizes under at least high stringency conditions with (i) the mature polypeptide coding sequence of SEQ ID NO: 9, (ii) the cDNA sequence contained in the mature polypeptide coding sequence of SEQ ID NO: 9, or (iii) a full-length complementary strand of (i) or (ii); and(c) a polypeptide which is encoded by a polynucleotide having at least 80% sequence identity with the mature polypeptide coding sequence of SEQ ID NO: 9.2. The polypeptide of claim 1 , which comprises or consists of the amino acid sequence of SEQ ID NO: 10; or a fragment thereof having endoglucanase activity.3. The polypeptide of claim 1 , which is encoded by a polynucleotide comprising or consisting of SEQ ID NO: 9; or a subsequence thereof which encodes a polypeptide fragment having endoglucanase activity.4E. coli. The polypeptide of claim 1 , which is encoded by the polynucleotide contained in plasmid pPBCel5C which is contained in NRRL B-30900N.5. An isolated polynucleotide comprising a nucleotide sequence which encodes the polypeptide of claim 1 , further comprising at least one mutation in the mature polypeptide coding sequence of SEQ ID NO: 9 in which the mutant nucleotide sequence encodes the mature polypeptide of SEQ ID NO: 10.6. A nucleic acid construct comprising a nucleotide sequence which encodes the polypeptide of operably linked to one or more heterologous control sequences that direct ...

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Номер записи: 33

02-01-2014 дата публикации

Protein variant generation by region shuffling

Номер: US20140005057A1

Автор: Louis Clark, Trish Choudhary

Принадлежит: Codexis Inc

Region shuffling methods for efficiently introducing diversity and exploring sequence space are described. Libraries produced directly from these methods contain high fractions of protein variants harboring multiple beneficial mutations. Typically, the methods produce these variants efficiently without the need for sequencing beneficial mutants identified at intermediate stages of the process.

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Номер записи: 34

09-01-2014 дата публикации

Methods of increasing secretion of polypeptides having biological activity

Номер: US20140011256A1

Автор: Merino Sandra

Принадлежит:

The present invention relates to methods for producing a secreted polypeptide having biological activity, comprising: (a) transforming a fungal host cell with a fusion protein construct encoding a fusion protein, which comprises: (i) a first polynucleotide encoding a signal peptide; (ii) a second polynucleotide encoding at least a catalytic domain of an endoglucanase or a portion thereof; and (iii) a third polynucleotide encoding at least a catalytic domain of a polypeptide having biological activity; wherein the signal peptide and at least the catalytic domain of the endoglucanase increases secretion of the polypeptide having biological activity compared to the absence of at least the catalytic domain of the endoglucanase; (b) cultivating the transformed fungal host cell under conditions suitable for production of the fusion protein; and (c) recovering the fusion protein, a component thereof, or a combination thereof, having biological activity, from the cultivation medium. 1. An isolated fusion protein , comprising:(a) a first amino acid sequence comprising a signal peptide;(b) a second polynucleotide comprising a nucleotide sequence encoding at least a catalytic domain of a Cel45 endoglucanase or a portion thereof; and(c) a third amino acid sequence comprising at least a catalytic domain of a polypeptide having biological activity or a portion thereof.2. The fusion protein of claim 1 , wherein the C-terminal end of the first amino acid sequence is linked in frame to the N-terminal end of the second amino acid sequence and the C-terminal end of the second amino acid sequence is linked in frame to the N-terminal end of the third amino acid sequence or the C-terminal end of the first amino acid sequence is linked in frame to the N-terminal end of the third amino acid sequence and the C-terminal end of the third amino acid sequence is linked in frame to the N-terminal end of the second amino acid sequence.3Humicola insolens. The fusion protein of claim 1 , wherein ...

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Номер записи: 35

09-01-2014 дата публикации

PROCESSING BIOMASS

Номер: US20140011258A1

Автор: LYNCH James J., Masterman Thomas Craig, Medoff Marshall, MOON YEE FUNG Jennifer, YOSHIDA Aiichiro

Принадлежит: XYLECO, INC.

Provided are methods of inducing enzymes, and for treating cellulosic and lignocellulosic biomass with the enzyme. 1. A method comprising:combining a cellulosic or lignocellulosic biomass, which has been treated to reduce its recalcitrance, with a microorganism, and inducing the production of one or more enzymes by the microorganism by maintaining the microorganism-biomass combination under conditions that allow for the production of the enzyme(s) by the microorganism.2. The method of claim 1 , further comprising combining a second cellulosic or lignocellulosic biomass with the microorganism-biomass combination.3. The method of claim 2 , wherein the second biomass is lignocellulosic.4. The method of claim 2 , where the first or second or both first and second biomass has been treated to reduce its recalcitrance by a treatment method selected from the group consisting of: bombardment with electrons claim 2 , sonication claim 2 , oxidation claim 2 , pyrolysis claim 2 , steam explosion claim 2 , chemical treatment claim 2 , mechanical treatment claim 2 , freeze grinding.5. The method of claim 4 , wherein the treatment method is bombardment with electrons.6. The method of claim 2 , further comprising mechanically treating the first cellulosic or lignocellulosic biomass to reduce its bulk density and/or increase its surface area.7. The method of claim 2 , wherein the first or second or both first and second cellulosic or lignocellulosic biomass is comminuted before being combined with the microorganism.8. The method of claim 7 , wherein the comminution comprises dry milling.9. The method of claim 7 , wherein the comminution comprises wet milling.10. The method of claim 2 , wherein the first or second or both first and second cellulosic or lignocellulosic biomass has a particle size of about 30 to 1400 μm.11. The method claim 2 , wherein the first or second or both first and second biomass is a lignocellulosic biomass selected from the group consisting of wood claim 2 , ...

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Номер записи: 36

06-02-2014 дата публикации

Polypeptides Having Isoamylase Activity and Polynucleotides Encoding Same

Номер: US20140038242A1

Автор: Hoff Tine, Norman Barrie Edmund, Sjoeholm Carsten

Принадлежит: NOVOZYMES A/S

The present invention relates to isolated polypeptides having isoamylase activity derived from and isolated polynucleotides encoding the polypeptides. The invention also relates to nucleic acid constructs, vectors, and host cells comprising the polynucleotides as well as methods of producing and using the polypeptides. The invention also relates to the use of said polypeptide having isoamylase activity for producing glucose syrup, fructose syrup, maltose syrup or maltitol. 1. An isolated polypeptide having isoamylase activity , which has at least 95% amino acid sequence identity to the amino acid sequence of amino acids 1-750 of SEQ ID NO: 8.2. The isolated polypeptide of claim 1 , having at least 96% amino acid sequence identity to the amino acid sequence of amino acids 1-750 of SEQ ID NO: 8.3. The isolated polypeptide of claim 1 , having at least 97% amino acid sequence identity to the amino acid sequence of amino acids 1-750 of SEQ ID NO: 8.4. The isolated polypeptide of claim 1 , having at least 98% amino acid sequence identity to the amino acid sequence of amino acids 1-750 of SEQ ID NO: 8.5. The isolated polypeptide of claim 1 , having at least 99% amino acid sequence identity to the amino acid sequence of amino acids 1-750 of SEQ ID NO: 8.6. The isolated polypeptide of claim 1 , comprising or consisting of the amino acid sequence of SEQ ID NO: 8.7. The isolated polypeptide of claim 1 , comprising or consisting of the amino acid sequence of amino acids 1-750 of SEQ ID NO: 8.8. The isolated polypeptide of claim 1 , which is a fragment of the amino acid sequence of SEQ ID NO: 8 having isoamylase activity.9. A composition comprising the isolated polypeptide of .10. The composition of claim 9 , further comprising a glucoamylase.11. The composition of claim 10 , wherein the glucoamylase is a Talaromyces emersonii glucoamylase.12. The composition of claim 9 , further comprising one or more enzymes selected from the group consisting of alpha-amylases claim 9 , beta- ...

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Номер записи: 37

13-02-2014 дата публикации

Polypeptides Having Isoamylase Activity and Polynucleotides Encoding Same

Номер: US20140045223A1

Автор: Barrie Edmund Norman, Carsten Sjoeholm, Tine Hoff

Принадлежит: Novozymes AS

The present invention relates to isolated polypeptides having isoamylase activity derived from Dyella japonica and isolated polynucleotides encoding the polypeptides. The invention also relates to nucleic acid constructs, vectors, and host cells comprising the polynucleotides as well as methods of producing and using the polypeptides. The invention also relates to the use of said polypeptide having isoamylase activity for producing glucose syrup, fructose syrup, maltose syrup or maltitol.

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Номер записи: 38

06-03-2014 дата публикации

Recombinant Beta-Glucosidase Variants for Production of Soluble Sugars from Cellulosic Biomass

Номер: US20140065678A1

Автор: Andor Attila, Yang Jie, Zhang Xiyun

Принадлежит: CODEXIS, INC.

The invention relates to recombinant expression of a variant form of a fungal C1 strain β-glucosidase. The invention also relates to the generation of fermentable sugars from biomass and the production of biofuels by fermentation of the sugars using genetically modified organisms expressing the β-glucosidase variant. The invention provides methods for producing a fermentable sugar, such as glucose, from cellobiose by contacting cellobiose with a recombinant β-glucosidase variant protein, such as a variant protein secreted by a recombinant host cell into culture medium. Methods of the invention may be used for conversion of a biomass substrate to a fermentable sugar, and ultimately to ethanol or other biofuel. 1. A β-glucosidase (Bgl1) variant that has at least 70% identity to amino acid residues 20-870 of SEQ ID NO:2 and comprises an amino acid substiution at position Q291 , an amino acid substitution at position D369 , or an amino acid substitution at position E402 , as determined with reference to SEQ ID NO:2.2. The Bgl1 variant of claim 1 , wherein the substitution at Q291 is W claim 1 , A claim 1 , or F; the substitution at D369 is L claim 1 , Y claim 1 , V claim 1 , A H claim 1 , R claim 1 , F claim 1 , E claim 1 , M claim 1 , I claim 1 , K claim 1 , C claim 1 , P claim 1 , or Q; or the substitution at E402 is N.3. A Bgl1 variant of that has claim 1 , relative to a native C1 Bgl1 comprising amino acids 20-870 of SEQ ID NO:2 claim 1 ,a) at least 5-fold greater thermoactivity at about pH 5 and about 65° C., orb) at least 3-fold greater thermostability at about pH 5 and about 65° C., orc) both (a) and (b).4. The Bgl1 variant of claim 1 , further comprising at least one amino acid substitution at a position selected from the group consisting of Q258 claim 1 , Q313 claim 1 , S434 claim 1 , A475 claim 1 , K495 claim 1 , and G628.5. A Bgl1 variant of that has claim 4 , relative to C1 Bgl1 Variant 3 (SEQ ID NO:5) claim 4 ,a) at least β-fold greater thermoactivity at ...

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Номер записи: 39

06-01-2022 дата публикации

ACE2-Fc FUSION PROTEINS FOR SARS-COV-2 MITIGATION

Номер: US20220002699A1

Автор: Keith Lynn Wycoff, Y Tran

Принадлежит: Planet Biotechnology Inc

The present disclosure relates to recombinant fusion proteins comprising an extracellular domain of the human angiotensin-converting enzyme 2 (ACE2), optionally having altered amino acid residues that result in increased binding affinity for the S1 spike protein of SARS-CoV-2, linked to a human immunoglobulin Fc region, that can extend the protein half-life (T1/2) and/or the duration of action as a decoy receptor, and compositions and methods of use of these fusion proteins.

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Номер записи: 40

06-01-2022 дата публикации

High-affinity human ace2 construct for use in diagnosing and treating coronaviruses

Номер: US20220002701A1

Автор: Bing Chen, Jun Zhang, Tianshu XIAO, Yongfei Cai

Принадлежит: Childrens Medical Center Corp

Provided herein, in some aspects, are polypeptide monomers comprising an angiotensin-converting enzyme 2 (ACE2) ectodomain and an oligomerization domain. Also provided herein are oligomeric complexes comprising ACE2 monomers. Methods of using such to monomers and oligomeric complexes for the diagnosis, prevention, and treatment of viral infections such as the coronavirus are also provided.

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Номер записи: 41

04-01-2018 дата публикации

Collagen 7 and related methods

Номер: US20180002401A1

Автор: Malini Viswanathan, Mark De Souza

Принадлежит: Phoenix Tissue Repair Inc

Disclosed are methods of making collagen 7, or functional fragments thereof, as well as collagen 7, and functional fragments thereof produced by such methods, nucleic acids encoding collagen 7, and functional fragments thereof, as well as vectors and host cells comprising such nucleic acids.

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Номер записи: 42

07-01-2021 дата публикации

AMINOPEPTIDASE AND ITS USES

Номер: US20210002623A1

Автор: APPOLAIRE Alexandre, BASBOUS Hind, FRANZETTI Bruno, GIRARD Eric

Принадлежит:

The present invention relates to the use of a TET protein as a N-terminus aromatic amino acid residues specific exopeptidase, said TET protein comprising the amino acid sequence as set forth in SEQ ID NO: 1. 1. A method for providing a N-terminus aromatic amino acid residues specific exopeptidase , wherein said a N-terminus aromatic amino acid residues specific exopeptidase is provided by a TET protein comprising , consisting essentially , or consisting of the amino acid sequence as set forth in SEQ ID NO: 1 ,or any homologous protein derived from said TET protein as set forth in SEQ ID NO: 1 by substitution, addition or deletion of at least one amino acid, provided that the derived protein retains at least 70% of identity with the amino acid sequence as set forth in SEQ ID NO: 1, and said derived protein retaining a N-terminus aromatic amino acid residues specific exopeptidase activity.2. A method for the modification of all or part of a polypeptide content of a substrate comprising peptides , polypeptides and/or proteins , wherein said modification is performed by at least a TET protein harboring at least a N-terminus aromatic amino acid residues specific exopeptidase activity , said at least a TET protein comprising , consisting essentially , or consisting of the amino acid sequence as set forth in SEQ ID NO: 1 ,or any homologous protein derived from said at least a TET protein as set forth in SEQ ID NO: 1 by substitution, addition or deletion of at least one amino acid, provided that the derived protein retains at least 70% of identity with the amino acid sequence as set forth in SEQ ID NO: 1, and said derived protein retaining a N-terminus aromatic amino acid residues specific exopeptidase activity.3. The method according to claim 1 , wherein said a TET protein or said derived protein originates from an extremophile microorganism belonging to the Methanococcales order.4Methanocaldococcus jannaschii.. The method according to claim 3 , wherein said extremophile ...

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Номер записи: 43

03-01-2019 дата публикации

PSMA BINDING LIGAND-LINKER CONJUGATES AND METHODS FOR USING

Номер: US20190002861A1

Автор: Chelvam Venkatesh, Kim Youngsoon, KULARATNE Sumith A., Low Philip Stewart

Принадлежит:

Described herein are prostate specific membrane antigen (PSMA) binding conjugates that are useful for delivering therapeutic, diagnostic and imaging agents. Also described herein are pharmaceutical compositions containing them and methods of using the conjugates and compositions. Also described are processes for manufacture of the conjugates and the compositions containing them. 1. A conjugate comprising a ligand of PSMA (B) , a linker (L) , and a drug (D) , wherein the ligand includes one or more of a carbon-sulfur double bond , a phosphorus-sulfur double bond , a phosphorus-sulfur single bond , a thioester , or a combination thereof , and where the linker is covalently bound to the drug and the linker is covalently bound to the ligand , and where the linker comprises a chain of at least seven atoms.234-. (canceled)35. A kit comprising a sterile vial claim 1 , a composition comprising the conjugate of as a lyophilized solid claim 1 , and instructions describing use of the composition for treating a patient with an inflammatory disease claim 1 , wherein the vial is an amber glass vial with a rubber stopper and an aluminum tear-off seal claim 1 , and the vial is stored inside a cardboard box. This application is a continuation-in part of U.S. application Ser. No. 13/580,436, filed Aug. 22, 2012, which is a U.S. national application under 35 U.S.C. § 371(b) of International Application Serial No. PCT/US2011/026238 filed Feb. 25, 2011, and claims priority under 35 USC § 119(e) to U.S. Provisional Application Ser. No. 61/308,190, filed on Feb. 25, 2010, the entire disclosures of each of which are incorporated herein by reference.The invention described herein pertains to compounds and methods for treating diseases of the prostate, such as prostate cancer and related diseases. More specifically, embodiments of the invention described herein pertain to conjugates of biologically active agents conjugated to PSMA binding ligands.The prostate is one of the male reproductive ...

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Номер записи: 44

13-01-2022 дата публикации

Anti-vegf protein compositions and methods for producing the same

Номер: US20220009997A1

Автор: Matthew Franklin

Принадлежит: Regeneron Pharmaceuticals Inc

The present disclosure pertains to compositions comprising anti-VEGF proteins and methods for producing such compositions.

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Номер записи: 45

20-01-2022 дата публикации

Consensus Prostate Antigens, Nucleic Acid Molecule Encoding The Same And Vaccine And Uses Comprising The Same

Номер: US20220016228A1

Автор: Bernadette Ferraro, David Weiner, Jian Yan, Mathura P. Ramanathan, Niranjan Y. Sardesai

Принадлежит: Inovio Pharmaceuticals Inc, University of Pennsylvania Penn

Provided herein are consensus amino acid sequences of prostate antigens that are capable of breaking tolerance in a targeted species, including PSA, PSMA, STEAP and PSCA antigens. Also provided are nucleic acid sequences that encode one or more consensus amino acid sequences of prostate antigens PSA, PSMA, STEAP and PSCA, as well as genetic constructs/vectors and vaccines expressing the sequences. Also provided herein are methods for generating an autoimmune response against prostate cancer cells by administering one or more of the vaccines, proteins, and/or nucleic acid sequences that are provided.

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Номер записи: 46

08-01-2015 дата публикации

COLLAGEN 7 AND RELATED METHODS

Номер: US20150011733A1

Автор: Desouza Mark, Viswanathan Malini

Принадлежит:

Disclosed are methods of making collagen 7, or functional fragments thereof, as well as collagen 7, and functional fragments thereof produced by such methods, nucleic acids encoding collagen 7, and functional fragments thereof, as well as vectors and host cells comprising such nucleic acids. 1. A method of making collagen 7 comprising:providing a cell recombinantly manipulated to express collagen 7, or a functional fragment thereof, and, optionally one or more polypeptides that increase expression of collagen 7, e.g., prolidase;culturing said cell under conditions sufficient for the production of collagen 7 and prolidase,thereby making collagen 7.2. The method of claim 1 , wherein said cell is genetically manipulated to express a glycosyl transferase.3. (canceled)4. The method of claim 1 , wherein said cell comprises exogenously introduced nucleic acid that encodes collagen 7 claim 1 , or a functional fragment thereof claim 1 , e.g. claim 1 , a high glycine codon optimized nucleic acid sequence described herein.5. The method of claim 1 , wherein said cell comprises exogenously introduced nucleic acid that encodes prolidase.6. The method of claim 1 , wherein said cell comprises exogenously introduced nucleic acid that encodes glycosyl transferase.7. The method of claim 1 , wherein said cell comprises an expression vector that comprises a sequence that encodes collagen 7.819-. (canceled)20. The method of claim 1 , further comprising recovering collagen 7 claim 1 , or functional fragment thereof claim 1 , from said cultured cell.2123-. (canceled)24. The method of claim 1 , wherein at least 30 claim 1 , 40 claim 1 , 50 claim 1 , 60 claim 1 , 70 claim 1 , 80 claim 1 , 90 or 95% of said collagen 7 claim 1 , or functional fragment thereof claim 1 , is incorporated into homotrimers.25. The method of claim 1 , wherein at least 30 claim 1 , 40 claim 1 , 50 claim 1 , 60 claim 1 , 70 claim 1 , 80 claim 1 , 90 or 95% of said collagen 7 claim 1 , or functional fragment thereof ...

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Номер записи: 47

03-02-2022 дата публикации

Anti-vegf protein compositions and methods for producing the same

Номер: US20220033472A1

Автор: Andrew TUSTIAN, Ankit Vartak, Erica PYLES, Matthew Franklin, Ning Li, Nisha Palackal, Shunhai WANG, Thomas Daly

Принадлежит: Regeneron Pharmaceuticals Inc

The present disclosure pertains compositions comprising anti-VEGF proteins and methods for producing such compositions.

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Номер записи: 48

03-02-2022 дата публикации

ACTIVE LOW MOLECULAR WEIGHT VARIANTS OF ANGIOTENSIN CONVERTING ENZYME 2 (ACE2)

Номер: US20220033794A1

Автор: Batlle Daniel, Wysocki Jan

Принадлежит:

Disclosed are variants of ACE2, pharmaceutical compositions comprising the variants of ACE2, and treatment methods for reducing Angiotensin II (1-8) plasma levels and/or increasing Angiotensin (1-7) plasma levels in a subject in need thereof. The disclosed variants of ACE2 may include polypeptide fragments of ACE2 having ACE2 activity for converting AngII(1-8) to Ang(1-7). Suitable subjects suitable for the disclosed methods of treatment may include subjects having or at risk for developing diabetic and non-diabetic chronic kidney disease, acute renal failure and its prevention, chronic kidney disease, severe hypertension, scleroderma and its skin, pulmonary, kidney and hypertensive complications, malignant hypertension, renovascular hypertension secondary to renal artery stenosis, idiopathic pulmonary fibrosis, liver fibrosis such as in liver cirrhosis patients, an aortic aneurysm, cardiac fibrosis and remodeling, left ventricular hypertrophy, and an acute stroke. 119.-. (canceled)20. A method of delivering ACE2 activity to the kidney , the method comprising administering to a subject suffering from or at risk of developing kidney damage a pharmaceutical composition that delivers into the kidney an enzymatically active ACE2 variant that is sufficiently C-terminally truncated that it is susceptible to glomerular filtration.21. The method of claim 20 , wherein the subject is suffering from or at risk of kidney disease.22. The method of claim 21 , wherein the subject does not demonstrate symptoms of marked alterations in glomerular permeability.23. The method of claim 20 , wherein the subject is suffering from acute kidney injury.24. The method of claim 20 , wherein the subject is in early phase of diabetic kidney disease.25. The method of claim 20 , wherein the variant is a truncated human ACE2.26. The method of claim 20 , wherein the variant is truncated at a site C-terminal to its residue analogous to residue 522 of SEQ ID NO 2.27. The method of claim 26 , wherein ...

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Номер записи: 49

03-02-2022 дата публикации

SOLUBILIZATION OF MSW WITH BLEND ENZYMES

Номер: US20220033861A1

Автор: Baekgaard Lone, Nielsen Henrik B., Rosgaard Lisa, Soerensen Hanne Risbjerg, Wawrzynczyk Joanna

Принадлежит: RENESCIENCE A/S

The present invention relates to a method for solubilisation or hydrolysis of Municipal Solid Waste (MSW) with an enzyme blend and an enzyme composition for solubilization of Municipal Solid Waste (MSW), the enzyme composition comprising a cellulolytic background composition and a protease, lipase and/or beta-glucanase. 1. A process for solubilizing waste comprising:contacting Municipal Solid Waste (MSW) with an enzyme composition comprising a cellulolytic background composition comprising (a) a cellobiohydrolase I or variant thereof; (b) a cellobiohydrolase II or variant thereof; (c) a beta-glucosidase or variant thereof; and (d) a polypeptide having cellulolytic enhancing activity;and one or more enzymes selected from (i) a protease; (ii) a lipase and (iii) a beta-glucanase.2. (canceled)3. (canceled)4. The process of claim 1 , wherein the waste is pretreated.5. (canceled)6. (canceled)7. The process of claim 1 , wherein the enzyme composition further comprises one or more enzymes selected from (iv) a pectate lyase; (v) a mannanase; and (vi) an amylase.8. (canceled)9. (canceled)10Aspergillus fumigatusAspergillus fumigatusAspergillus fumigatusPenicillium. The process of claim 1 , wherein the cellobiohydrolase I of (a) is an cellobiohydrolase I or variant thereof; the cellobiohydrolase II of (b) is an cellobiohydrolase II or variant thereof; the beta-glucosidase of (c) is an beta-glucosidase or variant thereof; and the polypeptide having cellulolytic enhancing activity of (d) is a sp. GH61 polypeptide having cellulolytic enhancing activity; or homologs thereof.11Bacillus.. The process of claim 1 , wherein the protease (i) of the enzyme composition is derived from the genus12ThermomycesHumicola.. The process of claim 1 , wherein the lipase (ii) of the enzyme composition is derived from the genus or from the genus13Aspergillus.. The process of claim 1 , wherein the beta-glucanase (iii) of the enzyme composition is derived from a member of the genus14. The process of ...

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Номер записи: 50

21-01-2021 дата публикации

METHODS FOR INCREASING GRAIN PRODUCTIVITY

Номер: US20210017532A1

Автор: Duan Penggen, Fu Xiangdong, Huang Ke, Li Yunhai, Liu Qian, Qian Qian, Wang Shuansuo, Wu Kun, Zhang Baolan

Принадлежит:

The invention relates to methods for increasing plant yield, and in particular grain yield by reducing or abolishing the expression and/or activity of OTUB1 in a plant. Also described are genetically altered plants characterised by the above phenotype and methods of producing such plants. 1. A method of increasing grain yield in a plant , the method comprising reducing the expression of at least one nucleic acid encoding a otubain-like protease (OTUB1) and/or reducing the activity of OTUB1.2. (canceled)3. The method of claim 1 , wherein the method comprises introducing at least one mutation into at least one nucleic acid sequence encoding a OTUB1 polypeptide and/or the promoter of the OTUB1 polypeptide.4. (canceled)5. (canceled)6. The method of claim 1 , wherein the nucleic acid encodes a OTUB1 polypeptide wherein the OTUB1 polypeptide comprises SEQ ID NO: 1 or a functional homologue or variant thereof and wherein the nucleic acid encoding a OTUB1 promoter comprises SEQ ID NO: 6 or a functional variant or homologue thereof.7. (canceled)8. (canceled)9. (canceled)10. (canceled)11. The method of claim 1 , wherein the method comprises using RNA interference to reduce the expression of a least one OTUB1 nucleic acid.12. (canceled)13. (canceled)14. The method of claim 1 , wherein the plant is selected from rice claim 1 , wheat claim 1 , maize claim 1 , sorghum claim 1 , barley claim 1 , soybean claim 1 , and brassica.15. (canceled)16. A genetically altered plant claim 1 , part thereof or plant cell claim 1 , wherein said plant comprises at least one mutation in at least one nucleic acid encoding an OTUB1 polypeptide and/or the OTUB1 promoter or wherein the plant comprises an RNA interference construct that reduces the expression of an OTUB1 polypeptide.17. (canceled)18. (canceled)19. (canceled)20. (canceled)21. (canceled)22. (canceled)23. (canceled)24. (canceled)25. The genetically altered plant of claim 16 , wherein claim 16 , the nucleic acid encoding a OTUB1 ...

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Номер записи: 51

25-01-2018 дата публикации

TREATMENT OF DISEASES RELATED TO HYPERACTIVITY OF THE COMPLEMENT SYSTEM

Номер: US20180021416A1

Автор: Lachmann Peter

Принадлежит: Cambridge Enterprise Limited

Raising the level of Factor I above physiological levels can be used to treat diseases in which the underlying pathology is linked to overactivity of the C3b-feedback cycle and the generation and pro-inflammatory effects of iC3b. Methods, agents, and compositions for treatment of such diseases are described. 173-. (canceled)74. A method of lowering the amount of C3b activity in a subject , the method comprising:increasing the level of C3b-inactivating activity and/or iC3b degrading activity in the subject;wherein the level of C3b-inactivating activity and/or iC3b degrading activity in the subject is increased to a level that exceeds a normal level of C3b-inactivating activity and/or iC3b degrading activity in the subject.75. The method according to claim 74 , further comprising not increasing the level of Factor H in the subject.76. The method according to claim 74 , wherein increasing the level of C3b-inactivating activity and/or iC3b degrading activity in the subject comprises increasing the level of Factor I in the subject.77. The method according to claim 76 , wherein the Factor I has at least 90% amino acid identity with native Factor I; andwherein the Factor I retains C3b-inactivating activity and/or iC3b degrading activity.78. The method according to claim 74 , wherein the level of C3b-inactivating activity and/or iC3b degrading activity is increased by at least 10% above the normal level.79. The method according to claim 74 , wherein the level of C3b-inactivating activity and/or iC3b degrading activity is increased by no more than 50% above the normal level.80. The method according to claim 74 , wherein the subject has a normal level of C3b-inactivating activity and/or iC3b degrading activity prior to increasing the level of C3b-inactivating activity and/or iC3b degrading activity in the subject.81. The method according to claim 74 , wherein the subject is human.82. The method according to claim 74 , wherein the subject suffers from Age-related Macular ...

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Номер записи: 52

17-04-2014 дата публикации

Polypeptides Having Carboxypeptidase Activity And Polynucleotides Encoding Same

Номер: US20140106400A1

Автор: Rey Michael

Принадлежит:

The present invention relates to isolated polypeptides having carboxypeptidase activity and isolated polynucleotides encoding the polypeptides. The invention also relates to nucleic acid constructs, vectors, and host cells comprising the polynucleotides as well as methods of producing and using the polypeptides. 1. A method of producing a hydrolysate from a proteinaceous substrate which comprises subjecting the substrate to an endopeptidase and a polypeptide having carboxypeptidase activity , selected from the group consisting of:(a) a polypeptide comprising an amino acid sequence having at least 95% sequence identity to the mature polypeptide of SEQ ID NO: 2;(b) a polypeptide encoded by a polynucleotide that hybridizes under at least very high stringency conditions with (i) the mature polypeptide coding sequence of SEQ ID NO: 1, (ii) the genomic DNA sequence comprising the mature polypeptide coding sequence of SEQ ID NO: 1, or (iii) the full-length complement of (i) or (ii), wherein very high stringency conditions are defined as prehybridization and hybridization at 42° C. in 5×SSPE, 0.3% SDS, 200 μg/ml sheared and denatured salmon sperm DNA, and 50% formamide, and washing three times each for 15 minutes using 2×SSC, 0.2% SDS at 70° C.; and(c) a polypeptide encoded by a polynucleotide comprising a nucleotide sequence having at least 95% sequence identity to the mature polypeptide coding sequence of SEQ ID NO: 1;wherein said polypeptide has the carboxypeptidase activity of SEQ ID NO: 2.2. The polypeptide of claim 1 , comprising the amino acid sequence of SEQ ID NO: 2 or the mature polypeptide thereof; or a fragment thereof having carboxypeptidase activity.3E. coli. The polypeptide of claim 1 , which is encoded by the polynucleotide contained in plasmid pTter44C2 which is contained in NRRL B-50207.4. A method of obtaining from a proteinaceous substrate a hydrolysate enriched in free glutamic acid and/or peptide bound glutamic acid residues claim 1 , comprising ...

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Номер записи: 53

28-01-2016 дата публикации

Milling Process

Номер: US20160024228A1

Автор: Han Wang, Long Zhen, McLaughlin Scott R.

Принадлежит: NOVOZYMES A/S

Process for treating crop kernels, comprising the steps of: a) soaking kernels in water to produce soaked kernels; b) grinding the soaked kernels; c) treating the soaked kernels in the presence of an effective amount of a feruloyl esterase, wherein step c) is performed before, during or after step b). 2. The process of claim 1 , further comprising treating the soaked kernels in the presence of a protease.3. The process of claim 1 , further comprising treating the soaked kernels in the presence of an enzyme selected from the group consisting of an endoglucanase claim 1 , a xylanase claim 1 , a cellobiohydrolase I claim 1 , a cellobiohydrolase II claim 1 , a GH61 claim 1 , or a combination thereof.4. The process of claim 1 , further comprising treating the soaked kernels in the presence of an endoglucanase.5. The process of claim 1 , further comprising treating the soaked kernels in the presence of a xylanase.6. The process of claim 1 , wherein the kernels are soaked in water for about 2-10 hours.7. The process of claim 1 , wherein the soaking is carried out at a temperature between about 40° C. and about 60° C.8. The process of claim 1 , wherein the soaking is carried out at acidic pH.9. The process of claim 1 , wherein the soaking is performed in the presence of between 0.01-1%.10. The process of claim 1 , wherein the crop kernels are from corn (maize) claim 1 , rice claim 1 , barley claim 1 , sorghum bean claim 1 , or fruit hulls claim 1 , or wheat.11Aspergillus,Chaetomium,Humicola,Thielavia,Penicillium.. The process of claim 1 , wherein the feruloyl esterase is derived from a strain of the genus a strain of a strain of a strain of and/or a strain of12. (canceled) This application contains a Sequence Listing in computer readable form. The computer readable form is incorporated herein by reference.The present invention relates to an improved process of treating crop kernels to provide a starch product of high quality suitable for conversion of starch into mono- and ...

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Номер записи: 54

24-01-2019 дата публикации

REWIRING ABERRANT CANCER SIGNALING TO A THERAPEUTIC EFFECTOR RESPONSE WITH A SYNTHETIC TWO-COMPONENT SYSTEM

Номер: US20190024070A1

Автор: Chung Hokyung, Lin Michael Z.

Принадлежит:

Compositions and methods for targeted treatment of cancer are disclosed. In particular, the invention relates to methods of targeting anti-cancer therapy to cells exhibiting aberrant signaling associated with cancer pathogenesis by administering synthetic signaling proteins that couple detection of an oncogenic signal to release of therapeutic agents into cancerous cells. 1. A method for targeted treatment of a cancer associated with hyperactivity of a receptor tyrosine kinase , the method comprising:a) administering to a subject in need thereof a therapeutically effective amount of a first fusion protein comprising a protease connected to a phosphotyrosine binding (PTB) domain capable of binding to a phosphorylated tyrosine residue on the receptor tyrosine kinase; andb) administering a therapeutically effective amount of a second fusion protein comprising an SH2 domain connected to i) a substrate comprising a cleavage site recognized by the protease and ii) an anti-cancer therapeutic agent, wherein cleavage of the substrate at the cleavage site by the protease of the first fusion protein releases the anti-cancer therapeutic agent from the second fusion protein.2. The method of claim 1 , wherein the receptor tyrosine kinase is a hyperactive ErbB receptor tyrosine kinase.3. The method of claim 1 , wherein the protease is a hepatitis C virus (HCV) NS3 protease.4. The method of claim 1 , wherein the first fusion protein further comprises a degron claim 1 , wherein degradation activity of the degron is inhibited by binding of the PTB domain of the fusion protein to the phosphorylated tyrosine residue on the receptor tyrosine kinase such that the fusion protein accumulates preferentially in cancerous cells.5. The method of claim 4 , wherein the degron is located in a loop of the PTB domain.6. The method of claim 4 , wherein the degron is a HIF1a degron.7. The method of claim 1 , wherein the PTB is a Shc PTB.8. The method of claim 1 , wherein the SH2 domain is a Vav1 SH2 ...

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Номер записи: 55

29-01-2015 дата публикации

Method for Producing an Acidified Milk Drink

Номер: US20150030723A1

Автор: Jeppe Wegener Tams, Preben Nielsen

Принадлежит: Chr Hansen AS, Novozymes AS

The present invention relates to a method for producing an acidified milk drink using an enzyme which reduces the isoelectric point of the milk proteins. The invention also relates to a novel enzyme having deamidase activity and its use in production of an acidified milk drink.

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Номер записи: 56

31-01-2019 дата публикации

ENHANCED PROTEIN EXPRESSION

Номер: US20190032065A1

Автор: BONGIORNI Cristina, Schmidt Brian F., Van Kimmenade Anita

Принадлежит: DANISCO US INC.

The present invention relates in general to bacterial cells having a genetic alteration that results in increased expression of a protein of interest and methods of making and using such cells. Aspects of the present invention include Gram positive microorganisms, such as species, having a genetic alteration that reduces the expression of a gene in the pdh operon and results in enhanced expression of a protein of interest. 1Bacillus. A method for increasing expression of a protein of interest from a sp. cell comprising:{'i': 'Bacillus', 'a) obtaining an altered sp. cell capable of producing a protein of interest, wherein said altered cell comprises at least one genetic alteration that reduces expression of one or more genes in the pdh operon; and'}{'i': 'Bacillus', 'b) culturing said altered cell under conditions such that said protein of interest is expressed by said altered cell, wherein expression of said protein of interest is increased in said altered cell compared to the expression of said protein of interest in a corresponding unaltered sp. cell grown under essentially the same culture conditions.'}2. (canceled)3Bacillus. The method of claim 1 , wherein said altered cell has reduced expression of the pdhA gene as compared to the expression of the phdA gene in a corresponding unaltered sp. cell grown under essentially the same culture conditions.4Bacillus. The method of claim 1 , wherein said altered cell has reduced expression of the pdhB gene as compared to the expression of the phdB gene in a corresponding unaltered sp. cell grown under essentially the same culture conditions.5Bacillus. The method of claim 1 , wherein said altered cell has reduced expression of the pdhA gene and the pdhB gene as compared to the expression of the phdA gene and the pdhB gene in a corresponding unaltered sp. cell grown under essentially the same culture conditions.6. The method of claim 1 , wherein said genetic alteration results in a decrease in the level of an mRNA ...

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Номер записи: 57

31-01-2019 дата публикации

DIGITAL MICROBIOLOGY

Номер: US20190032105A1

Автор: DIEVART Rebecca, Favier Christine, Lebofsky Ronald, MOUSCADET Jean Francois, QUIRING Christophe, SARFATI Patrice

Принадлежит:

Methods, compositions, and kits are provided for rapidly analyzing microbial growth and/or number in a plurality of water-in-oil emulsion droplets. 190-. (canceled)91. A method for determining the presence or absence of a micro-organism in a sample , the method comprising:i) encapsulating a sample in a plurality of water-in-oil emulsion droplets wherein the water-in-oil emulsion droplets further encapsulate a microbiological growth medium;ii) incubating the plurality of water-in-oil emulsion droplets at a temperature permissive of microbiological growth, and for a period of time sufficient to allow the target microorganisms to go through 5 to 45 doubling times;iii) identifying water-in-oil emulsion droplets comprising target microorganisms; andiv) responsive to identifying the target microorganism in at least one water-in-oil emulsion droplet, determining that the target microorganism is present in the sample, wherein the target microorganisms are selected from yeasts and molds and wherein the incubating step is performed for a period of time corresponding to:at least about 6 hours and no more than about 12 hours when the target microorganisms are yeasts; andat least about 8 hours and no more than about 36 hours when the target microorganisms are molds.92. A method for determining the presence or absence of a micro-organism in a sample , the method comprising:i) encapsulating a sample in a plurality of water-in-oil emulsion droplets comprising an intercalating dye and no lysing agent wherein the water-in-oil emulsion droplets further encapsulate a microbiological growth medium;ii) identifying water-in-oil emulsion droplets comprising target microorganisms by detection of the intercalating dye; andiii) responsive to identifying the target microorganism in at least one water-in-oil emulsion droplet, determining that the target microorganism is present in the sample.93. The method of claim 92 , wherein:the water-in-oil droplet further comprises labeled protein;the ...

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Номер записи: 58

04-02-2021 дата публикации

VECTOR LIBRARY FOR YEAST TWO HYBRID SCREENING AND METHOD FOR IDENTIFYING DEUBIQUITINATING ENZYME BINDING TO TARGET PROTEIN USING SAME

Номер: US20210032619A1

Автор: BAEK Kwang-hyun, KIM So-Ra, KIM Soo-Yeon, KWON Seul-Ki, LEE Da-Hye

Принадлежит: CHA UNIVERSITY INDUSTRY-ACADEMIC COOPERATION FOUNDATION

The present invention provides a vector library for yeast two-hybrid screening of a deubiquitinating enzyme that binds to a target protein and a method for identifying a deubiquitinating enzyme binding to a target protein using the same. Also, the present invention provides a method for screening an agent having anti-cancer activity targeting the deubiquitinating enzyme USP1, USP7, USP12, or USP49 identified by said identifying method. 1. A vector library for yeast two-hybrid screening of a deubiquitinating enzyme that binds to a target protein , comprising:a vector obtained by inserting a gene encoding a deubiquitinating enzyme USP1 in an empty vector having a DNA-binding domain;a vector obtained by inserting a gene encoding a deubiquitinating enzyme USP2 in an empty vector having a DNA-binding domain;a vector obtained by inserting a gene encoding a deubiquitinating enzyme USP3 in an empty vector having a DNA-binding domain;a vector obtained by inserting a gene encoding a deubiquitinating enzyme USP4 in an empty vector having a DNA-binding domain;a vector obtained by inserting a gene encoding a deubiquitinating enzyme USP5 in an empty vector having a DNA-binding domain;a vector obtained by inserting a gene encoding a deubiquitinating enzyme USP6 in an empty vector having a DNA-binding domain;a vector obtained by inserting a gene encoding a deubiquitinating enzyme USP7 in an empty vector having a DNA-binding domain;a vector obtained by inserting a gene encoding a deubiquitinating enzyme USP8 in an empty vector having a DNA-binding domain;a vector obtained by inserting a gene encoding a deubiquitinating enzyme USP10 in an empty vector having a DNA-binding domain;a vector obtained by inserting a gene encoding a deubiquitinating enzyme USP11 in an empty vector having a DNA-binding domain;a vector obtained by inserting a gene encoding a deubiquitinating enzyme USP12 in an empty vector having a DNA-binding domain;a vector obtained by inserting a gene encoding a ...

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Номер записи: 59

08-02-2018 дата публикации

METHODS FOR CONTROLLING PROTEASE PRODUCTION

Номер: US20180037920A1

Автор: Juntunen Kari, Makinen Susanna, Paloheimo Marja, PUNT Peter, PURANEN Terhi, Vehmaanpera Jari

Принадлежит:

The present description is related to the field of protein production. It introduces novel host cells with low protease activity, a novel protease regulator, its use in expression systems and protein production, and a method of producing host cells for protein production 123-. (canceled)24. A host cell comprising at least one inactivated chromosomal gene wherein the inactivated chromosomal gene comprises a nucleic acid sequence encoding a polypeptide comprising a sequence having at least 90% sequence identity with the amino acids 402-533 of SEQ ID NO: 13;the inactivated chromosomal gene is inactivated by disruption, inhibition of translation or transcription of the chromosomal gene, at least partial deletion, truncation, deletion, insertion, mutation, or silencing, by RNAi, or by CRISPR/Cas9 technology;and the host cell has reduced protease activity compared to the host cell without said inactivation.25AscomycotaPezizomycotinaHypocrealesMicroascalesAspergillus, Chrysosporium, MyceliophthoraHumicolaTrichoderma, Hypocrea, Fusarium, Gibberella, Nectria, Stachybotrys, Claviceps, Metarhizium, Villosiclava, Ophiocordyceps, CephalosporiumScedosporiumTrichoderma reesei, Hypocrea jecorina, T. citrinoviridae, T. longibrachiatum, T. virens, T. harzianum, T. asperellum, T. atroviridae, T. parareesei, Fusarium oxysporum, F. gramineanum, F. pseudograminearum, F. venenatum, Gibberella fujikuroi, G. mondiformis, G. zeaea, Nectria haematococca, Stachybotrys chartarum, S. chlorohalonata, Claviceps purpurea, Metarhizium acridum, M. anisopliae, Villosiclava virens, Ophiocordyceps sinensis, Acremonium chrysogenum, Scedosporium apiospermum, Aspergillus niger, A. awamori, A. oryzae, Chrysosporium lucknowense, Myceliohpthora thermophila, Humicola insolensHumicola griseaTrichoderma reesei.. The host cell of claim 24 , wherein the host cell is selected from the group consisting of filamentous fungal cells from Division claim 24 , Subdivision ; preferably from the group consisting of members ...

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Номер записи: 60

07-02-2019 дата публикации

PROSTATE-ASSOCIATED ANTIGENS AND VACCINE-BASED IMMUNOTHERAPY REGIMENS

Номер: US20190038728A1

Автор: Binder Joseph John, Cho Helen Kim, Dermyer Michael Robert, Jooss Karin Ute, Merson James Richard, Pierce Brian Gregory, Tan Joyce Tsi, Tsai Van To

Принадлежит:

The present disclosure provides (a) isolated immunogenic PAA polypeptides; (b) isolated nucleic acid molecules encoding immunogenic PAA polypeptides; (c) vaccine compositions comprising an immunogenic PAA polypeptide or an isolated nucleic acid molecule encoding an immunogenic PAA polypeptide; (d) methods relating to uses of the polypeptides, nucleic acid molecules, and compositions; and (e) vaccine-based immunotherapy regimens which involve co-administration of a vaccine in combination with an immune-suppressive-cell inhibitor and an immune-effector-cell enhancer. 126-. (canceled)27. A multi-antigen construct comprising two coding nucleotide sequences , wherein the two coding nucleotide sequences encode two different immunogenic PAA polypeptides selected from the group consisting of:(1) an immunogenic PSMA polypeptide and an immunogenic PSA polypeptide; and(2) an immunogenic PSA polypeptide and an immunogenic PSCA polypeptide.28. The multi-antigen construct according to claim 27 , wherein the immunogenic PSA polypeptide comprises an amino acid sequence selected from the group consisting of:(1) an amino acid sequence comprising amino acids 27-263 of SEQ ID NO: 15;(2) an amino acid sequence comprising amino acids 4-240 of SEQ ID NO:17; and(3) the amino acid sequence of SEQ ID NO:17.29. The multi-antigen construct according to claim 28 , wherein the immunogenic PSCA polypeptide comprises an amino acid sequence selected from the group consisting of:(1) the amino acid sequence of SEQ ID NO:21;(2) an amino acid sequence comprising amino acids 2-125 of SEQ ID NO:21; and(3) an amino acid sequence comprising amino acids 4-125 Of SEQ ID NO:21.30. The multi-antigen construct according to claim 28 , wherein the immunogenic PSMA polypeptide comprises an amino acid sequence selected from the group consisting of:(1) an amino acid sequence comprising amino acids 15-750 of SEQ ID NO:1;(2) the amino acid sequence of SEQ ID NO:3;(3) the amino acid sequence of SEQ ID NO:5;(4) the ...

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Номер записи: 61

24-02-2022 дата публикации

ANGIOTENSIN-CONVERTING ENZYME 2 (ACE2) IMMUNOADHESIN MICROBODY

Номер: US20220056429A1

Автор: Landau Nathaniel R., Tada Takuya

Принадлежит:

Provided are polypeptides comprising an enzymatically inactive angiotensin-converting enzyme 2 (ACE2) ectodomain, a segment of an immunoglobulin Fc and optionally a purification tag. A cDNA or an expression vector encoding the polypeptide along with a method of culturing cells comprising the expression vector is also provided. The disclosure also provides a method for prophylaxis or therapy for a Coronavirus infection by administering the polypeptide to an individual in need thereof. 1. A polypeptide comprising an enzymatically inactive angiotensin-converting enzyme 2 (ACE2) ectodomain that does not comprise an intact ACE2 transmembrane domain or an intact cytoplasmic tail , the polypeptide further comprising a segment of an immunoglobulin Fc that is not an intact Fc region.2. The polypeptide of claim 1 , wherein the ACE2 is enzymatically inactive by a mutation of an amino acid in an ACE2 catalytic active site.3. The polypeptide of claim 2 , wherein the mutation is at position 345 of SEQ ID NO:2 such that the amino acid at said position in not Histidine.4. The polypeptide of claim 3 , wherein the amino acid at position 345 of SEQ ID NO:2 is an alanine.5. The polypeptide claim 1 , wherein the segment of the immunoglobulin Fc that is not an intact Fc region comprises a microbody.6. The polypeptide of claim 5 , wherein the microbody comprises a segment of an Fc IgG-CH3.7. The polypeptide of claim 6 , wherein the microbody comprises SEQ ID NO:3.8. The polypeptide of claim 1 , wherein the polypeptide comprises the sequence of amino acids 1-871 of SEQ ID NO:5.9. The polypeptide of claim 8 , wherein the polypeptide further comprises a purification tag.10. The polypeptide of claim 9 , wherein the purification tag is at the C-terminus of the polypeptide.11. The polypeptide of claim 10 , wherein the purification tag comprises a poly-Histidine tag.12. A cDNA or an expression vector encoding the polypeptide of .13. A method comprising culturing cells comprising the expression ...

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Номер записи: 62

16-02-2017 дата публикации

ANTIGENS OF PNEUMOCYSTIS MURINA AND USES THEREOF

Номер: US20170042988A1

Автор: Cai Yang, RAMSAY ALISTAIR JOHN, RUAN SANBAO, SHELLITO JUDD E., WELSH DAVID A.

Принадлежит:

A surface protein of the murine fungal pathogen can be used to generate an immune response in a recipient animal or human that provides prophylactic protection and an anti-fungal activity in subjects already infected with a species. Further, the disclosure provides novel polypeptides or peptides derived from the surface protein Surface Peptidase 1 (SPD-1) that are useful, alone or in combination with the SPD-1 polypeptide, in compositions and methods for the generation of an anti-immune reaction by a recipient subject. The compositions and methods of the disclosure provide advantageous alternatives to available immunogenic determinants for the treatment or prevention of fungal pneumonia. 1Pneumocystis murinaPneumocystis murinaPneumocystis. An immunogenic composition comprising at least one immunogenic component selected from the group consisting of: (a) an isolated Surface Peptidase 1 (SPD-1) polypeptide of and having an amino acid sequence having at least 90% similarity to the sequence according to SEQ ID NO: 1 and (b) at least one immunogenic fragment of an SPD-1 polypeptide of wherein said at least one fragment has an amino acid sequence of at least 90% similarity to an amino acid sequence selected from the group consisting of: SEQ ID NOs: 2 , 4 , 6 , 7 , and 10-40 , and wherein the composition further comprises a pharmaceutically acceptable carrier and is formulated to induce an anti-immune response when administered to an animal or human recipient.2. The composition of claim 1 , wherein the pharmaceutically acceptable carrier comprises an adjuvant.3. The composition of claim 1 , wherein the SPD-1 polypeptide has an amino acid sequence according to SEQ ID NO: 1.4. The composition of claim 1 , wherein the at least one immunogenic fragment of the SPD-1 polypeptide has an amino acid sequence selected from the group consisting of: SEQ ID NOs: 2 claim 1 , 4 claim 1 , 6 claim 1 , 7 claim 1 , and 10-40.5. The composition of claim 3 , wherein the at least one ...

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Номер записи: 63

18-02-2021 дата публикации

METHODS OF AAV VECTOR PRODUCTION BY MODULATING DEUBIQUITINATING ENZYME ACTIVITY

Номер: US20210047657A1

Автор: Kollu Swapna, Nakai Hiroyuki

Принадлежит:

Disclosed are host cells that have modulated DUB gene product activity and methods of using such host cells for increased AAV vector production yield. The disclosure also provides fusion proteins that comprise a DUB domain from a DUB gene product and a viral protein domain, and methods of increasing production of AAV vectors from a host cell that comprise expressing at least one of these fusion proteins in the host cell. 1. A host cell for producing AAV vectors comprising a modulated DUB gene product activity.2. The host cell of claim 1 , wherein the modulated DUB gene product activity comprises at least one of (a) alteration of expression of the DUB gene or (b) alteration of the subcellular localization of the DUB gene product.3. The host cell of claim 1 , wherein the modulated DUB gene product activity comprises expression of a DUB gene that is not normally expressed in the host cell.4. The host cell of claim 1 , wherein the modulated DUB gene product activity comprises overexpression of a DUB gene in the host cell.5. The host cell of claim 1 , wherein the modulated DUB gene product activity comprises suppression of expression of a DUB gene in the host cell.6. The host cell of claim 1 , wherein the modulated DUB gene product activity comprises a loss of the DUB gene activity in the host cell.7. The host cell of claim 1 , wherein the DUB gene is wild-type.8. The host cell of claim 1 , wherein the DUB gene is mutated.9. The host cell of claim 1 , wherein the modulated DUB gene product activity comprises alteration of the subcellular localization of the DUB gene product.10. The host cell of claim 9 , wherein the DUB gene product comprises a heterologous localization peptide.11. The host cell of claim 9 , wherein the DUB gene is wild-type and the DUB gene product is fused with a wild-type AAP protein.12. The host cell of claim 9 , wherein the DUB gene is mutant and the DUB gene product is fused with a wild-type AAP protein.13. The host cell of claim 9 , wherein the ...

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Номер записи: 64

03-03-2022 дата публикации

Anti-Human Transferrin Receptor Antibody Permeating Blood-Brain Barrier

Номер: US20220064288A1

Автор: SONODA Hiroyuki, Takahashi Kenichi

Принадлежит: JCR PHARMACEUTICALS CO., LTD.

Disclosed are a means to convert compounds having physiological or pharmacological activity and unable to pass through the blood-brain barrier into a form that allows them to pass through the blood-brain barrier, and compounds converted thereby. The means is an anti-human transferrin receptor antibody and the converted compounds are molecular conjugates between physiologically active protein or pharmacologically active low-molecular-weight compounds and an anti-human transferrin receptor antibody. 169-. (canceled)70. A fusion protein comprising the amino acid sequences of a humanized anti-human transferrin receptor antibody and iduronate 2-sulfatase ,wherein the amino acid sequence of iduronate 2-sulfatase is linked to the light chain of the antibody on the C-terminal side or the N-terminal side of the light chain, or linked to the heavy chain of the antibody on the C-terminal side or the N-terminal side of the heavy chain, andwherein the light chain variable region and the heavy chain variable region of the antibody are selected from (1) or (2) below:(1) the light chain variable region comprising the amino acid sequence having an identity not lower than 90% to the amino acid sequence set forth as SEQ ID NO: 191, and comprising the amino acid sequence set forth as SEQ ID NO:16 as CDR1, the amino acid sequence set forth as SEQ ID NO:18 as CDR2, and the amino acid sequence set forth as SEQ ID NO:20 as CDR3, andthe heavy chain variable region comprising the amino acid sequence having an identity not lower than 90% to the amino acid sequence set forth as SEQ ID NO: 205, and comprising the amino acid sequence set forth as SEQ ID NO:88 as CDR1, the amino acid sequence set forth as SEQ ID NO:90 as CDR2, and the amino acid sequence set forth as SEQ ID NO:92 as CDR3;(2) the light chain variable region comprising the amino acid sequence having an identity not lower than 90% to the amino acid sequence set forth as SEQ ID NO: 191, and comprising the amino acid sequence set ...

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Номер записи: 65

03-03-2022 дата публикации

Catalysis deactivated angiotensin-converting enzyme 2 (ACE2) variants and their uses

Номер: US20220064618A1

Автор: LIU SHENGJIANG

Принадлежит:

Angiotensin-converting enzyme 2 (ACE2) has been confirmed as a specific receptor for several (3 group coronaviruses include severe respiratory syndrome (SARS) coronavirus (SARS-CoV-1) and recently the causative agent for the World pandemic CoVID-19, SARS-CoV-2, and low pathogenic coronavirus of HCoV-NL63, a member in α-coronavirus group. Viral spike protein (S) of viral envelope is confirmed to bind to ACE2 as viral receptor to start a virus replication cycle. The present invention provides ACE2 and its mutants or variants, the viral or non-viral vectors thereof. Methods of treatment of viral infection of a human subject by using such mutants or variants are also provided.

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Номер записи: 66

14-02-2019 дата публикации

Consensus Prostate Antigens, Nucleic Acid Molecule Encoding The Same And Vaccine And Uses Comprising The Same

Номер: US20190046621A1

Автор: Ferraro Bernadette, Ramanathan Mathura P., Sardesai Niranjan Y., Weiner David, Yan Jian

Принадлежит:

Provided herein are consensus amino acid sequences of prostate antigens that are capable of breaking tolerance in a targeted species, including PSA, PSMA, STEAP and PSCA antigens. Also provided are nucleic acid sequences that encode one or more consensus amino acid sequences of prostate antigens PSA, PSMA, STEAP and PSCA, as well as genetic constructs/vectors and vaccines expressing the sequences. Also provided herein are methods for generating an autoimmune response against prostate cancer cells by administering one or more of the vaccines, proteins, and/or nucleic acid sequences that are provided. 1. A nucleic acid molecule comprising a coding sequence encoding one or more proteins selected from the group comprising:a) SEQ ID NO:2, a protein that is 98% homologous to SEQ ID NO:2, provided amino acids 69, 78, 80, 82, 102, 110, 137, 139, 165, 189, 203, 220, 232 and 248 of SEQ ID NO:2 are conserved, or an immunogenic fragment of SEQ ID NO:2 comprising amino acids corresponding to at least 256 amino acid residues of SEQ ID NO:2 provided amino acids 69, 78, 80, 82, 102, 110, 137, 139, 165, 189, 203, 220, 232 and 248 of SEQ ID NO:2 are conserved;b) SEQ ID NO:4, a protein that is 98% homologous to SEQ ID NO:4, provided amino acids 21, 86, 127, 129, 154, 156, 182, 195, 206, 218, 220, 237, 249, 255, 265, 271 or 275 of SEQ ID NO:4 are conserved, or an immunogenic fragment of SEQ ID NO:4 comprising amino acids corresponding to at least 274 amino acid residues of SEQ ID NO:4, provided amino acids 21, 86, 127, 129, 154, 156, 182, 195, 206, 218, 220, 237, 249, 255, 265, 271 or 275 of SEQ ID NO:4 are conserved;c) SEQ ID NO:6, a protein that is 98% homologous to SEQ ID NO:6, provided amino acids 14, 15, 32, 47, 58, 79, 111, 157, 223, 320, 350, 475, 499, 569, 613, 624, 653, 660, 663, 733 and 734 of SEQ ID NO:6 are conserved, or an immunogenic fragment of SEQ ID NO:6 comprising amino acids corresponding to at least 735 amino acid residues of SEQ ID NO:6, provided amino acids 14, 15 ...

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Номер записи: 67

03-03-2022 дата публикации

Methods, Compositions, and Systems for Detecting Coronavirus Neutralizing Antibodies

Номер: US20220065869A1

Автор: DiTirro Danielle, Petropoulos Christos J., Wrin Mary T.

Принадлежит:

The present disclosure relates to methods, compositions, and systems for detecting whether a subject exposed to a coronavirus has developed a neutralizing antibody response. Also disclosed are methods for determining whether a patient infected by a coronavirus is likely to respond to treatment with an antibody preparation. Also disclosed are methods for detecting the level of neutralizing antibody response in a sample of serum from a subject exposed to a coronavirus or to a coronavirus vaccine. 1. A method for detecting whether a subject exposed to a coronavirus has developed a neutralizing antibody response , comprising: i) a nucleic acid encoding a coronavirus spike protein, and', 'ii) a viral expression vector which comprises an indicator nucleic acid which produces a detectable signal;, '(a) transfecting into a plurality of first cells'}(b) incubating the first cells under conditions such that the first cells produce viral particles comprising the coronavirus spike protein;(c) contacting the viral particles of step (b) with a second cell in the presence or absence of a sample comprising an antibody from the subject, wherein the second cell expresses a cell surface receptor to which the coronavirus binds;(d) measuring the amount of the detectable signal produced by the second cell in the presence or absence of the sample; and(e) comparing the amount of signal measured in step (d) in the presence of the sample with the amount of signal produced in step (d) in the absence of the sample, wherein a reduced amount of signal measured in the presence of the sample indicates that the subject has developed a neutralizing antibody response capable of reducing infection.2. The method of claim 1 , wherein the indicator nucleic acid comprises an indicator gene.3. The method of claim 2 , wherein the indicator gene is a luciferase gene.4. The method of claim 1 , wherein the cell surface receptor is ACE-2.5. The method of claim 1 , wherein the subject was infected with severe ...

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Номер записи: 68

25-02-2021 дата публикации

Selection methods for genetically-modified t cells

Номер: US20210054346A1

Автор: David Rushworth, Laurence J.N. Cooper

Принадлежит: University of Texas System

In some aspects, isolated transgenic cells (e.g., transgenic T cells) are provided that comprise or express a transgene and DHFRFS and/or TYMSSS. Methods for selecting transgeneic cells are also provided.

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Номер записи: 69

23-02-2017 дата публикации

MOLECULES AND METHODS FOR ITERATIVE POLYPEPTIDE ANALYSIS AND PROCESSING

Номер: US20170052194A1

Автор: Borgo Benjamin, Havranek James J.

Принадлежит: WASHINGTON UNIVERSITY

Reagents and methods for the digital analysis of proteins or peptides are provided. Specifically provided herein are proteins for identifying the N-terminal amino acid or N-terminal phosphorylated amino acid of a polypeptide. Also, an enzyme for use in the cleavage step of the Edman degradation reaction and a method for using this enzyme are described. 1. An isolated , synthetic , or recombinant N-terminal amino acid binding protein (NAAB) comprising:{'i': 'E. coli', '(1) an amino acid sequence having a glutamate residue at a position corresponding to position 42 of wild-type methionine aminopeptidase (eMAP) (SEQ ID NO: 1), a tryptophan residue at a position corresponding to position 46 of wild-type eMAP, a threonine or serine residue at a position corresponding to position 56 of wild-type eMAP, an aspartate residue at a position corresponding to position 57 of wild-type eMAP, a serine residue at a position corresponding to position 58 of wild-type eMAP, a leucine residue at a position corresponding to position 59 of wild-type eMAP, a threonine or serine residue at a position corresponding to position 60 of wild-type eMAP, a histidine residue at a position corresponding to position 62 of wild-type eMAP, an asparagine residue at a position corresponding to position 63 of wild-type eMAP, a isoleucine or valine residue at a position corresponding to position 65 of wild-type eMAP, an aspartate residue at a position corresponding to position 66 of wild-type eMAP, a glycine residue at a position corresponding to position 67 of wild-type eMAP, a histidine residue at a position corresponding to position 68 of wild-type eMAP, a glycine residue at a position corresponding to position 69 of wild-type eMAP, a serine or threonine residue at a position corresponding to position 70 of wild-type eMAP, a valine residue at a position corresponding to position 81 of wild-type eMAP, an arginine residue at a position corresponding to position 101 of wild-type eMAP, a histidine residue ...

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Номер записи: 70

21-02-2019 дата публикации

Novel polypeptides with improved proteolytic stability, and methods of preparing and using same

Номер: US20190055279A1

Автор: Krishna Kumar, Martin Beinborn, Venkata RAMAN, Vittorio Montanari

Принадлежит: Tufts Medical Center Inc, TUFTS UNIVERSITY

The present invention includes methods of improving proteolytic stability of a polypeptide, comprising alkylating at least one selected from the group consisting of a N-terminus amino group, the NH group of the N-terminus first internal amide bond, another primary amino group, a thiol group and a thioether group within the polypeptide. The present invention further includes polypeptides incorporating such chemical modifications.

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Номер записи: 71

21-02-2019 дата публикации

METHOD FOR CONTROLLING ENZYME PRODUCTIVITY OF MICROORGANISMS

Номер: US20190055539A1

Автор: Minamitani Yasushi, Sugiura Toshiyuki

Принадлежит:

An object of the present invention is to provide a novel method for controlling enzyme productivity of a microorganism. A pulsed electric field is applied to a microorganism to control the enzyme productivity of the microorganism. 1. A method for controlling the enzyme productivity of a microorganism characterized by applying a pulsed electric field to a microorganism.2. The method according to claim 1 , comprising a step of applying the pulsed electric field to the culture solution during culture of the microorganism.3. The method according to claim 2 , wherein the culture solution circulates in an electrode part that generates the pulsed electric field during culture.4. The method according to claim 2 , wherein the pulsed electric field is repeatedly applied during culture.5. The method according to claim 1 , wherein a pulse waveform of the pulsed electric field is a damped oscillation waveform.6. The method according to claim 1 , wherein a field strength of the pulsed electric field is 10 kV/cm to 50 kV/cm.7. The method according to claim 1 , wherein a production amount of one or more enzymes selected from the group consisting of amylase claim 1 , glucosidase claim 1 , galactosidase claim 1 , cellulase claim 1 , esterase claim 1 , lipase claim 1 , protease claim 1 , phosphatase claim 1 , peptidase claim 1 , nuclease claim 1 , deaminase claim 1 , oxidase claim 1 , dehydrogenase claim 1 , glutaminase claim 1 , pectinase claim 1 , catalase claim 1 , dextranase claim 1 , transglutaminase claim 1 , protein deamidase claim 1 , and pullulanase is controlled.8. The method according to claim 1 , wherein a production amount of one or more enzymes selected from the group consisting of α-amylase claim 1 , α-glucosidase claim 1 , β-glucosidase claim 1 , α-galactosidase claim 1 , β-galactosidase claim 1 , cellulase claim 1 , esterase claim 1 , lipase claim 1 , protease claim 1 , acid phosphatase claim 1 , alkaline phosphatase claim 1 , leucine peptidase claim 1 , alanine ...

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Номер записи: 72

17-03-2022 дата публикации

FLAVOUR MODIFYING INGREDIENT DERIVED FROM DIETARY FIBRE

Номер: US20220079197A1

Автор: Bhowmik Tarun, LINCH Stephanie Ann Sander, Myaka Stefka Ivanova

Принадлежит:

A method for making a flavour modifying ingredient, the method comprising subjecting a dietary fibre to enzymatic hydrolysis and/or fermentation; flavour modifying ingredients obtainable by said method; flavour compositions and food products comprises said flavour modifying ingredient; uses of said flavour modifying ingredient. 1Lactobacillus plantarum, Lactobacillus casei, Lactobacillus brevis, Lactobacillus helveticus, L. delbrueckiibulgaricus, Streptococcus thermophiles, Lactobacillus acidophilusBifidobacterium.. A method for making a flavour modifying ingredient , the method comprising subjecting a dietary fibre to enzymatic hydrolysis or fermentation , or enzymatic hydrolysis and fermentation , wherein the fermentation uses one or more than one lactic acid bacteria selected from the group consisting of ssp. and/or2. The method of claim 1 , wherein the dietary fibre is isolated dietary fibre.3. The method of claim 1 , wherein the dietary fibre is an aqueous slurry of dietary fibre.4. The method of claim 1 , wherein the dietary fibre is a cereal fibre claim 1 , a vegetable fibre claim 1 , or a fruit fibre.5. The method of claim 1 , wherein the enzymatic hydrolysis uses one or more enzymes selected from carbohydrases and proteolytic enzymes.6. The method of claim 1 , wherein the enzymatic hydrolysis uses at least one or more enzymes selected from cellulases claim 1 , pectinases claim 1 , and other carbohydrases.7. (canceled)8. The method of claim 1 , wherein the enzymatic hydrolysis is performed at a temperature ranging from about 25° C. to about 60° C.9. The method of claim 1 , wherein the enzymatic hydrolysis takes place for a period of time ranging from about 1 hour to about 48 hours.10. The method of claim 1 , wherein the fermentation is performed at a temperature ranging from about 20° C. to about 45° C.11. The method of claim 1 , wherein the fermentation takes place for a period of time ranging from about 1 day to about 10 days.12. (canceled)13. The method ...

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Номер записи: 73

22-05-2014 дата публикации

Granule with hydrated barrier material

Номер: US20140141971A1

Автор: Alfred L. Gaertner, Douglas A. Dale, Mahmood M. Ghani, Nathaniel T. Becker, Robert I. Christensen, Jr.

Принадлежит: DANISCO US INC

A granule having high stability and low dust is described. The granule includes a hydrated barrier material having moderate or high water activity. Also described are methods of producing the granules.

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Номер записи: 74

28-02-2019 дата публикации

Cell Differentiation Marker and its Uses

Номер: US20190062697A1

Автор: MAIORANO DOMENICO, VAN DER LAAN Siem

Принадлежит:

The use of Dub3 protein, a nucleic acid molecule coding for the protein, or an inhibitor of the activity and/or of the expression of the protein for modulating cell differentiation. 1. A method for modulating cell differentiation comprising the administration to a determined cell:Dub3 protein, said protein comprising the amino acid sequence as set forth in SEQ ID NO: 1, or any variant thereof having at least 43% identity with said amino acid sequence SEQ ID NO: 1, and having ubiquitin hydrolase activity ora nucleic acid molecule coding for said protein or said variant thereof, oran inhibitor of the activity, i.e. the ubiquitin hydrolase activity and/or of the expression of said protein or said variant thereof.2. The method according to claim 1 , for modulating totipotent or pluripotent cell differentiation.3. A method for inducing dedifferentiation of differentiated cells claim 1 , the cells obtained from the dedifferentiation of differentiated cells being iPS cells claim 1 , the method comprising a step of administering to a differentiated cellsDub3 protein, said protein comprising the amino acid sequence as set forth in SEQ ID NO: 1, or any variant thereof having at least 43% identity with said amino acid sequence SEQ ID NO: 1, ora nucleic acid molecule coding for said protein or said variant thereof.4. The method according to for inducing dedifferentiation of differentiated cells claim 3 , wherein said cells Dub3 protein or said nucleic acid molecule coding for said protein are associated with at least an Oct family member protein and a Sox family member protein.5. The method according to claim 3 , wherein said Dub3 protein is expressed in said iPS cells at a level corresponding to at least 2 fold lower than the expression of said Dub3 protein in totipotent cell.6. A method for inducing a spontaneous differentiation of totipotent or pluripotent cells claim 3 , comprising the administration to a determined cell of an inhibitor of the activity and/or of the ...

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Номер записи: 75

11-03-2021 дата публикации

PEPTIDASE AND ITS USES

Номер: US20210071162A1

Автор: APPOLAIRE Alexandre, BASBOUS Hind, FRANZETTI Bruno, GIRARD Eric

Принадлежит:

The invention relates to the uses of a new characterized TET protein showed restricted to N-terminus glycine residues exopeptidase. The invention also relates to a method comprising said use of said new characterized TET protein as a N-terminus glycine residues specific exopeptidase. The invention further relates to a support wherein it is immobilized on said new characterized TET protein as a N-terminus glycine residues specific exopeptidase. 1. A method for providing a N-terminus glycine residues specific exopeptidase , wherein said N-terminus glycine residues specific exopeptidase is provided by a TET protein comprising the amino acid sequence as set forth in SEQ ID NO: 1 , or any homologous protein derived from said TET protein as set forth in SEQ ID NO: 1 by substitution , addition or deletion of at least one amino acid , provided that the derived protein retains at least 70% , preferably at least 79% of identity with the amino acid sequence as set forth in SEQ ID NO: 1 , and said derived protein retaining a N-terminus glycine residues specific exopeptidase activity.2. A method for the modification of all or part of the polypeptide content of a substrate comprising peptides , polypeptides and/or proteins harbouring a N-terminus glycine residue , wherein said modification is performed by at least a TET protein harbouring at least a N-terminus glycine residues specific exopeptidase activity , said at least TET protein comprising the amino acid sequence as set forth in SEQ ID NO: 1 ,or any homologous protein derived from said at least TET protein as set forth in SEQ ID NO: 1 by substitution, addition or deletion of at least one amino acid, provided that the derived protein retains at least 70%, preferably at least 79% of identity with the amino acid sequence as set forth in SEQ ID NO: 1, and said derived protein retaining a N-terminus glycine residues specific exopeptidase activity.3. The method according to claim 1 , wherein said TET protein or said derived ...

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Номер записи: 76

11-03-2021 дата публикации

MOLECULES AND METHODS FOR ITERATIVE POLYPEPTIDE ANALYSIS AND PROCESSING

Номер: US20210072252A1

Автор: Borgo Benjamin, Havranek James J.

Принадлежит: WASHINGTON UNIVERSITY

Reagents and methods for the digital analysis of proteins or peptides are provided. Specifically provided herein are proteins for identifying the N-terminal amino acid or N-terminal phosphorylated amino acid of a polypeptide. Also, an enzyme for use in the cleavage step of the Edman degradation reaction and a method for using this enzyme are described. 183-. (canceled)84. An isolated N-terminal amino acid binding protein (NAAB) , comprising a modified , non-naturally occurring tRNA synthetase (RS) that selectively binds to a N-terminal amino acid residue of a polypeptide with at least about a 1.5:1 ratio of specific to non-specific binding.85. The isolated NAAB of claim 84 , wherein the modified claim 84 , non-naturally occurring aminoacyl tRNA synthetase is coupled with or bound to a fluorescent label.86. The isolated NAAB of claim 85 , wherein the fluorescent label is covalently attached to the modified claim 85 , non-naturally occurring RS.87. The isolated NAAB of claim 84 , wherein the modified claim 84 , non-naturally occurring RS selectively binds to N-terminal amino acid residue of a particular type.88. The isolated NAAB of claim 87 , wherein the type of N-terminal amino acid residue is one selected from the group consisting of alanine claim 87 , arginine claim 87 , asparagine claim 87 , aspartic acid claim 87 , cysteine claim 87 , glutamine claim 87 , glutamic acid claim 87 , glycine claim 87 , histidine claim 87 , isoleucine claim 87 , leucine claim 87 , lysine claim 87 , methionine claim 87 , phenylalanine claim 87 , proline claim 87 , serine claim 87 , threonine claim 87 , tryptophan claim 87 , tyrosine claim 87 , and valine.89. The isolated NAAB of claim 84 , wherein the modified claim 84 , non-naturally occurring RS binds to an N-terminal amino acid residue with a post translational-modification.90. The isolated NAAB of claim 89 , wherein the N-terminal amino acid residue with a post translational-modification is a phosphorylated N-terminal amino acid ...

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Номер записи: 77

16-03-2017 дата публикации

INFLAMMATION-ENABLING POLYPEPTIDES AND USES THEREOF

Номер: US20170072071A1

Автор: GROS Philippe

Принадлежит:

This present technology relates to the use of inflammation-enabling polypeptides (or their coding sequences) to screen for agents useful for the prevention, treatment and/or alleviations of symptoms associated with an inflammatory disorder, to identify individuals susceptible of developing an exacerbated inflammatory response as well as to determine if a therapeutic regimen is capable of preventing, treating or alleviating the symptoms associated to an inflammatory disorder in an individual. The present technology also provides methods for preventing, treating and/or alleviating the symptoms associated to an inflammatory condition based on the inhibition of expression or activity of the inflammation-enabling targets. 1. A method for assessing the ability of an agent to prevent , treat and/or alleviate the symptoms associated with an inflammatory condition in an individual , said method comprising:(a) combining the agent with an inflammatory enabling polypeptide selected from the group consisting of a USP15 polypeptide and a TRIM25 polypeptide;(b) measuring a biological activity of the inflammatory enabling polypeptide of step (a) to obtain a test level;(c) comparing the test level to a control level, wherein the control level is associated with the biological activity of the inflammatory enabling polypeptide observed during the onset or maintenance of the inflammatory condition; and(d) characterizing the agent as (i) useful for the prevention, treatment and/or alleviation of the symptoms associated with the inflammatory condition when the at least one biological activity associated with the test level is lower than the biological activity associated with the control level or (ii) lacking utility for the prevention, treatment and/or alleviation of the symptoms associated with the inflammatory condition when the at least one biological activity associated with the test level is equal to or higher than the biological activity associated with the control level.2. The ...

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Номер записи: 78

24-03-2022 дата публикации

PROTEIN M FUSION PROTEINS AND USES

Номер: US20220089656A1

Автор: DELA CRUZ Jay

Принадлежит:

Fusion proteins with immunoglobulin binding properties, their uses and related methods and compositions are disclosed. The fusion proteins are comprised of an antibody-binding fragment of protein M from spp. conjugated to a receptor fragment. The receptor fragment is a protein fragment to which a pathogen or a toxin can specifically bind. The fusion proteins can be used to neutralize or eradicate a wide group of pathogens or toxins. 1. A method for neutralizing a pathogen , wherein the pathogen has a specific binding affinity for a receptor fragment , the method comprising: providing conditions for interaction between the pathogen and a fusion protein that comprises a polypeptide having at least 90% identity over its entire length with either the sequence set forth in SEQ ID NO: 1 or the sequence set forth in SEQ ID NO: 2 conjugated to the receptor fragment , whereby the fusion protein binds to and neutralizes the pathogen.2. The method according to claim 1 , wherein the receptor fragment is a protein fragment of a cellular receptor.3. The method according to claim 2 , wherein the pathogen is SARS-CoV-2 virus and the receptor fragment comprises the sequence set forth in SEQ ID NO: 15.4. The method according to claim 1 , wherein the fusion protein further comprises a spacer between the polypeptide and the receptor fragment.5. The method according to claim 1 , wherein the receptor fragment comprises one of the following sequences: SEQ ID NO: 16-36.6. The method according to claim 1 , wherein the fusion protein neutralizes the pathogen via recruitment of C1q protein.7. A method for eradicating a bloodborne pathogen in a subject claim 1 , wherein the pathogen has a specific binding affinity for a receptor fragment inside a body of the subject claim 1 , the method comprising:receiving a sample of blood, serum or plasma from the subject or from a donor compatible with the subject, wherein the sample comprises immunoglobulins;adding a fusion protein that comprises a ...

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Номер записи: 79

05-03-2020 дата публикации

COMPOSITIONS AND METHODS COMPRISING KLK3 OR FOLH1 ANTIGEN

Номер: US20200069785A1

Автор: Paterson Yvonne, ROTHMAN John, SHAHABI Vafa

Принадлежит:

The present invention provides KLK3 peptides, FOLH1 peptides, recombinant polypeptides comprising same, recombinant nucleotide molecules encoding same, recombinant strains comprising same, and immunogenic and therapeutic methods utilizing same. 150-. (canceled)51. A method of inhibiting prostate cancer metastasis in a subject , comprising:{'i': 'Listeria', 'administering to the subject a composition comprising a recombinant strain encoding a recombinant fusion peptide consisting of a KLK3 peptide operatively linked to a non-KLK3 peptide, wherein the non-KLK3 peptide is a N-terminal non-hemolytic listeriolysin (LLO) peptide, the fusion peptide consisting of the sequence of SEQ ID NO: 54 or a sequence at least 99% homologous (throughout the length of the peptide), wherein the metastasis is inhibited.'}52ListeriaListeria.. The method of claim 51 , wherein the recombinant strain is an auxotrophic53Listeria. The method of claim 52 , wherein the auxotrophic strain is a dal/dat mutant comprising a deletion in the endogenous ActA gene.54ListeriaListeria. The method of claim 52 , wherein the auxotrophic strain comprises an episomal expression vector encoding a metabolic enzyme that complements the auxotrophy of the auxotrophic strain.55. The method of claim 54 , wherein the metabolic enzyme is an alanine racemase enzyme.56. The method of claim 54 , wherein the metabolic enzyme is a D-amino acid transferase enzyme.57ListeriaListeria monocytogenes. The method of claim 51 , wherein the recombinant is a recombinant strain.58. The method of claim 51 , wherein the inhibiting prostate cancer metastasis comprises metastasis-free prostate cancer progression.59. The method of claim 51 , wherein the inhibiting prostate cancer metastasis comprises a reduced rate of growth or reduced number of prostate cancer metastases.60. A method of treating prostate cancer metastasis in a subject claim 51 , comprising:{'i': 'Listeria', 'administering to the subject a composition comprising a ...

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Номер записи: 80

24-03-2022 дата публикации

ENGINEERED PROTEASE VARIANTS

Номер: US20220090039A1

Автор: Alaoui Ismaili Moulay Hicham, Chng Chinping, Dellas Nikki, Garcia Ravi David, McCluskie Kerryn, Vallieu Kristen Jean

Принадлежит:

The present invention provides engineered protease polypeptides and compositions thereof. The engineered protease polypeptides have been optimized to provide improved activity, improved thermostability, protease stability, autolytic stability, and stability under a range of pH conditions, including acidic (pH<7) and basic (pH>7) conditions. The invention also relates to the use of the compositions comprising the engineered protease polypeptides for therapeutic and/or nutritional purposes. The present invention also provides polynucleotides encoding the engineered protease polypeptides, as well as methods for making the engineered polynucleotides and protease polypeptides. 1. A recombinant protease comprising an amino acid sequence comprising at least 70% , at least 75% , at least 80% , at least 85% , at least 90% , at least 91% , at least 92% , at least 93% , at least 94% , at least 95% , at least 96% , at least 97% , at least 98% , or at least 99% sequence identity to SEQ ID NO: 2 , 4 , 190 , 292 , 342 , 382 , 396 , 400 , 454 , 562 , 638 , 680 , 756 , 812 , 1030 , 1136 , 1180 , 1250 , 1308 , 1366 , 1370 , 1424 , 1532 , 1608 , 1650 , 1726 , 1782 , 2000 , 2106 , 2150 , 2220 , and/or 2278.2. (canceled)3. The recombinant protease of claim 1 , wherein said recombinant protease comprises a polypeptide sequence having at least 85% claim 1 , 86% claim 1 , 87% claim 1 , 88% claim 1 , 89% claim 1 , 90% claim 1 , 91% claim 1 , 92% claim 1 , 93% claim 1 , 94% claim 1 , 95% claim 1 , 96% claim 1 , 97% claim 1 , 98% claim 1 , 99% claim 1 , or more sequence identity to SEQ ID NO: 2 claim 1 , wherein said recombinant protease comprises at least one substitution at one or more positions selected from 236 claim 1 , 258 claim 1 , 261 claim 1 , 339 claim 1 , 439 claim 1 , 446 claim 1 , and 454 claim 1 , wherein the amino acid positions of said polypeptide sequence are numbered with reference to SEQ ID NO: 2.4. The recombinant protease of claim 3 , wherein the substitution at positions ...

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Номер записи: 81

24-03-2022 дата публикации

COMPOSITION FOR CONVERTING INSULIN PRECURSOR INTO INSULIN ENZYME AND METHOD FOR CONVERTING INSULIN PRECURSOR INTO INSULIN BY USING SAME

Номер: US20220090160A1

Автор: BYUN Seungmin, JO Munjeong, Kim Dongkyu, KIM Hyunuk, Kim Jinhwan

Принадлежит:

The present invention relates to: a composition for an enzymatic conversion reaction for converting proinsulin or a proinsulin analogue into insulin or an insulin analogue, the composition comprises one or more selected from the group consisting of calcium chloride, glycine, and proline, and trypsin and/or carboxypeptidase B; and a method for converting proinsulin or a proinsulin analogue into insulin or an insulin analogue by using the composition. The present invention increases the structural stability of an insulin protein and the stability of the enzyme at the same time so as to significantly improve the enzymatic conversion yield and the purity of insulin, thereby being useful in insulin production processes. 1. A composition for enzymatically converting an insulin precursor into insulin , comprising:one or more selected from the group consisting of calcium chloride, glycine, and proline; andtrypsin and/or carboxypeptidase B.2. The composition according to claim 1 , further comprising a buffer solution.3. The composition according to claim 2 , wherein the buffer solution is 1-100 mM Tris-HCl or 1-100 mM borate.4. The composition according to claim 1 , wherein the trypsin is comprised at a weight ratio of 1/1 claim 1 ,000 to 1/40 claim 1 ,000 relative to the insulin precursor claim 1 , and/or the carboxypeptidase B is comprised at a weight ratio of 1/600 to 1/20 claim 1 ,000 relative to the insulin precursor.5. The composition according to claim 1 , wherein the insulin is insulin glargine.6. The composition according to claim 1 , wherein the composition comprises calcium chloride claim 1 , glycine claim 1 , and proline.7. The composition according to claim 6 , wherein calcium chloride is comprised at 5-30 mM claim 6 , glycine is comprised at 3-60 mM claim 6 , and proline is comprised at 20-80 mM.8. A method for converting an insulin precursor into insulin claim 1 , comprising adding an insulin precursor to the composition according to and carrying out a ...

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Номер записи: 82

14-03-2019 дата публикации

Polynucleotide Constructs For In Vitro and In Vivo Expression

Номер: US20190078097A1

Автор: Charles EMRICH, Jesper Vind

Принадлежит: Novozymes AS

The present invention relates to polynucleotide constructs for in vitro and in vivo transcription/translation of genes of interest or variants of a gene of interest as well as microorganism host cells comprising such constructs and methods for producing a polypeptide of interest in such microorganism host cells.

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Номер записи: 83

12-03-2020 дата публикации

DPEP-1 Binding Compositions and Methods of Use

Номер: US20200078442A1

Автор: Babes Liane, Choudhury Saurav Roy, Kubes Paul, Lau Arthur Wing Sze, Muruve Daniel Abraham, Rahn Jennifer Joy, Robbins Stephen Mark, Senger Donna Lorraine

Принадлежит:

Pharmaceutical compositions and methods of their use are provided for reducing inflammation in a subject, blocking leukocyte recruitment, inhibiting tumor metastasis, treating sepsis and preventing/reducing acute kidney injury. 1. A method for treating inflammation in a subject in need thereof , comprising administering an effective amount of a compound that binds to DPEP-1 to the subject , thereby treating inflammation.2. The method of claim 1 , wherein the compound is selected from a competitive antagonist claim 1 , a non-competitive antagonist claim 1 , and uncompetitive antagonist claim 1 , or a silent antagonist of DPEP-1 or a combination thereof.3. The method of claim 1 , wherein the compound comprises a peptide.4. The method of claim 3 , wherein the peptide comprises an LSALT sequence (LSALTPSPSWLKYKAL).5. The method of claim 3 , wherein the peptide comprises a GFE tripeptide sequence selected from CGFECVRQCPERC (GFE-1) or CGFELETC (GFE-2).6. The method of claim 5 , wherein the peptide is not conjugated to cilastatin.7. The method of claim 1 , wherein the compound comprises a blocking antibody of DPEP-1.8. The method of claim 1 , wherein the compound comprises a small molecule.10. The method of claim 1 , wherein the compound is provided as a pharmaceutical composition.11. The method of claim 10 , wherein the pharmaceutical composition is suitable for parenteral or intravenous administration.12. The method of claim 1 , wherein the effective amount is between about 0.01 mg/kg and about 100 mg/kg.13. The method of claim 1 , wherein the inflammation is associated with acute kidney injury.14. The method of claim 1 , further comprising identifying the subject by performing a diagnostic test to determine a need for reduction in inflammation.15. A method for block leukocyte recruitment in a subject in need thereof claim 1 , comprising administering an effective amount of a composition that binds to DPEP-1 to the subject claim 1 , thereby blocking leukocyte ...

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Номер записи: 84

12-06-2014 дата публикации

Erap1-derived peptide and use thereof

Номер: US20140162952A1

Автор: Takuya Tsunoda, Toyomasa Katagiri

Принадлежит: ONCOTHERAPY SCIENCE INC, University of Tokushima NUC

Provided is a novel cancer-treating agent which can be used as a novel choice for the treatment of cancer. Specifically provided are: a peptide that inhibits binding of ERAP1 polypeptide to PHB2 polypeptide, which comprises a binding site of the ERAP1 polypeptide to the PHB2 polypeptide, and a pharmaceutical composition comprising the peptide. In addition, provided is a method for screening a drug candidate for treating and/or preventing cancer using inhibition of the binding of the ERAP1 polypeptide to PP1α polypeptide, PKA polypeptide or PKB polypeptide as an index.

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Номер записи: 85

31-03-2022 дата публикации

Anti-vegf protein compositions and methods for producing the same

Номер: US20220098280A1

Автор: Amardeep Singh Bhupender Bhalla, Hunter Chen, Ning Li, Shunhai WANG

Принадлежит: Regeneron Pharmaceuticals Inc

The present disclosure pertains to compositions comprising anti-VEGF proteins and methods for producing such compositions.

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Номер записи: 86

31-03-2022 дата публикации

PSMA BINDING LIGAND-LINKER CONJUGATES AND METHODS FOR USING

Номер: US20220098564A1

Автор: Chelvam Venkatesh, Kim Youngsoon, KULARATNE Sumith A., Low Philip Stewart

Принадлежит:

Described herein are prostate specific membrane antigen (PSMA) binding conjugates that are useful for delivering therapeutic, diagnostic and imaging agents. Also described herein are pharmaceutical compositions containing them and methods of using the conjugates and compositions. Also described are processes for manufacture of the conjugates and the compositions containing them. 1. (canceled)235-. (canceled)38. The conjugate of claim 36 , wherein the ligand is a prostate specific membrane antigen (PSMA) that is a thiourea of two amino acids claim 36 , wherein the two amino acids are independently selected from asparagine claim 36 , aspartic acid claim 36 , cysteine claim 36 , glutamic acid claim 36 , lysine claim 36 , glutamine claim 36 , arginine claim 36 , serine claim 36 , ornithine claim 36 , threonine claim 36 , and combinations thereof.39. The conjugate of claim 36 , or a salt thereof claim 36 , wherein the chelating group is chelated to a radioactive metal isotope.40. The conjugate of claim 36 , or a salt thereof claim 36 , wherein the divalent linker is covalently bound to the chelating group through the formation of an amide bond claim 36 , and the divalent linker is covalently bound to the ligand through the formation of an amide bond.41. The conjugate of claim 36 , or a salt thereof claim 36 , wherein L is covalently bound to B through an amide bond.42. The conjugate of claim 36 , or a salt thereof claim 36 , wherein L is covalently bound to the chelating group through a carbon-nitrogen single bond.43. The conjugate of claim 37 , or a salt thereof claim 37 , wherein the chelating group is chelated to a radioactive metal isotope.44. The conjugate of claim 37 , or a salt thereof claim 37 , wherein the divalent linker is covalently bound to the chelating group through the formation of an amide bond claim 37 , and the divalent linker is covalently bound to the ligand through the formation of an amide bond.45. The conjugate of claim 37 , or a salt thereof ...

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Номер записи: 87

29-03-2018 дата публикации

Immunogenic Fusion Proteins For The Treatment Of Cancer

Номер: US20180085446A1

Автор: Brockstedt Dirk G., Drake Charles G., Fasso Marcella, Hanson William G., Lauer Peter M., Leong Meredith Lai Ling, Rae Christopher Steven

Принадлежит:

Provided herein are compositions and methods for eliciting an immune response in a subject. In particular, the present disclosure is directed to immunogenic fusion proteins and methods of eliciting an immune response using host cells comprising nucleic acid molecules encoding said fusion proteins. 1195.-. (canceled)196. A recombinant nucleic acid molecule encoding three separate fusion proteins , wherein the three separate fusion proteins are EGFRvIIIx5-SSX2 , EGFRvIIIx5-PAP , and EGFRvIIIx5-NKX3.1(R41G)-PSMA , and wherein:a) EGFRvIIIx5-SSX2 is encoded by a nucleic acid sequence comprising the sequence set forth in SEQ ID NO:3;{'sub': '33-386', 'b) EGFRvIIIx5-PAPis encoded by a nucleic acid sequence comprising the sequence set forth in SEQ ID NO:11; and'}{'sub': 11-234', '1-20, 44-138, 169-750, 'c) EGFRvIIIx5-NKX3.1(R41G)-PSMAis encoded by a nucleic acid sequence comprising the sequence set forth in SEQ ID NO:15.'}197. The nucleic acid molecule of claim 196 , further comprising a promoter claim 196 , a signal sequence claim 196 , or both claim 196 , wherein the promoter claim 196 , signal sequence claim 196 , or both are operably linked with the nucleotide sequence encoding the EGFRvIIIx5 polypeptide and the nucleotide sequence encoding the SSX2 polypeptide.198. The nucleic acid molecule of which is operably linked to an ActA promoter claim 196 , said ActA promoter having the sequence set forth in SEQ ID NO:21.199. A method of eliciting an immune response in a subject claim 196 , said method comprising administering to the subject a therapeutically effective amount of a composition comprising a recombinant nucleic acid molecule claim 196 , wherein the nucleic acid molecule encodes the fusion proteins EGFRvIIIx5-SSX2 claim 196 , EGFRvIIIx5-PAP claim 196 , and EGFRvIIIx5-NKX3.1(R41G)-PSMA claim 196 , and wherein:a) EGFRvIIIx5-SSX2 is encoded by a nucleic acid sequence comprising the sequence set forth in SEQ ID NO:3;{'sub': '33-386', 'b) EGFRvIIIx5-PAPis encoded by a ...

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Номер записи: 88

31-03-2022 дата публикации

Methods of identifying genetic variants

Номер: US20220101948A1

Автор: Himanshu Joshi, Sandra Cooper

Принадлежит: Sydney Childrens Hospitals Network Randwick and Westmead, UNIVERSITY OF SYDNEY

The present invention relates to identification of an abnormal splice site. Provided are methods of identifying an abnormal splice site. Methods of classifying the risk of abnormal splicing of a splice site are also provided. Databases for use in the methods provided herein are also disclosed.

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Номер записи: 89

29-03-2018 дата публикации

NOVEL METALLOPROTEASES

Номер: US20180087038A1

Автор: Babe Lilia M., Ghirnikar Roopa, Goedegebuur Frits, Gu Xiaogang, Kolkman Marc, Yao Jian

Принадлежит:

Aspects of the present compositions and methods relate to novel metalloproteases, polynucleotides encoding the novel metalloproteases, and compositions and methods for use thereof. 1. A polypeptide comprising an amino acid sequence having at least 60% sequence identity to the amino acid sequence selected from the group consisting of SEQ ID NOs: 3 , 8 , 13 , 18 , 23 , 28 , 33 and 38.2. The polypeptide of claim 1 , wherein said polypeptide has at least 80% sequence identity to the amino acid sequence selected from the group consisting of SEQ ID NOs: 3 claim 1 , 8 claim 1 , 13 claim 1 , 18 claim 1 , 23 claim 1 , 28 claim 1 , 33 and 38.3. The polypeptide of any of or claim 1 , wherein said polypeptide has at least 95% sequence identity to the amino acid sequence selected from the group consisting of SEQ ID NOs: 3 claim 1 , 8 claim 1 , 13 claim 1 , 18 claim 1 , 23 claim 1 , 28 claim 1 , 33 and 38.4. The polypeptide of any of the above claims claim 1 , wherein said amino acid sequence is the amino acid sequence selected from the group consisting of SEQ ID NOs: 3 claim 1 , 8 claim 1 , 13 claim 1 , 18 claim 1 , 23 claim 1 , 28 claim 1 , 33 and 38.5. The polypeptide of any of the above claims claim 1 , wherein said polypeptide is derived from a member of the order Bacillales.6. The polypeptide of any of the above claims claim 1 , wherein said Bacillales member is a Paenibacillaceae family member.7Paenibacillus. The polypeptide of claim 6 , wherein said Bacillales member is a spp.8Planococcus. The polypeptide of any of - claim 6 , wherein said polypeptide is derived from a species.9. The polypeptide of any of the above claims claim 6 , wherein said polypeptide has protease activity.10. The polypeptide of claim 9 , wherein said protease activity comprises casein hydrolysis claim 9 , collagen hydrolysis claim 9 , elastin hydrolysis claim 9 , keratin hydrolysis claim 9 , soy protein hydrolysis or corn meal protein hydrolysis.11. The polypeptide of any of the above claims claim 9 ...

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Номер записи: 90

05-05-2022 дата публикации

Multivalent particles compositions and methods of use

Номер: US20220135626A1

Автор: Chang-Zheng Chen, Guoqiang Dong, Hua Zhou, Michael Chen, Tian-Qiang Sun, Yiling LUO

Принадлежит: Achelois Biopharma Inc

Provided herein are multivalent particles and compositions of multivalent particles for blocking viral infection.

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Номер записи: 91

19-03-2020 дата публикации

Multiple Proteases Deficient Filamentous Fungal Cells and Methods of Use Thereof

Номер: US20200087696A1

Автор: Hiltunen Jukka, Huuskonen Anne, Kanerva Anne, Landowski Christopher, Saloheimo Markku, Westerholm-Parvinen Ann

Принадлежит: GLYKOS FINLAND OY

The present disclosure relates to compositions and methods useful for the production of heterologous proteins in filamentous fungal cells. 116-. (canceled)17Myceliophthora thermophilaMyceliophthora thermophila. A filamentous fungal cell comprising at least one endogenous amp or pep protease having no protease activity and a recombinant polynucleotide encoding a mammalian polypeptide , wherein a gene encoding an endogenous amp protease having at least 98% identity to SEQ ID NO: 767 , 774 or 780 or pep protease having at least 98% identity to XP_003667167.1 of the filamentous fungal cell comprises a mutation that eliminates the activity of the endogenous amp or pep protease.18Myceliophthora thermophila. The filamentous fungal cell of claim 17 , wherein the gene encoding endogenous amp or pep protease is deleted.19Myceliophthora thermophila. The cell of comprising at least three claim 17 , four claim 17 , five claim 17 , six claim 17 , seven or eight endogenous proteases having eliminated activity.20Myceliophthora thermophila. The cell of claim 19 , wherein the proteases are selected from the group consisting of aspartic proteases claim 19 , trypsin-like serine proteases claim 19 , subtilisin proteases claim 19 , glutamic proteases claim 19 , and metalloproteases.21Myceliophthora thermophilaMyceliophthora thermophila. The cell of claim 19 , wherein the cell has no detectable protease activity of pep4 protease having at least 98% identity to SEQ ID NO: 499 claim 19 , slp2 protease having at least 98% identity to SEQ ID NO: 540 claim 19 , and slp3 protease having at least 98% identity to SEQ ID NO: 546.22Myceliophthora thermophila. The cell of claim 17 , wherein the mammalian polypeptide is selected from the group consisting of an antibody claim 17 , a growth factor claim 17 , an interferon claim 17 , a cytokine claim 17 , and an interleukin.23Myceliophthora thermophilaMyceliophthora thermophila. The cell of claim 17 , wherein the cell further comprises ALG3 having ...

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Номер записи: 92

05-04-2018 дата публикации

DIPEPTIDYL PEPTIDASE-IV (DPPIV), INHIBITORY PEPTIDE COMPOUND, COMPOSITION CONTAINING THE SAME, AND PRODUCTION METHOD FOR THE SAME

Номер: US20180094027A1

Автор: KAMATA Akira, KONISHI Tatsuya, Takahashi Yoshinori

Принадлежит: MARUHA NICHIRO CORPORATION

A peptide compound having a dipeptidyl peptidase-IV (DPPIV) inhibitory activity or a composition containing the peptide compound that can make a contribution to the prevention of the onset of pathology or the progression in diabetes mellitus patients or those at risk of diabetes mellitus can be provided according to the present invention by a simple method using, as a raw material, milt of a fishery product, which has been eaten for ages and has high safety. In the present invention, a peptide compound having a peptidyl peptidase-IV (DPPIV) inhibitory activity obtained in a hydrolysate of a milt protein source obtained from a fishery product is used as an active component of a composition for inhibiting DPPIV. 111-. (canceled)12. A production method for a hydrolysate having a dipeptidyl peptidase-IV (DPPIV) inhibitory activity , comprising:hydrolyzing a protein source derived from milt of a fishery product to obtain the hydrolysate having a DPPIV inhibitory activity.1317.-. (canceled)18. The production method according to claim 12 , wherein the hydrolyzing step is performed under a condition such that at least one peptide compound selected from the group consisting of Phe-Pro-Val-Gly and salts thereof claim 12 , Ile-Pro-Leu and salts thereof claim 12 , Leu-Pro-Val-Leu and salts thereof claim 12 , and Val-Pro-Phe-Pro and salts thereof is contained in the hydrolysate.19. (canceled)20. A production method for a peptide compound having a dipeptidyl peptidase-IV (DPPIV) inhibitory activity claim 12 , comprising the steps of:{'claim-ref': {'@idref': 'CLM-00012', 'claim 12'}, '(a) obtaining a hydrolysate by the production method according to ; and'}(b) isolating the peptide compound having a DPPIV inhibitory activity from the hydrolysate.21. The method of claim 12 , wherein the fishery product is one or more of salmon claim 12 , pink salmon claim 12 , herring claim 12 , pacific cod claim 12 , skipjack claim 12 , yellowtail (young yellowtail) and squid.22. The method of ...

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Номер записи: 93

13-04-2017 дата публикации

COMPOSITIONS AND METHODS COMPRISING KLK3 OR FOLH1 ANTIGEN

Номер: US20170100469A1

Автор: Paterson Yvonne, ROTHMAN John, SHAHABI Vafa

Принадлежит:

The present invention provides KLK3 peptides, FOLH1 peptides, recombinant polypeptides comprising same, recombinant nucleotide molecules encoding same, recombinant strains comprising same, and immunogenic and therapeutic methods utilizing same. 1Listeria. A recombinant strain expressing a folate hydrolase 1 (FOLH1) peptide , wherein either (a) the sequence of said FOLH1 peptide is a sequence selected from the group consisting of SEQ ID No: 41 , 43 , 44 , and 45; or (b) said FOLH1 peptide is an immunogenic fragment of a larger FOLH1 peptide , wherein the sequence of said larger FOLH1 peptide is selected from the group consisting of SEQ ID No: 41 , 43 , 44 , and 45.2Listeria. The recombinant strain of claim 1 , wherein said FOLH1 peptide is in the form of a fusion peptide claim 1 , wherein said fusion peptide further comprises a non-FOLH1 peptide claim 1 , wherein said non-FOLH1 peptide enhances the immunogenicity of said fragment.3Listeria. The recombinant strain of claim 1 , wherein said non-FOLH1 peptide is selected from the group consisting of a listeriolysin (LLO) peptide claim 1 , an ActA peptide claim 1 , and a PEST-like sequence peptide.4Listeria. The recombinant strain of claim 1 , wherein said FOLH1 peptide does not contain an FOLH1 signal sequence.5Listeria. An immunogenic composition comprising the recombinant strain of and an adjuvant.6ListeriaListeriaListeria monocytogenes. The recombinant strain of claim 1 , wherein said recombinant strain is a recombinant strain.7ListeriaListeria. The recombinant strain of claim 1 , wherein said recombinant strain has been passaged through an animal host.8ListeriaListeriaListeria. The recombinant strain of claim 1 , wherein said strain is an auxotrophic strain.9ListeriaListeria. The recombinant strain of claim 8 , wherein said auxotrophic strain is a dal/dat mutant.10ListeriaListeriaListeria. The recombinant strain of claim 9 , wherein said auxotrophic strain comprises an episomal expression vector comprising a ...

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Номер записи: 94

08-04-2021 дата публикации

METHODS FOR CONTROLLING PROTEASE PRODUCTION

Номер: US20210102231A1

Автор: Juntunen Kari, Makinen Susanna, Paloheimo Marja, PUNT Peter, PURANEN Terhi, Vehmaanpera Jari

Принадлежит: ROAL OY

The present description is related to the field of protein production. It introduces novel host cells with low protease activity, a novel protease regulator, its use in expression systems and protein production, and a method of producing host cells for protein production. 1. A protein preparation comprising protein of interest produced in a host cell having at least one inactivated chromosomal gene wherein:the at least one inactivated chromosomal gene comprises a nucleic acid sequence encoding a polypeptide comprising a sequence having at least 90% sequence identity with the amino acids 402-533 of SEQ ID NO: 13;the at least one inactivated chromosomal gene is inactivated by disruption;and the host cell has reduced protease activity compared to the host cell without said inactivation.2. The protein preparation of claim 1 , wherein the protein preparation further comprises at least one further component selected from stabilizer claim 1 , preservative claim 1 , fragrant claim 1 , buffer claim 1 , salt and colorant.3. The protein preparation of claim 1 , wherein the protein preparation has an improved stability compared to a corresponding protein preparation produced in a host cell with an intact nucleic acid sequence encoding a polypeptide comprising a sequence having at least 90% sequence identity with the amino acids 402-533 of SEQ ID NO: 13.4. The protein preparation of claim 2 , wherein the protein preparation has an improved stability compared to a corresponding protein preparation produced in a host cell with an intact nucleic acid sequence encoding a polypeptide comprising a sequence having at least 90% sequence identity with the amino acids 402-533 of SEQ ID NO: 13.5. The protein preparation of claim 1 , wherein the protein preparation has a reduced amount of endogenous proteases compared to a corresponding protein preparation produced in a host cell with an intact nucleic acid sequence encoding a polypeptide comprising a sequence having at least 90% sequence ...

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Номер записи: 95

04-04-2019 дата публикации

A Liquid Formulation of Alpha-Amylase

Номер: US20190100738A1

Автор: HAN Yun

Принадлежит:

The present disclosure relates to liquid enzyme formulations containing one or more alpha-amylases for use in starch processing, wherein the pH of the enzyme formulation is about pH 6.0-8.0, and methods of use thereof. The present disclosure further relates to methods of making a liquid enzyme formulation containing one or more alpha-amylase having improved stability, comprising titrating the pH of the liquid enzyme formulation to a range of pH 6.0-8.0. 1. A liquid enzyme formulation comprising:(a) an alpha-amylase;(b) a buffering agent;(c) a stabilizer; and(d) a preservative,wherein the pH of the enzyme formulation is about pH 6.0-8.0.2. The liquid enzyme formulation of claim 1 , wherein the pH of the liquid enzyme formulation is about pH 6.3-6.7.3. The liquid enzyme formulation of claim 1 , wherein the stabilizer comprises sucrose claim 1 , sorbitol claim 1 , mannitol claim 1 , glycerol claim 1 , trehalose claim 1 , sodium chloride claim 1 , sodium sulfate claim 1 , or any combination thereof.4. The liquid enzyme formulation of claim 1 , wherein the buffering agent comprises: sodium citrate claim 1 , potassium citrate claim 1 , citric acid claim 1 , sodium acetate claim 1 , acetic acid claim 1 , sodium phosphate claim 1 , potassium phosphate claim 1 , or any combination thereof.5. The liquid enzyme formulation of claim 1 , wherein the alpha-amylase retains at least 90% of its activity at a temperature of 4-40° C.6. The liquid enzyme formulation of claim 1 , wherein the alpha-amylase retains at least 90% of its activity at a temperature of 25-30° C.7. The liquid enzyme formulation of claim 1 , wherein the alpha-amylase retains at least 90% of its activity for 1 year.8. The liquid enzyme formulation of claim 1 , wherein the alpha-amylase has a shelf life of at least 1 year.9. The liquid enzyme formulation of claim 8 , wherein the alpha-amylase has a shelf life of at least 1 year at 25° C.10. The liquid enzyme formulation of claim 1 , wherein the preservative ...

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Номер записи: 96

03-07-2014 дата публикации

Methods For Purifying Insect Membrane-Bound Receptor Proteins From Recombinant Production Hosts

Номер: US20140187758A1

Автор: HASLER James M., LI JIANQUAN, Sheets Joel J.

Принадлежит: DOW AGROSCIENCES LLC

The invention is drawn to a method for purifying membrane-bound proteins expressed in recombinant insect cells using N-laurosarcosine. The invention is particularly suited for expressing cadherin-type receptors cloned from European Corn Borer, and expressed in Sf9 insect cells. The method is optionally adapted for use with 6-his tag proteins. 1. A method for purifying a membrane-bound protein from a recombinant insect cell which comprises:a) suspending the recombinant insect cells in a suitable lysis buffer containing N-laurylsarcosine for an effective period of time, and optionally sonicating;b) centrifuging the lysate from step a);c) dialyzing the supernatant from step b) against a suitable buffer containing 0.15% N-laurylsarcosine, and;d) isolating the membrane-bound protein using a chromatographic method.29. The method of claim 1 , wherein the recombinant insect cell is the Sf insect cell line.3. The method of claim 1 , wherein the suitable buffer is 50 mM Tris® claim 1 , 300 mM NaCl claim 1 , 0.1 mM dithiothreitol claim 1 , and 1.0% N-laurylsarcosine at pH4. The method of claim 1 , wherein the isolation is performed over a HiTrap® Q column or a HisTrap HP column. This application claims the benefit of priority under 35 U.S.C. §119(e) to U.S. Provisional Application Ser. No. 61/746,641, filed Dec. 28, 2012, the disclosure of which is incorporated herein by reference.This invention is in the field of biochemistry and molecular biology. In particular the invention relates to purification of membrane receptor proteins from recombinant host systems.Membrane receptor proteins located in epithelial cells of insect midguts are target sites for the action of crystalline protein toxins (cry toxins) produced by (Bt). Activated cry toxins bind to insect receptor proteins on insect midgut epithelial cells and cause toxicity and death to specific insect pests. The specific interactions between the receptor and toxin are key events in discerning the structure-activity ...

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Номер записи: 97

29-04-2021 дата публикации

METHOD FOR PRODUCING A PROTEIN HYDROLYSATE EMPLOYING AN ASPERGILLUS FUMIGATUS TRIPEPTIDYL PEPTIDASE

Номер: US20210120845A1

Автор: Bak Steffan Yde, Degn Peter Edvard, EISELE Thomas, Haaning Svend, Kragh Karsten Matthias, MEINJOHANNS Ernst

Принадлежит:

The present invention relates to compositions and methods for the production of a hydrolysate comprising at least one endoprotease and a tripeptidyl peptidase capable of cleaving tripeptides from the N-terminus a peptide and/or proteins having one or more of lysine, arginine or glycine in the P1 position wherein said tripeptidyl peptidase is capable of being used at a temperature between 45° C. and 70° C. 1. A method for the production of a hydrolysate comprising: i) comprises the amino acid sequence SEQ ID No. 3, SEQ ID No. 4 or a functional fragment thereof;', 'ii) comprises an amino acid having at least 70% identity to SEQ ID No. 3 or SEQ ID No. 4;', 'iii) is encoded by a nucleotide sequence comprising the sequence SEQ ID No. 1 or SEQ ID No. 2;', 'iv) is encoded by a nucleotide sequence which has at least about 70% identity to SEQ ID No. 1 or SEQ ID No. 2;', 'v) is encoded by a nucleotide sequence which hybridises to SEQ ID No. 1 or SEQ ID No. 2 under medium stringency conditions; or', 'vi) is encoded by a nucleotide sequence which differs from SEQ ID No. 1 or SEQ ID No. 2 due to degeneracy of the genetic code;, 'a) admixing at least one protein or a portion thereof with a tripeptidyl peptidase whichb) incubating at a temperature between 45° C. and 70° C., andc) recovering the hydrolysate.2. A method according to wherein the temperature of the incubation is between 50° C. and 65° C.3. A method according to wherein the temperature of the incubation is between 55° C. and 65° C.4. A method according to claim 3 , wherein the method further comprises admixing the recovered hydrolysate with at least one feed or food ingredient.5. A method according to wherein the protein or portion thereof is further treated with an endoprotease.6. A method according to wherein the endoprotease and the tripeptidyl peptidase are added simultaneously.7. A method according to wherein the endoprotease and the tripeptidyl peptidase are added sequentially claim 6 , e.g. with the tripeptidyl ...

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Номер записи: 98

09-06-2022 дата публикации

PROLINE TOLERANT TRIPEPTIDYL PEPTIDASES AND USES THEREOF

Номер: US20220174981A1

Автор: BAK Steffen Yde, Degn Peter Edvard, EISELE Thomas, Haaning Svend, Kragh Karsten Matthias, MA Maria, MEINJOHANNS Ernst, Miasnikov Andrei

Принадлежит: DUPONT NUTRITION BIOSCIENCES APS

A method for the production of a hydrolysate comprising: (a) admixing at least one protein or a portion thereof with: (A) at least one endoprotease; and (B) (a′) at least one proline tolerant tripeptidyl peptidase or fermentate comprising a proline tolerant tripeptidyl peptidase predominantly having exopeptidase activity wherein said proline tolerant tripeptidyl peptidase is capable of cleaving tri-peptides from the N-terminus of peptides having: Proline at P1; and synthetic amino acids at P1; or (b′) at least one proline tolerant tripeptidyl peptidase having exopeptidase activity wherein said proline tolerant tripeptidyl peptidase is capable of cleaving tri-peptides from the N-terminus of peptides having: Proline at PV; and synthetic amino acids at PV; and (b) recovering the hydrolysate. The invention also relates to methods for producing a hydrolysate comprising the use of an endoprotease an exo-tripeptidyl peptidase of the S53 family and an aminopeptidase, to uses of a proline tolerant tripeptidyl peptidase, compositions, food and/or feed additive compositions comprising the same, as well as hydrolysates and uses of proline tolerant tripeptidyl peptidases. 1. A method for the production of a hydrolysate comprising: (A) at least one endoprotease; and', Proline at P1; and', 'an amino acid selected from alanine, arginine, asparagine, aspartic acid, cysteine, glutamine, glutamic acid, glycine, histidine, isoleucine, leucine, lysine, methionine, phenylalanine, serine, threonine, tryptophan, tyrosine, valine or synthetic amino acids at P1; or', '(b′) at least one proline tolerant tripeptidyl peptidase having exopeptidase activity wherein said proline tolerant tripeptidyl peptidase is capable of cleaving tri-peptides from the N-terminus of peptides having:', 'Proline at P1′; and', 'an amino acid selected from alanine, arginine, asparagine, aspartic acid, cysteine, glutamine, glutamic acid, glycine, histidine, isoleucine, leucine, lysine, methionine, phenylalanine, ...

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Номер записи: 99

09-06-2022 дата публикации

METHOD FOR PREVENTING OR TREATING METABOLIC DISORDER

Номер: US20220175895A1

Автор: Chen Ruey-Hwa, Chen Yu-Hsuan, Huang Tzu-Yu, Li Wen-Hsin, Shen Zhao-Qing, Tsai Ting-Fen

Принадлежит:

Provided is a method for preventing or treating a metabolic disorder, including administering to a subject a therapeutically effective amount of TRABID protein or a functionally related variant thereof, or a nucleic acid encoding TRABID protein or a functionally related variant thereof. Also provided is a method for reducing fat accumulation through TRABID-induced deubiquitination to promote autophagy activity and lipid metabolism. 1. A method for preventing or treating a metabolic disorder in a subject in need thereof , comprising administering to the subject a therapeutically effective amount of tumor-necrosis factor receptor-associated factor (TRAF)-binding protein domain (TRABID) protein or a functionally related variant thereof , or a nucleic acid encoding the TRABID protein or a functionally related variant thereof.2. The method according to claim 1 , wherein the TRABID protein comprises an amino acid sequence of SEQ ID NO:1 or SEQ ID NO:3 claim 1 , and the functionally related variant of the TRABID protein comprises an amino acid sequence having at least 80% sequence identity to SEQ ID NO:1 or SEQ ID NO:3.3. The method according to claim 1 , wherein the nucleic acid encoding the TRABID protein comprises a nucleic acid sequence of SEQ ID NO:2 or SEQ ID NO:4 claim 1 , and the functionally related variant of the nucleic acid encoding the TRABID protein comprises a nucleic acid sequence having at least 80% sequence identity to SEQ ID NO:2 or SEQ ID NO:4.4. The method according to claim 1 , wherein the metabolic disorder is selected from the group consisting of pre-diabetes claim 1 , diabetes claim 1 , obesity claim 1 , diabetic dyslipidemia claim 1 , hyperlipidemia claim 1 , hypertriglyceridemia claim 1 , hyperfattyacidemia claim 1 , hypercholesterolemia claim 1 , fatty liver disease claim 1 , and any combination thereof.5. The method according to claim 4 , wherein the fatty liver disease is selected from the group consisting of non-alcoholic fatty liver disease ...

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