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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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Форма поиска

Поддерживает ввод нескольких поисковых фраз (по одной на строку). При поиске обеспечивает поддержку морфологии русского и английского языка
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06-09-2012 дата публикации

nucleic acid molecule for encoding xylose isomerase and xylose isomerase encoded by the nucleic acid molecule

Номер: US20120225452A1
Автор: Ruilei GE, Xiaoming Bao, Yu Shen
Принадлежит: Shandong University

A novel xylose isomerase nucleotide sequence obtained from a bovine rumen fluid metagenomic library and also provides the amino acid sequence encoded by the nucleotide sequence, and a vector and a transformant containing the nucleotide sequence. When the xylose isomerase is expressed, a host cell is endowed with the capability of converting xylose into xylulose, and the xylulose is further metabolized by the host cell. Therefore, the host cell can take the xylose as a carbon source for growth. The xylose isomerase from a new source is expressed with high activity in Saccharomyces cerevisiae and is a mesophilic enzyme with optimal temperature of 60° C.

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Номер записи: 1
04-04-2013 дата публикации

Transformed cells that ferment-pentose sugars and methods of their use

Номер: US20130084617A1
Автор: Christiaan Van Der Drift, Harry Ramancedj Harhangi, Hubertus Johannes Marie Op Den Camp, Jacobus Thomas Pronk
Принадлежит: C5 Yeast Co BV

The present invention relates to host cells transformed with a nucleic acid sequence encoding a eukaryotic xylose isomerase obtainable from an anaerobic fungus. When expressed, the sequence encoding the xylose isomerase confers to the host cell the ability to convert xylose to xylulose which may be further metabolized by the host cell. Thus, the host cell is capable of growth on xylose as carbon source. The host cell preferably is a eukaryotic microorganism such as a yeast or a filamentous fungus. The invention further relates to processes for the production of fermentation products such as ethanol, in which a host cell of the invention uses xylose for growth and for the production of the fermentation product. The invention further relates to nucleic acid sequences encoding eukaryotic xylose isomerases and xylulose kinases as obtainable from anaerobic fungi.

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Номер записи: 2
08-08-2013 дата публикации

Agent for use in the case of fructose intolerance

Номер: US20130202695A1
Автор: Daniel Henry Wyrobnik, Isaac Harry Wyrobnik
Принадлежит: Vitacare GmbH and Co KG

There is provided in accordance with embodiments of the invention a method of treating or reducing the effects in a subject of a condition selected from fructose intolerance and impaired fructose metabolism, the method comprising administering to a subject in need of such treatment or reduction an efficacious amount of a glucose isomerase, other than in combination with 5-D-fructose dehydrogenase. Other embodiments are also disclosed.

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Номер записи: 3
26-12-2013 дата публикации

Engineered microbes and methods for microbial oil overproduction from cellulosic materials

Номер: US20130344548A1
Автор: Gregory Stephanopoulos, Mitchell Tai
Принадлежит: Massachusetts Institute of Technology

The invention relates to engineering microbial cells for utilization of cellulosic materials as a carbon source, including xylose.

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Номер записи: 4
07-01-2016 дата публикации

COMPOSITIONS AND METHODS FOR INCREASED ETHANOL PRODUCTION FROM BIOMASS

Номер: US20160002676A1
Автор: ARISTIDOU Aristos, JESSEN Holly J., Liao Hans, LUNDORFF Joshua, NEGRETE-RAYMOND Ana, SUOMINEN Pirkko, YI Jian
Принадлежит:

The present application discloses the identification of the novel xylose transporter genes KHT105 and RAG4, as well as the identification of a novel set of pentose phosphate pathway genes The present application further discloses a series of genetically modified yeast cells comprising various combinations of arabinose fermentation pathways, xylose fermentation pathways, pentose phosphate pathways, and/or xylose transporter genes, and methods of culturing these cells to produce ethanol in fermentation media containing xylose. 116-. (canceled)17. A genetically modified yeast cell comprising an active arabinose fermentation pathway , wherein said cell comprises one or more exogenous arabinose fermentation pathway genes selected from the group consisting of AI , RK , and RE genes , wherein the selected exogenous arabinose fermentation pathway gene encodes a polypeptide comprising an amino acid sequence with at least 80% sequence identity to an amino acid sequence selected from the group consisting of the amino acid sequences set forth in SEQ ID Nos: 6 , 8 , 10 , 12 , 14 , 16 , 18 , and 20.18. (canceled)19. The genetically modified yeast cell of further comprising an active xylose fermentation pathway claim 17 , wherein said cell comprises one or more exogenous xylose fermentation pathway genes selected from the group consisting of XR claim 17 , XDH claim 17 , and XK genes.20. The genetically modified yeast cell of further comprising an active xylose fermentation pathway claim 17 , wherein said cell comprises one or more exogenous xylose fermentation pathway genes selected from the group consisting of XI and XK genes.21. The genetically modified yeast cell of further comprising an active non-oxidative pentose phosphate pathway claim 17 , wherein said cell comprises one or more exogenous non-oxidative pentose phosphate pathway genes selected from the group consisting of TKL and TAL genes.2224-. (canceled)25. The genetically modified yeast cell of claim 17 , wherein the AI ...

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Номер записи: 5
04-01-2018 дата публикации

Synthetic carbon fixation pathways

Номер: US20180002704A1
Автор: Achuthanunni Chokkathukalam, Alex van Eck CONRADIE, Katherine Louise Tibbles, Ramdane Haddouche, Satnam Surae
Принадлежит: Invista North America LLC

The present disclosure relates to methods for more efficiently recycling reduced electron carriers in a hydrogen-oxidizing microorganism with an operable Calvin-Benson cycle; synthetic carbon fixation pathways that recycle reduced electron carriers more efficiently than the Calvin-Benson cycle, such as methods for enzymatically converting carbon dioxide to formate and assimilating the resulting formate into central carbon metabolism; methods for producing biochemical products; and recombinant hosts utilizing one or more synthetic carbon fixation pathways.

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Номер записи: 6
08-01-2015 дата публикации

METHODS AND COMPOSITIONS FOR USING MHC CLASS II INVARIANT CHAIN POLYPEPTIDES AS A RECEPTOR FOR MACROPHAGE MIGRATION INHIBITORY FACTOR

Номер: US20150010570A1
Автор: Bucala Richard J., Leng Lin, Metz Christine N.
Принадлежит:

Methods and compositions for using the MHC class II invariant chain polypeptide, Ii (also known as CD74), as a receptor for macrophage migration inhibitory factor (MIF), are disclosed. These include methods and compositions for using this receptor, as well as agonists and antagonists of MIF which bind to this receptor, or which otherwise modulate the interaction of MIF with CD74 or the consequences of such interaction, in treatment of conditions characterized by locally or systemically altered MIF levels, particularly inflammatory conditions and cancer. 1. A method for screening compounds for an agonist or antagonist of MIF comprising:contacting an MHC class II invariant chain (Ii) polypeptide with MIF in the presence and absence of a candidate compound, and a candidate compound that enhances the interaction of said MIF with said Ii polypeptide is identified as an agonist of MIF, and', 'a candidate compound that inhibits the interaction of said MIF with said Ii polypeptide is identified as an antagonist of MIF;, 'comparing the interaction of the MIF and said Ii polypeptide in the presence of said candidate compound with their interaction in the absence of said candidate compound, whereby'}{'figref': {'@idref': 'DRAWINGS', 'FIG. 5'}, 'wherein said Ii polypeptide comprises the complete Ii amino acid sequence of (SEQ ID. NO:2) or an MIF-binding fragment thereof.'}2. An agonist or antagonist of MIF identified by the method of .3. An agonist or antagonist according to which is an antibody or antigen-binding fragment thereof.4. The agonist or antagonist according to wherein said antibody is an anti-CD74 antibody.5. An anti-CD74 antibody of selected from the group consisting ofa monoclonal antibody, a human antibody, a humanized antibody and a chimeric antibody.6. A method of inhibiting an effect of MIF on a cell comprising on its surface an MHC class II invariant chain (Ii) polypeptide which binds MIF and thereby mediates said effect of MIF claim 4 , said method ...

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Номер записи: 7
12-01-2017 дата публикации

VECTORS AND STRAINS FOR PRODUCING MYRCENE AND METHOD OF PRODUCING MYRCENE USING THE SAME

Номер: US20170009240A1
Автор: GONG Gyeongtaek, KIM Eun Mi, KIM Yunje, Lee Sun Mi, UM Youngsoon, WOO Han Min
Принадлежит: KOREA INSTITUTE OF SCIENCE AND TECHNOLOGY

Disclosed herein are an expression vector capable of expressing myrcene, an strain transformed with the vector and having improved capability of producing myrcene and a method for producing myrcene and a method for recycling glycerol using the same. In an aspect, the transformed strain of the present disclosure can produce myrcene with high purity on a large scale using glycerol or glucose as a carbon source. Also, the strain of the present disclosure is economical and environment-friendly because it can produce high value-added myrcene using waste glycerol as a carbon source. In addition, the strongly volatile myrcene can be produced and isolated at the same time. 1Escherichia coli. A transformed strain transformed with a first vector and a second vector ,the first vector comprising, in sequence,a chloramphenicol resistance gene as a selection marker;a p15A replication origin as a replication origin;a lacUV5 promoter;a first domain comprising a gene encoding an enzyme which produces mevalonate from acetyl-CoA; anda second domain comprising a gene encoding an enzyme which produces dimethylallyl pyrophosphate (DMAPP) from mevalonate, andthe second vector comprising, in sequence,an ampicillin resistance gene as a selection marker;a ColE1 replication origin as a replication origin;a trc promoter; anda gene encoding an enzyme which is capable of producing myrcene from geranyl pyrophosphate (GPP).2Escherichia coli. The transformed strain according to claim 1 ,wherein the first vector further comprises one or more selected from a trc promoter; and a gene encoding an enzyme which is capable of producing geranyl pyrophosphate (GPP) from dimethylallyl pyrophosphate (DMAPP) and isopentenyl diphosphate (IPP),the trc promoter is located between the first domain and the second domain, andthe gene encoding an enzyme which is capable of producing geranyl pyrophosphate (GPP) from dimethylallyl pyrophosphate (DMAPP) and isopentenyl diphosphate (IPP) is located downstream of the ...

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Номер записи: 8
14-01-2016 дата публикации

PENTOSE FERMENTATION BY A RECOMBINANT MICROORGANISM

Номер: US20160010132A1
Автор: Cho Catherine M., Mijts Benjamin N., Subbian Ezhilkani, Zhang Xiyun
Принадлежит:

The present invention provides recombinant nucleic acid constructs comprising a xylose isomerase polynucleotide, a recombinant fungal host cell comprising a recombinant xylose isomerase polynucleotide, and related methods. 1. A recombinant fungal host cell comprising a polynucleotide sequence that encodes a polypeptide that is capable of catalyzing the isomerization of D-xylose directly to D-xylulose , wherein the polynucleotide is a recombinant polynucleotide encoding a polypeptide comprising an amino acid sequence having at least 70% identity to SEQ ID NO:2 , wherein said polypeptide further comprises the substitution E372G relative to SEQ ID NO:2 , or a polynucleotide that hybridizes under stringent hybridization conditions to the complement of a polynucleotide that encodes a polypeptide having the amino acid sequence of SEQ ID NO:2.2. The recombinant fungal host cell of claim 1 , wherein said polypeptide capable of catalyzing the isomerization of D-xylose directly to D-xylulose is a mature recombinant xylose isomerase variant having xylose isomerase activity further comprising a substitution at one or more positions selected from 2 claim 1 , 6 claim 1 , 13 claim 1 , 16 claim 1 , 18 claim 1 , 29 claim 1 , 62 claim 1 , 64 claim 1 , 67 claim 1 , 70 claim 1 , 71 claim 1 , 74 claim 1 , 75 claim 1 , 78 claim 1 , 81 claim 1 , 91 claim 1 , 106 claim 1 , 111 claim 1 , 116 claim 1 , 127 claim 1 , 128 claim 1 , 139 claim 1 , 156 claim 1 , 164 claim 1 , 182 claim 1 , 199 claim 1 , 201 claim 1 , 206 claim 1 , 211 claim 1 , 223 claim 1 , 237 claim 1 , 233 claim 1 , 236 claim 1 , 244 claim 1 , 248 claim 1 , 250 claim 1 , 274 claim 1 , 277 claim 1 , 281 claim 1 , 284 claim 1 , 325 claim 1 , 328 claim 1 , 329 claim 1 , 330 claim 1 , 339 claim 1 , 342 claim 1 , 356 claim 1 , 360 claim 1 , 371 claim 1 , 373 claim 1 , 375 claim 1 , 378 claim 1 , 380 claim 1 , 382 claim 1 , 386 claim 1 , 389 claim 1 , 390 claim 1 , 391 claim 1 , 393 claim 1 , 397 claim 1 , 398 claim 1 , 399 claim 1 ...

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Номер записи: 9
11-01-2018 дата публикации

PRODUCTION OF FATTY ACID DERIVATIVES

Номер: US20180010137A1
Автор: Clarke Elizabeth J., Da Costa Bernardo M., Greenfield Derek L., Groban Eli S., HELMAN Noah, Holden Kevin, HU Zhihao, Schirmer Andreas W.
Принадлежит:

The invention relates to compositions and methods, including polynucleotide sequences, amino acid sequences, recombinant host cells and recombinant host cell cultures engineered to produce fatty acid derivative compositions comprising fatty acids, fatty alcohols, fatty aldehydes, fatty esters, alkanes, terminal olefins, internal olefins or ketones. The fatty acid derivative composition is produced extracellularly with a higher titer, yield or productivity than the corresponding wild type or non-engineered host cell. 151.-. (canceled)52. A recombinant host cell comprising a decreased activity of a phosphoenolpyruvate carboxylase (ppc) polypeptide , wherein said recombinant host cell produces a fatty acid derivative composition at a higher titer , yield or productivity than a corresponding wild type host cell when cultured in a medium containing a carbon source under conditions effective to decrease expression of said ppc polypeptide.53. A cell culture comprising the recombinant host cell according to .54. The cell culture of claim 52 , wherein said cell culture comprises a fatty acid derivative composition.55. The cell culture of claim 54 , wherein the fatty acid derivative composition comprises at least one fatty acid derivative selected from the group consisting of fatty acid claim 54 , a fatty ester claim 54 , a fatty alcohol claim 54 , a fatty aldehyde claim 54 , an alkane claim 54 , a terminal olefin claim 54 , an internal olefin claim 54 , and a ketone.56. The cell culture of claim 53 , wherein the fatty acid derivative isa) a C6, C8, C10, C12, C13, C14, C15, C16, C17, or C18 fatty acid derivative, orb) a C10:1, C12:1, C14:1, C16:1, or C18:1 unsaturated fatty acid derivative.57. The cell culture of claim 54 , wherein the fatty acid derivative composition comprises:a) one or more of C8, C10, C12, C14, C16, and C18 fatty acid derivatives,b) fatty acids,c) fatty aldehydes,d) fatty alcohols,e) fatty esters,f) alkanes,g) terminal olefins,h) internal olefins, ori) ...

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Номер записи: 10
14-01-2021 дата публикации

AGARASE-3,6-ANHYDRO-L-GALACTOSIDASE-ARABINOSE ISOMERASE ENZYME COMPLEX AND METHOD FOR PRODUCTION OF TAGATOSE FROM AGAR USING THE SAME

Номер: US20210009982A1
Автор: Han Sung Ok, HYEON Jeong Eun, JEONG Da-Woon
Принадлежит: KOREA UNIVERSITY RESEARCH AND BUSINESS FOUNDATION

The present disclosure relates to an enzyme complex of arabinose isomerase, agarase and 3,6-anhydro galactosidase and a method for producing tagatose by degrading agar using the same. By using the enzyme complex according to the present disclosure, agar obtained from marine biomass can be degraded effectively and useful physiologically active substances such as tagatose can be obtained effectively therefrom. 1. An agarase complex wherein:a fusion protein 1 in which a monosaccharide convertase and a dockerin module are bound;a fusion protein 2 in which agarase and a dockerin module are bound; anda fusion protein 3 in which 3,6-anhydro-L-galactosidase and a dockerin module are bound;are linked via dockerin-cohesin binding by a mini scaffold protein comprising a cohesin module.2Lactobacillus.. The enzyme complex according to claim 1 , wherein the monosaccharide convertase is arabinose isomerase derived from3. The enzyme complex according to claim 2 , wherein the arabinose isomerase comprises amino acid sequence of SEQ ID NO 1.4. The enzyme complex according to claim 1 , wherein the dockerin is derived from cellulase.5. The enzyme complex according to claim 4 , wherein the dockerin is encoded nucleotide sequence of SEQ ID NO 35.6. The enzyme complex according to claim 4 , wherein the cellulase is selected from a group consisting of endo-β-1 claim 4 ,4-glucanase B claim 4 , endo-β-1 claim 4 ,4-xylanase B and exo-glucanase S.7Pseudomonas, SaccharophagusAleromonas.. The enzyme complex according to claim 1 , wherein the agarase is derived from one selected from a group consisting of and8. The enzyme complex according to claim 7 , wherein the agarase is β-agarase.9. The enzyme complex according to claim 8 , wherein the β-agarase is encoded nucleotide sequence of SEQ ID NO 26.10Zobellia.. The enzyme complex according to claim 1 , wherein the 3 claim 1 ,6-anhydro-L-galactosidase is derived from11. The enzyme complex according to claim 10 , wherein the 3 claim 10 ,6-anhydro-L- ...

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Номер записи: 11
09-01-2020 дата публикации

ENZYMATIC PRODUCTION OF HEXOSES

Номер: US20200010824A1
Автор: ROGERS Edwin O., WICHELECKI Daniel Joseph
Принадлежит: BONUMOSE LLC

Disclosed herein are methods of producing hexoses from saccharides by enzymatic processes. The methods utilize fructose 6-phosphate and at least one enzymatic step to convert it to a hexose. 1. An enzymatic process for preparing fructose from a starch derivative , the process comprising the steps of:(i) a step of converting a starch derivative to glucose 1-phosphate (G1P) using alpha glucan phosphorylase (αGP);(ii) a step of converting G1P to glucose 6-phosphate (G6P), wherein the step is catalyzed by phosphoglucomutase (PGM)(iii) a step of converting G6P to fructose 6-phosphate (F6P), wherein the step is catalyzed by phosphoglucoisomerase (PGI)(iv) a step of converting F6P to fructose catalyzed by fructose 6-phosphate phosphatase (F6PP).2. The process of claim 1 , further comprising the step of converting starch to a starch derivative wherein the starch derivative is prepared by enzymatic hydrolysis of starch or by acid hydrolysis of starch claim 1 , wherein the enzymatic hydrolysis of starch is catalyzed by isoamylase claim 1 , pullulanase claim 1 , alpha-amylase claim 1 , or a combination thereof.3. The process of claim 1 , wherein 4-glucan transferase (4GT) is added to the process.4. The process of claim 1 , wherein the process steps are conducted under at least one of the following process conditions:at a temperature ranging from about 37° C. to about 85° C.,at a pH ranging from about 5.0 to about 9.0, orfor about 0.5 hours to about 48 hours.5. The process of claim 1 , wherein the process steps are conducted under at least one of the following process conditions:without adenosine triphosphate (ATP) as a source of phosphate,without nicotinamide adenosine dinucleotide,at a phosphate concentration from about 0.1 mM to about 150 mM,where phosphate is recycled, orwhere step (iv) involves an energetically favorable chemical reaction.6. The process of claim 5 , wherein phosphate is recycled and the phosphate produced by F6PP dephosphorylation of F6P is used in the ...

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Номер записи: 12
19-01-2017 дата публикации

ENHANCING MICROBIAL METABOLISM OF C5 ORGANIC CARBON

Номер: US20170015988A1
Автор: Armenta Roberto E., Benjamin Jeremy, Merkx-Jacques Alexandra, Muise Denise, Rasmussen Holly, Scaife Mark, Woodhall David
Принадлежит: Mara Renewables Corporation

Provided herein are recombinant microorganisms having two or more copies of a nucleic acid sequence encoding xylose isomerase, wherein the nucleic acid encoding the xylose isomerase is an exogenous nucleic acid. Optionally, the recombinant microorganisms include at least one nucleic acid sequence encoding a xylulose kinase and/or at least one nucleic acid sequence encoding a xylose transporter. The provided recombinant microorganisms are capable of growing on xylose as a carbon source. 1. A recombinant microorganism comprising two or more copies of a nucleic acid sequence encoding xylose isomerase , wherein the nucleic acid encoding xylose isomerase is an exogenous nucleic acid.2. The recombinant microorganism of claim 1 , further comprising at least one nucleic acid sequence encoding a xylulose kinase.3. The recombinant microorganism of claim 2 , further comprising at least one nucleic acid sequence encoding a xylose transporter.4. The recombinant microorganism of claim 1 , wherein the microorganism comprises at least 2 claim 1 , 3 claim 1 , 4 claim 1 , 5 claim 1 , 6 claim 1 , 7 claim 1 , 8 claim 1 , 9 claim 1 , 10 claim 1 , 11 claim 1 , 12 claim 1 , 13 claim 1 , 14 claim 1 , 15 claim 1 , 16 claim 1 , 17 claim 1 , 18 claim 1 , 19 claim 1 , 20 claim 1 , 21 claim 1 , 22 claim 1 , 23 claim 1 , 24 claim 1 , 25 claim 1 , 26 claim 1 , 27 claim 1 , 28 claim 1 , 29 claim 1 , 30 claim 1 , 31 claim 1 , 32 claim 1 , 33 claim 1 , 34 claim 1 , 35 claim 1 , 36 claim 1 , 37 claim 1 , 38 claim 1 , 39 claim 1 , or 40 copies of the exogenous nucleic acid sequence encoding xylose isomerase.5. The recombinant microorganism of claim 1 , wherein the 6 nucleic acid sequence encoding the xylose isomerase is at least 90% identical to SEQ ID NO:2.6. The recombinant microorganism of claim 2 , wherein the microorganism comprises at least 2 claim 2 , 3 claim 2 , 4 claim 2 , 5 claim 2 , 6 claim 2 , 7 claim 2 , 8 claim 2 , 9 claim 2 , 10 claim 2 , 11 claim 2 , 12 claim 2 , 13 claim 2 , 14 claim ...

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Номер записи: 13
19-01-2017 дата публикации

METHODS AND STRAINS FOR PRODUCING BIOPRODUCTS IN AUREOBASIDIUM PULLULANS

Номер: US20170016039A1
Автор: LEATHERS Timothy D., PRICE Neil P., Skory Christopher D.
Принадлежит:

The present disclosure provides methods for producing bioproducts from novel genetically altered strains of . Methods and materials for the construction of these strains, examination of the bioproducts and analysis and isolation of the bioproducts from genetically altered strains is provided. Genetically altered strains in which one or more genes encoding biosynthetic enzymes are knocked out is detailed and the benefits of using such strains described. 1. A method of producing arabitol-liamocins , comprising the steps of{'i': 'A. pullulans', 'a) growing a culture of comprising a biologically pure strain lacking a functional MPD1 gene under conditions sufficient to support the production of arabitol-liamocins, wherein said conditions comprise the substantial absence of arabitol; and'}b) collecting said arabitol-liamocins from at least part of said culture, thereby producing arabitol-liamocins.2. The method of claim 1 , wherein the biologically pure strain comprises NRRL 67079.3. The method of claim 1 , wherein said conditions further comprise a growth medium containing glucose as the sole carbon source.4. A method of producing one or more bioproducts claim 1 , comprising the steps of{'i': 'A. pullulans', 'a) growing a culture of comprising a biologically pure strain lacking a functional MDH2 gene and lacking a functional MPD1 gene under conditions sufficient to support the production of one or more bioproducts selected from the group consisting of a liamocin and an exophilin; and'}b) collecting said one or more bioproducts from at least part of said culture, thereby producing the bioproduct.5. The method of claim 4 , wherein said conditions comprise a growth medium containing glucose or fructose as the sole carbon source.6. The method of claim 4 , wherein the bioproduct is an exophilin.7. The method of claim 4 , wherein the bioproduct is a liamocin and wherein said liamocin has a head group comprising lactose claim 4 , glucose claim 4 , mannose claim 4 , galactose ...

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Номер записи: 14
21-01-2016 дата публикации

Xylose isomerases and their uses

Номер: US20160017310A1
Автор: Adam Martin Burja, David Neal Nunn, Jr., Jon Peter Flash BARTNEK, LING Li, Peter Luginbuhl
Принадлежит: BP Corp North America Inc

This disclosure relates to novel xylose isomerases and their uses, particularly in fermentation processes that employ xylose-containing media.

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Номер записи: 15
21-01-2016 дата публикации

NON-CO2 EVOLVING METABOLIC PATHWAY FOR CHEMICAL PRODUCTION

Номер: US20160017339A1
Автор: BOGORAD Igor, Liao James C.
Принадлежит:

Provided are microorganisms that catalyze the synthesis of chemicals and biochemicals from a suitable carbon source. Also provided are methods of generating such organisms and methods of synthesizing chemicals and biochemicals using such organisms. 1. A recombinant microorganism comprising a non-COevolving metabolic pathway for the synthesis of acetyl phosphate with improved carbon yield beyond 1:2 molar ratio (fructose 6-phosphate:Acetyl phosphate) from a carbon substrate using a pathway comprising an enzyme having (i) fructose-6-phosphoketolase (Fpk) activity and/or xylulose-5-phosphoketolase (Xpk) activity and (ii) a fructose 1 ,6 bisphosphatase or a sedoheptuloase 1 ,6 bisphosphatase activity.2. The recombinant microorganism of claim 1 , wherein the microorganism can convert a sugar phosphate to acetyl phosphate with improved yield beyond those obtained by pathways that involve pyruvate decarboxylation.3. The recombinant microorganism of claim 2 , wherein the sugar phosphate is selected from the group consisting of: sugar phosphates of a triose claim 2 , an erythrose claim 2 , a pentose claim 2 , a hexose claim 2 , and a sedoheptulose.4. The recombinant microorganism of claim 3 , wherein the sugar phosphate of a triose is selected from the group consisting of G3P and DHAP; wherein the pentose is selected from the group consisting of RSP claim 3 , Ru5P claim 3 , RuBP claim 3 , and X5P; wherein the hexose is selected from the group consisting of F6P claim 3 , H6P claim 3 , FBP claim 3 , and G6P; and wherein the sedoheptulose is selected from the group consisting of S7P and SBP.5. The recombinant microorganism of claim 3 , wherein the sugar phosphates are derived from a carbon source selected from the group consisting of methanol claim 3 , methane claim 3 , CO claim 3 , CO claim 3 , formaldehyde claim 3 , formate claim 3 , glycerol claim 3 , a carbohydrate having the general formula CHO claim 3 , wherein n=3 to 7 claim 3 , and cellulose.6. The recombinant ...

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Номер записи: 16
21-01-2016 дата публикации

UNIVERSAL PROTEIN OVEREXPRESSION TAG COMPRISING RAMP FUNCTION, AND APPLICATION THEREOF

Номер: US20160017341A1
Автор: KIM Geun-Joong, LEE Eun-Bin, LEE Jin-Young, MIN Sa-Young, PARK Won Ji, YOU Sung-Hwan
Принадлежит: INDUSTRY FOUNDATION OF CHONNAM NATIONAL UNIVERSITY

Provided is a ramp tag capable of solving instability in translation rate resulting from poor compatibility between codons in a foreign gene and a host when expressing a recombinant protein in . Unlike the conventional codon optimization or codon deoptimization method for solving the problem of rare codons, the present invention increases an expression efficiency of a target protein by merely having the ramp tag be fused with a target gene or independently expressed, without changing the original codon sequence, thereby allowing tRNA to be reused. Thus, the present invention provides a novel method for increasing recombinant protein expression which is capable of reducing costs and time in comparison to the codon optimization method that artificially synthesizes DNA sequences. Therefore, it is expected that the method of the present invention will be able to be used in production of high value-added pharmaceuticals or industrial enzymes. 1. A method of producing a ramp tag for controlling translation speed , comprising:making a rare codon table according to a host cell;converting DNA sequence of a target gene into codons;analyzing frequency and position at which rare codons in the rare codon table appear in an open reading frame (ORF) of the target gene; andcollecting and arranging the rare codons.2. The method of claim 1 , wherein the collecting of the rare codons is performed by analyzing frequency of the codons and the number of isoacceptor tRNA genes.3. The method of claim 2 , wherein the frequency of the codons is 0.5 to 3% claim 2 , and the number of isoacceptor tRNA genes is 0 to 2.4. The method of claim 1 , wherein in the arranging of the rare codons claim 1 , the rare codons are arranged in the order in which the rare codon appears in the ORF.5. The method of claim 1 , wherein a preferred codon is arranged between the rare codons.6E. coli. The method of claim 1 , wherein the host cell is selected from the group consisting of claim 1 , yeast claim 1 , a ...

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Номер записи: 17
21-01-2016 дата публикации

HOST CELLS AND METHODS OF USE

Номер: US20160017343A1
Автор: JIN Yonghwan, Zhu Yuan
Принадлежит: GlaxoSmithKline LLC

The present invention relates to genetically modified host cells, in particular yeast cells, comprising at least one isolated polynucleotide encoding a Killer Expression protease (Kex2p) or a fragment and/or variant thereof which has at least one Kex2p functional activity and at least one isolated polynucleotide encoding a Protein Disulfide-Isomerase (Pdi1) or a fragment and/or variant thereof which has at least one Pdi functional activity. Also provided herein are genetically modified host cells comprising at least one isolated polynucleotide encoding a Killer Expression protease (Kex2p) or a fragment and/or variant thereof which has at least one Kex2p functional activity, at least one isolated polynucleotide encoding a Protein Disulfide-Isomerase (Pdi1) or a fragment and/or variant thereof which has at least one Pdi1 functional activity and at least one isolated polynucleotide encoding a Endoplasmic Reticulum Oxidoreductin (Ero1) or a fragment and/or variant thereof which has at least one Ero1 functional activity.

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Номер записи: 18
18-01-2018 дата публикации

L-ARABINOSE ASSIMILATION PATHWAY AND USES THEREOF

Номер: US20180016586A1
Автор: BERNARD RÉMI, Joseph Pascale, Leonetti Jean-Paul, Zigha Assia
Принадлежит:

The present invention relates to a new L-arabinose assimilation pathway and uses thereof. In particular, the present invention relates to polypeptides exhibiting L-arabinose isomerase, L-ribulokinase or L-ribulose-5-phosphate-4-epimerase activity, and recombinant host cells expressing said polypeptides. The present invention also relates to a method of producing a fermentation product, preferably ethanol, from an arabinose containing substrate, using a polypeptide or a host cell of the invention. 121-. (canceled)22. A recombinant host cell comprising a nucleic acid construct , an expression cassette or a vector comprising:a nucleic acid sequence encoding a polypeptide comprising an amino acid sequence having at least 73% identity to SEQ ID NO: 5 and exhibiting L-ribulose-5-phosphate 4 epimerase activity, or a functional fragment thereof, and/ora nucleic acid sequence encoding a polypeptide comprising an amino acid sequence having at least 72% identity to SEQ ID NO: 1 and exhibiting L-arabinose isomerase activity, or a functional fragment thereof, and/ora nucleic acid sequence encoding a polypeptide comprising an amino acid sequence having at least 73% identity to SEQ ID NO: 3 and exhibiting L-ribulokinase activity, or a functional fragment thereof.23. The recombinant host cell according to claim 22 , wherein the recombinant nucleic acid construct claim 22 , expression cassette or vector comprises a nucleic acid sequence encoding a polypeptide comprising an amino acid sequence having at least 75 claim 22 , 80 claim 22 , 90 claim 22 , 95 claim 22 , 98 claim 22 , 99% identity to SEQ ID NO: 5 and exhibiting L-ribulose-5-phosphate 4 epimerase activity claim 22 , or a functional fragment thereof.24. The recombinant host cell according to claim 22 , wherein the recombinant nucleic acid construct claim 22 , expression cassette or vector comprises a nucleic acid sequence encoding a polypeptide comprising the amino acid sequence of SEQ ID NO: 5.25. The recombinant host cell ...

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Номер записи: 19
21-01-2021 дата публикации

XYLOSE METABOLIZING YEAST

Номер: US20210017526A1
Автор: Jackson Christopher, Satory Dominik, Xu Haowen
Принадлежит:

Described herein are microorganisms, in particular yeast, which have been transformed with one or more expression construct(s) for i) the overexpression of the native genes encoding xylulose kinase (XKS1), transaldolase (TAL1), transketolase 1 (TKL1) and transketolase 2 (TKL2) and ii) the expression of a functional heterologous gene encoding a xylose isomerase (XI), where the xylose isomerase (XI) gene is derived from a microorganism selected from the group consisting of and . Also described herein are expression constructs, methods for fermenting pentose sugars using the microorganisms and methods for producing such microorganisms. 1. A microorganism which has been transformed with one or more expression construct(s) fori) the overexpression of native genes encoding xylulose kinase (XKS1), transaldolase (TAL1), transketolase 1 (TKL1) and transketolase 2 (TKL2) and{'i': Thermotoga neapolitana, Anditalea andensis', 'Clostridium clariflavum., 'ii) the expression of a functional heterologous gene encoding a xylose isomerase (XI), wherein the xylose isomerase (XI) gene is derived from a microorganism selected from the group consisting of and'}2. The microorganism according to claim 1 , wherein the xylose isomerase (XI) is encoded by a nucleic acid sequence having at least 66% sequence identity to SEQ ID No 21 claim 1 , SEQ ID No 5 or SEQ ID No 25.3. The microorganism according to claim 1 , wherein the xylose isomerase (XI) is represented by an amino acid sequence having at least 80% sequence identity to SEQ ID No 22 claim 1 , SEQ ID No 6 or SEQ ID No 26.4. The microorganism according to claim 1 , wherein the xylulose kinase (XKS1) is encoded by a nucleic acid sequence having at least 80% sequence identity to SEQ ID No 74 claim 1 , the transaldolase (TAL1) is encoded by a nucleic acid sequence having at least 80% sequence identity to SEQ ID No 77 claim 1 , the transketolase 1 (TKL1) is encoded by a nucleic acid sequence having at least 80% sequence identity to SEQ ID No ...

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Номер записи: 20
25-01-2018 дата публикации

METHOD AND DEVICE FOR THE BIOTECHNOLOGICAL REDUCTION OF SUGARS IN FRUIT EDUCTS FOR THE PURPOSE OF OBTAINING REDUCED-SUGAR FRUIT PRODUCTS

Номер: US20180020702A1
Автор: JAEGER Astrid, LOETZBEYER Thomas, WESTERMEIER Rosina
Принадлежит: GUSTAV LERMER GMBH & CO KG

An inventive method and a device for the biotechnological reduction of sugar substances in fruit educts for the purpose of obtaining low-sugar fruit products characterized by enzymatic and/or fermentative reaction processes. Said method is characterized by a closed-loop control process, by means of which the pH value in the low-sugar fruit product is adjusted to a predetermined higher value, as compared to the pH value in the fruit educt, in such a way 2. Method claim 1 , as claimed in claim 1 , characterized in that in the case of fermentatively formed sugar alcohols claim 1 , the resulting low pH value correlates linearly to the % by weight fraction of the sugar alcohols in such a way that claim 1 , for example claim 1 ,at 1.0% by weight of fermentatively formed sugar alcohols, the pH value increase turns out to be less by 0.1 pH units, andat 2.0% by weight of fermentatively formed sugar alcohols, the pH value increase turns out to be less by 0.2 pH units, andat 3.0% by weight of fermentatively formed sugar alcohols, the pH value increase turns out to be less by 0.3 pH units.3. Method claim 1 , as claimed in claim 1 , characterized by anenzymatic conversion of sucrose into glucose and fructose by means of invertase; and/orenzymatic conversion of fructose into glucose by means of glucose isomerase.4. Method claim 1 , as claimed in claim 1 , characterized by an 'with simultaneous use of catalase to convert the resulting hydrogen peroxide into water and oxygen.', 'enzymatic degradation of glucose to form gluconic acid and hydrogen peroxide by means of glucose oxidase'}5. Method claim 4 , as claimed in claim 4 , characterized in that during the enzymatic reaction processes by means of glucose oxidase and catalase claim 4 , the required oxygen is supplied claim 4 , wherein the oxygen supply is adjusted preferably to saturations between 5% and 60% claim 4 , in particular claim 4 , between 10% and 40% claim 4 , even more preferably between 30% and less than 40%.6. Method ...

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Номер записи: 21
10-02-2022 дата публикации

Compositions and methods for converting styrene to biodegradable alternatives

Номер: US20220042025A1
Автор: Aarati Pokharel, Alec Brewer, Annabel Wright, Keith Kozminski, Kobe Rogers, Mark Kester, Simonne Guenette
Принадлежит: UNIVERSITY OF VIRGINIA PATENT FOUNDATION

Provided are nucleic acids and vectors that collectively encode various gene products related to converting styrene to polyhydroxybutyrate (PHB). In some embodiments, the nucleic acids and vectors collectively encode a styrene monooxygenase polypeptide, a flavin reductase polypeptide, a styrene-oxide isomerase polypeptide, and a phenylacetaldehyde dehydrogenase polypeptide, an acetyl-CoA C-acetyltransferase polypeptide, a 3-ketoacyl-ACP reductase polypeptide, a class I poly(R)-hydroxyalkanoic acid synthase polypeptide, and optionally an influx porin polypeptide. Also provided are systems and methods for producing PHB from styrene, methods and systems for remediating polystyrene waste. In some embodiments, the systems are in vivo systems.

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Номер записи: 22
28-01-2021 дата публикации

NUCLEIC ACID ENCODING AN ISOMERASE AND USES THEREOF

Номер: US20210024914A1
Автор: IYAPPAN Saravanakumar, Pandey Banibrata, VENKATA NARAYANAN Karthikeyan
Принадлежит: PETIVA PRIVATE LIMITED

The present invention provides for a nucleic acid encoding an isomerase and uses of the isomerase for bioconversion of sugar substrates. The invention represents an advancement in the field of enzyme engineering and discloses a modified nucleic acid for achieving optimum expression of a protein having isomerase activity in a heterologous host. The invention also discloses vectors carrying the modified nucleic acid and recombinant host cells carrying the vectors. The invention also discloses the process for producing a recombinant host cell, process for production of the recombinant enzyme and the process for bioconversion of sugars into their respective isomers using the recombinant protein. 1. A modified nucleic acid comprising the nucleotide sequence of SEQ ID NO: 1 , wherein the nucleic acid encodes a polypeptide having isomerase activity in a prokaryotic host cell.2. A vector comprising the nucleic acid as claimed in claim 1 , wherein the modified nucleic acid is operably linked to a T7 promoter.3. The vector as claimed in claim 2 , wherein the vector is selected from a group comprising pET11 vector and pET23 vector.4. The vector as claimed in claim 3 , wherein the pET11 vector comprises the nucleotide sequence of SEQ ID NO: 3 and the pET23 vector comprises the nucleotide sequence of SEQ ID NO: 4.5. A recombinant prokaryotic host cell comprising the vector as claimed in .6Escherichia coli. The recombinant host cell as claimed in claim 5 , wherein the host cell is JM 109.7. A process for producing a recombinant host cell capable of expressing a polypeptide having isomerase activity claim 5 , the said process comprising the steps of:a. constructing a recombinant vector harbouring the nucleic acid of SEQ ID NO: 1, wherein the nucleic acid is operably linked to a T7 promoter; andb. transforming a prokaryotic host cell with the recombinant vector to obtain a recombinant host cell.8. The process as claimed in claim 7 , wherein the vector is selected from a group ...

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Номер записи: 23
04-02-2016 дата публикации

Process for the production of hyaluronic acid in escherichia coli or bacillus megaterium

Номер: US20160032337A1
Автор: Alessandro Negro, Sonia Bisicchia, Vincenza Corsa
Принадлежит: Fidia Farmaceutici SpA

A method of producing hyaluronic acid (HA) in Escherichia coli and Bacillus megaterium through episomal plasmid vectors wherein the gene is under the control of strong promoter T7, preferably under the control of strong promoter T7 of bacteriophage T7, and a system for the selection of stable bacterial strains producing high levels of hyaluronic acid, are provided.

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Номер записи: 24
30-01-2020 дата публикации

HIGH TEMPERATURE SEED GERMINATION

Номер: US20200032287A1
Автор: COPPOOLSE Eric Roland, POST Miriam
Принадлежит:

The present invention relates to a seed comprising in its genome a modified NXS gene and/or modified regulatory sequences thereof. The modified NXS gene and/or modified regulatory sequences thereof provides the seed with the capability to germinate at a high temperature as compared to a wild type seed not having the modified NXS gene. The modification to the gene and/or its regulatory sequences may lead to the expression of the NXS gene being substantially reduced or prevented. In addition to or alternatively, the seed can have a reduced level, reduced activity or complete absence of NXS protein. The modified NXS gene may for example comprise a premature stop codon and/or encode an NXS protein that comprises one or more amino acid substitutions. 120-. (canceled)21Lactuca sativa. A lettuce seed () comprising its genome a modified NXS gene , the wild type of which is identified in SEQ ID No. 1 , encoding the wherein the modified NXS gene encodes an NXS protein that comprises one or more amino acid substitutions.22. The lettuce seed as claimed in claim 21 , wherein a conserved residue of the encoded NXS protein of SEQ ID No. 2 is substituted.23. The lettuce seed as claimed in claim 22 , wherein the conserved residue is a proline residue which is substituted with a serine residue claim 22 , in particular proline at position 212 in the encoded protein of SEQ ID No. 2 is substituted with serine as a result of a C>T SNP at position 3518 of SEQ ID No. 1.24. The lettuce seed as claimed in claim 22 , wherein the conserved residue is a tryptophan residue which is substituted with any other amino acid resulting in a non-conservative amino acid change claim 22 , in particular tryptophan at position 175 of the encoded NXS protein of SEQ ID No. 2.2540-. (canceled) This application is a continuation-in-part application of International Patent Application Serial No. PCT/EP2015/071082 filed Sep. 15, 2015, which published as PCT Publication No. WO 2016/041952 on Mar. 24, 2016, which ...

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Номер записи: 25
05-02-2015 дата публикации

ENGINEERED PROTEINS WITH A PROTEASE CLEAVAGE SITE

Номер: US20150037868A1
Автор: Blake William Jeremy, Cunningham Drew S.
Принадлежит: GreenLight Biosciences, Inc.

Various aspects and embodiments herein relate to recombinant proteins with at least one protease recognition sequence that can be inactivated by a cognate protease and methods of preparing such proteins. In some embodiments, recombinant phosphoglucose isomerase (Pgi) proteins are provided. In other embodiments, recombinant phosphotransacetylase (Pta) proteins are provided. In yet other embodiments, recombinant transketolase A (TktA) proteins are provided. 1. A recombinant phosphoglucose isomerase protein with a protease recognition sequence located between two amino acids of the wild-type protein.2Armillaria mellea. The recombinant protein of claim 1 , wherein the protease recognition sequence is the protease recognition sequence recognized by a protease selected from the group consisting of alanine carboxypeptidase claim 1 , astacin claim 1 , bacterial leucyl aminopeptidase claim 1 , cancer procoagulant claim 1 , cathepsin B claim 1 , clostripain claim 1 , cytosol alanyl aminopeptidase claim 1 , elastase claim 1 , endoproteinase Arg-C claim 1 , enterokinase claim 1 , gastricsin claim 1 , gelatinase claim 1 , Gly-X carboxypeptidase claim 1 , glycyl endopeptidase claim 1 , human rhinovirus 3C protease claim 1 , hypodermin C claim 1 , Iga-specific serine endopeptidase claim 1 , leucyl aminopeptidase claim 1 , leucyl endopeptidase claim 1 , lysC claim 1 , lysosomal pro-X carboxypeptidase claim 1 , lysyl aminopeptidase claim 1 , methionyl aminopeptidase claim 1 , myxobacter claim 1 , nardilysin claim 1 , pancreatic endopeptidase E claim 1 , picornain 2A claim 1 , picornain 3C claim 1 , proendopeptidase claim 1 , prolyl aminopeptidase claim 1 , proprotein convertase I claim 1 , proprotein convertase II claim 1 , russellysin claim 1 , saccharopepsin claim 1 , semenogelase claim 1 , T-plasminogen activator claim 1 , thrombin claim 1 , tissue kallikrein claim 1 , tobacco etch virus (TEV) claim 1 , togavirin claim 1 , tryptophanyl aminopeptidase claim 1 , U-plasminogen ...

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Номер записи: 26
05-02-2015 дата публикации

ENZYME CATALYSTS FOR DIELS-ALDER REACTIONS

Номер: US20150037870A1
Автор: Baker David, Saint-Clair Jennifer, Siegel Justin, Zanghellini Alexandre
Принадлежит: UNIVERSITY OF WASHINGTON

The present invention provides enzyme catalysts for Diels-Alder reactions, including intermolecular Diels-Alder reactions, as well as protein scaffolds for making such enzyme catalysts. In other aspects, the invention provides methods of making the enzyme catalysts, including by de novo computational design. The present invention thereby provides enzyme catalysts capable of catalyzing a desired Diels-Alder reaction, including with a specified or desired stereo-selectivity. 1. An non-naturally occurring enzyme catalyst of a Diels-Alder reaction , the enzyme comprising a non-immunoglobulin scaffold , and an active site pocket that accommodates a Diels-Alder reaction.2Loligo vulgarisPseudomonas putida. The enzyme of claim 1 , wherein the enzyme comprises a protein scaffold corresponding to diisopropylfluorophosphosphatase from claim 1 , or a homolog thereof claim 1 , or ketosteroid isomerase from claim 1 , or a homolog thereof.3. The enzyme of claim 2 , wherein the active site comprises amino acid side chains that stabilize the Diels-Alder transition state by electron-withdrawing and/or electron-donating effects.4. The enzyme of claim 3 , wherein the active site comprises an amino acid side chain that stabilizes the Diels-Alder transition state by accepting a hydrogen bond from the diene portion of the transition state.5. The enzyme of claim 3 , wherein the active site comprises an amino acid side chain that stabilizes the Diels-Alder transition state by donating a hydrogen bond to the dienophile portion of the transition state.6. The enzyme of claim 1 , wherein the enzyme contains a substrate-binding pocket having a hydrophobic and/or polar and/or charged interface that is complementary to the Diels-Alder substrates.7. The enzyme of claim 4 , wherein the hydrogen-bond acceptor at the position corresponding to position 195 of SEQ ID NO:2.8. The enzyme of claim 7 , wherein the hydrogen bond acceptor is a side chain of asparagine or glutamine.9. The enzyme of claim 5 , ...

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Номер записи: 27
11-02-2016 дата публикации

PROTEIN HAVING XYLOSE ISOMERASE ACTIVITY AND USE OF SAME

Номер: US20160040151A1
Автор: IMAMURA Chie, ISHIDA Nobuhiro, Katahira Satoshi, NAGURA Risa, Onishi Toru, Tada Nobuki, Tokuhiro Kenro, Yasutani Noriko
Принадлежит:

A eukaryotic cell having xylose utilization ability. Provided is a protein that has xylose isomerase activity and has an amino acid sequence including, when aligned with an amino acid sequence expressed by SEQ ID NO:1, the 1st to 6th motifs expressed respectively by SEQ ID NOs:2 to 7 from the N-terminus side in the order described, and having, in place of asparagine (N) in an amino acid sequence of the 6th motif, another amino acid. 1. A protein that has xylose isomerase activity and has an amino acid sequence including , when aligned with an amino acid sequence expressed by SEQ ID NO:1 , the following 1st to 6th motifs from the N-terminus of the protein in the order described , and having , in place of asparagine (N) in an amino acid sequence of the 6th motif , an amino acid selected from the group consisting of cysteine , threonine , valine , and alanine: 'wherein X represents a naturally occurring amino acid,', '1 st motif: FXXXXKXXXXXXXXHDXD (SEQ ID NO:2)'} 'wherein X represents a naturally occurring amino acid,', '2nd motif: XXXXXXXWGGREGYXXLXNT (SEQ ID NO:3)'} 'wherein X represents a naturally occurring amino acid,', '3rd motif: XXXXXXXXEPKPXEPXXHQYDXD (SEQ ID NO:4)'} 'wherein X represents a naturally occurring amino acid,', '4th motif: LXXXXXXNXEXNHXXLXXHXXXH (SEQ ID NO:5)'} 'wherein X represents a naturally occurring amino acid, and', '5th motif: XGSXDXNXGXXXXGWDXDXXP (SEQ ID NO:6)'} 'wherein X represents a naturally occurring amino acid.', '6th motif: GGXNFDXKXRR (SEQ ID NO:7)'}2. The protein according to claim 1 , wherein:the 1st motif is expressed by FXXXXKXGXXXXXFHDXD (SEQ ID NO:8),the 2nd motif is expressed by XXXXXVFWGGREGYXXLLNT (SEQ ID NO:9),the 3rd motif is expressed by XXXXXFXIEPKPXEPXXHQYDXD (SEQ ID NO:10),the 4th motif is expressed by LXXXFKXNXEXNHXXLAGHXXXH (SEQ ID NO:11),the 5th motif is expressed by XGSXDXNXGXXXXGWDTDXFP (SEQ ID NO:12), andthe 6th motif is expressed by GGXNFDXKXRR (SEQ ID NO:13).3. The protein according to claim 1 , wherein: ...

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Номер записи: 28
11-02-2016 дата публикации

CHIMERIC POLYPEPTIDES HAVING XYLOSE ISOMERASE ACTIVITY

Номер: US20160040152A1
Автор: Froehlich Allan, Henningsen Brooks
Принадлежит:

There is provided chimeric polypeptides capable of converting xylose to xylulose, engineered host cells that express the chimeric polypeptides, methods of creating chimeric polypeptides, and methods of fermenting cellulosic biomass to produce biofuels, including ethanol. 1. A polypeptide having a xylose isomerase activity , the polypeptide comprising an amino acid sequence having at least 90% , 95% , 98% , 99% or 100% sequence identity with an amino acid sequence of SEQ ID NOs: 1 , 3 , 5 , 7 , 9 , 25 or 27.2. A polypeptide having a xylose isomerase activity , the polypeptide comprising a C-terminal region and an N-terminal region , wherein the C-terminal region of the polypeptide comprises at least 5 contiguous amino acids from the amino acid sequence of SEQ ID NO:13 and the N-terminal region of the polypeptide comprises at least 5 contiguous amino acids from an amino acid sequence of SEQ ID NOs: 11 , 15 , 17 , 23 or combinations thereof.3. The polypeptide of claim 2 , wherein the N-terminal region of the polypeptide comprises at least 5 contiguous amino acids from an amino acid sequence of SEQ ID NOs: 11 claim 2 , 23 or a combination thereof.4. The polypeptide of claim 2 , wherein the N-terminal region of the polypeptide comprises at least 5 contiguous amino acids from the amino acid sequence of SEQ ID NOs: 11 claim 2 , 17 claim 2 , 15or combinations thereof.5. A polypeptide having a xylose isomerase activity claim 2 , the polypeptide comprising a C-terminal region and an N-terminal region claim 2 , wherein the C-terminal region comprises at least 5 contiguous amino acids from the amino acid sequence of SEQ ID NO:15 and the N-terminal region comprises at least 5 contiguous amino acids from an amino acid sequence of SEQ ID NOs: 19 claim 2 , 21 claim 2 , 23 or combinations thereof.6. The polypeptide of claim 1 , wherein the polypeptide comprises:a. the amino acids VXW[GP]GREG[YSTA] present at positions 188-196, wherein “X” is any amino acid and wherein amino acids in ...

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Номер записи: 29
11-02-2016 дата публикации

MUTATIONS IN IRON-SULFUR CLUSTER PROTEINS THAT IMPROVE XYLOSE UTILIZATION

Номер: US20160040153A1
Автор: Covalla Sean, Froehlich Allan, Henningsen Brooks
Принадлежит:

There is provided an engineered host cells comprising (a) one or more mutations in one or more endogenous genes encoding a protein associated with iron metabolism; and (b) at least one gene encoding a polypeptide having xylose isomerase activity, and methods of their use thereof. 1. A recombinant yeast cell comprising (a) at least one heterologous gene encoding a protein associated with iron metabolism and/or one or more mutations in one or more endogenous gene encoding a protein associated with iron metabolism; and (b) at least one heterologous gene encoding a polypeptide having xylose isomerase activity.2. The recombinant yeast cell of claim 1 , wherein the one or more mutations in an endogenous gene is in a gene of ISU1 claim 1 , YFH1 claim 1 , NFS1 claim 1 , AFT1 claim 1 , AFT2 claim 1 , YAP5 claim 1 , FRA1 claim 1 , FRA2 claim 1 , GREX3 claim 1 , GREX4 claim 1 , CCC1 claim 1 , or any combination thereof.3. The recombinant yeast cell of claim 2 , wherein the recombinant yeast cell comprises one or more mutations in the endogenous ISU1 gene that results in a polypeptide comprising at least one amino acid substitution selected from the group consisting of D71N claim 2 , D71G claim 2 , and S98F claim 2 , wherein the position of the substitution is relative to the amino acid positions of SEQ ID NO:29.4. The recombinant yeast cell of claim 2 , wherein the recombinant yeast cell comprises one or more mutations in the endogenous YFH1 gene that results in a polypeptide comprising a T163P substitution claim 2 , wherein the position of the substitution is relative to the amino acid positions of SEQ ID NO:31.5. The recombinant yeast cell of claim 2 , wherein the recombinant yeast cell comprises one or more mutations in the endogenous NFS1 gene that results in a polypeptide comprising at least one amino acid substitution selected from the group consisting of L115W and E458D claim 2 , wherein the position of the substitution is relative to the amino acid positions of SEQ ID ...

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Номер записи: 30
11-02-2016 дата публикации

Microorganisms of corynebacterium which can utilize xylose and method for producing l-lysine using same

Номер: US20160040200A1
Автор: Chang Gyeom Kim, Hyung Joon Kim, Jin Seok Sung, Jun Ok Moon, Kwang Ho Lee, Kyung Han Lee, Lan Huh, So Yeon Rah
Принадлежит: CJ CHEILJEDANG CORP

The present invention relates to microorganisms of corynebacterium which can utilize xylose and to a method for producing L-lysine using same. More particularly, the present invention relates to microorganisms of corynebacterium which are modified, in which genes encoding xylose isomerase and xylulokinase which are xylose synthases are introduced to express the xylose synthase. The present invention also relates to a method for producing L-lysine, comprising a step of culturing the modified microorganisms of corynebacterium using xylose as a carbon source, and recovering L-lysine from the culture.

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Номер записи: 31
09-02-2017 дата публикации

SYNTHETIC METHANOTROPHIC AND METHYLOTROPHIC MICROORGANISMS

Номер: US20170037438A1
Автор: CLARKE Elizabeth, GREENFIELD Derek, HELMAN Noah
Принадлежит: INDUSTRIAL MICORBES, INC.

Provided herein are non-naturally occurring microbial organisms comprising a methane-oxidizing metabolic pathway. The invention additionally comprises non-naturally occurring microbial organisms comprising pathways for the production of chemicals. The invention additionally provides methods for using said organisms for the production of chemicals. 1. A synthetic microorganism , wherein said synthetic microorganism comprises a natural methanol-consuming microorganism and one or more genetic modifications that improve the production of a chemical.2. (canceled)3. A synthetic microorganism comprising a natural non-methanol-consuming microorganism and one or more genetic modifications that allow said synthetic microorganism to oxidize methanol.4Escherichia coli, Bacillus subtilis, Pseudomonas putida, Saccharomyces cerevisiae, Corynebacterium glutamicum Klebsiella oxytoca, Anaerobiospirillum succiniciproducens, Actinobacillus succinogenes, Mannheimia succiniciproducens, Rhizobium etli, Gluconobacter oxydans, Zymomonas mobilis, Lactococcus lactis, Lactobacillus plantarum, Streptomyces coelicolor, Clostridium acetobutylicum, Pseudomonas fluorescens, Schizosaccharomyces pombe, Kluyveromyces lactis, Kluyveromyces marxianus, Aspergillus terreusAspergillus niger.. The synthetic microorganism of claim 3 , wherein the natural non-methanol-consuming microorganism is selected from the group consisting of claim 3 , and5Corynebacterium glutamicumEscherichia coli.. The synthetic microorganism of claim 4 , wherein the natural non-methanol-consuming microorganism is not or6. The synthetic microorganism of claim 3 , further comprising exogenous polynucleotides claim 3 , wherein said exogenous polynucleotides encode enzymes selected from the group consisting of methanol dehydrogenase (EC 1.1.1.224 or 1.1.99.37 or 1.1.2.7) claim 3 , alcohol dehydrogenase (EC 1.1.1.1) claim 3 , 3-hexulose-6-phosphate synthase (EC 4.1.2.43) and 6-phospho-3-hexuloisomerase (EC 5.3.1.27).7. The synthetic ...

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Номер записи: 32
08-02-2018 дата публикации

Electrochemical Bioreactor Module and Engineered Metabolic Pathways for 1-Butanol Production with High Carbon Efficiency

Номер: US20180037914A1
Автор: Armiger William B., Dodds David R., Koffas Mattheos
Принадлежит: Biocheminsights, Inc.

A combination of an electrochemical device for delivering reducing equivalents to a cell, and engineered metabolic pathways within the cell capable of utilizing the electrochemically provided reducing equivalents is disclosed. Such a combination allows the production of commodity chemicals by fermentation to proceed with increased carbon efficiency. 1. A system for 1-butanol production , comprising:an electrochemical bioreactor module for providing reducing equivalents;a first engineered pathway for producing 1-butanol from acetyl-CoA; anda second engineered pathway for recovering carbon as formate from pyruvate, and converting the recovered formate to fructose-6-phosphate;wherein the reducing equivalents are provided to one or more redox enzymes in the first and/or second engineered pathways; and wherein optionally the first and second engineered pathways are present in an engineered cell.2. The system of wherein the first engineered pathway comprises acetyl-CoA acetyltransferase (AtoB claim 1 , EC 2.3.1.9) claim 1 , 3-hydroxybutyryl-CoA dehydrogenase (Hbd claim 1 , EC 1.1.1.157) claim 1 , 3-hydroxybutyryl-CoA dehydratase (Crt claim 1 , EC 4.2.1.5) claim 1 , trans-enoyl-CoA reductase (Ter claim 1 , EC 1.3.1.38) and aldehyde/alcohol dehydrogenase (AdhE2 claim 1 , EC 1.2.157/EC 1.1.1.1).3. The system of or wherein the second engineered pathway comprises pyruvate:formate lyase (Pfl claim 1 , EC 2.3.1.54) claim 1 , formaldehyde dehydrogenase (Fld claim 1 , EC 1.2.1.46) claim 1 , hexulose-6-phosphate synthase (HPS claim 1 , EC 4.1.2.43) claim 1 , and 6-phospho-3-hexuloisomerase (HPI claim 1 , EC 5.3.1.27).4. The system of or wherein in the engineered cell claim 1 , the endogenous pyruvate dehydrogenase (Pdh claim 1 , EC 1.2.4.1) has been disabled claim 1 , deleted or otherwise rendered non-functional.5. The system of or wherein in the engineered cell claim 1 , the endogenous fumarate reductase (FrdBC claim 1 , EC 1.3.1.6) claim 1 , lactate dehydrogenase (Ldh claim 1 , ...

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Номер записи: 33
24-02-2022 дата публикации

GENETICALLY MODIFIED MICROORGANISM AND METHOD BOTH FOR PRODUCING NICOTINAMIDE DERIVATIVE, AND VECTOR FOR USE IN SAME

Номер: US20220056458A1
Автор: ISHII Jun, KANOU Masanobu, Kondo Akihiko, Nakajima Ryota, Shoji Shinichiro, Watanabe Hidekazu
Принадлежит:

Provided is a technique for synthesizing a nicotinamide derivative (NAm derivative) such as a nicotinamide mononucleotide (NMN) with high efficiency. A genetically modified microorganism is used, which can express, as nicotinamide phosphoribosylt ransferase (NAMPT), NAMPT having a conversion efficiency of 5-folds or more that of human NAMPT. 1. A recombinant microorganism for producing a nicotinamide derivative , wherein the microorganism has been engineered to express a nicotinamide phosphoribosyl transferase (NAMPT) , which converts nicotinamide and phosphoribosyl pyrophosphate into nicotinamide mononucleotide , and/or has been transformed with a vector carrying a nucleic acid encoding the amino acid sequence of the NAMPT , wherein the conversion efficiency of the NAMPT from nicotinamide to nicotinamide mononucleotide is five times or more of the conversion efficiency of a human NAMPT.2. The recombinant microorganism according to claim 1 , wherein the NAMPT is composed of a polypeptide with a sequence homology of 80% or more with the amino acid sequence represented by SEQ ID NO:3 or SEQ ID NO:6.3. The recombinant microorganism according to claim 1 , wherein the microorganism has been engineered to express a niacin transporter claim 1 , which promotes cellular uptake of nicotinic acid and/or nicotinamide claim 1 , and/or has been transformed with a vector carrying a nucleic acid encoding the amino acid sequence of the niacin transporter claim 1 , wherein the niacin transporter increases the intracellular uptake efficiency of nicotinic acid and/or nicotinamide by the host microorganism by 1.1 times or more.4. The recombinant microorganism according to claim 3 , wherein the niacin transporter is composed of a polypeptide with a sequence homology of 80% or more with the amino acid sequence represented by SEQ ID NO:9 or SEQ ID NO:12.5. The recombinant microorganism according to claim 1 , wherein the microorganism has been engineered to express a nicotinamide derivative ...

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Номер записи: 34
12-02-2015 дата публикации

METHODS FOR INCREASING PRODUCTION OF 3-METHYL-2-BUTENOL USING FUSION PROTEINS

Номер: US20150044747A1
Автор: Chou Howard, Keasling Jay D.
Принадлежит: The Regents of the University of California

The invention relates, in part, to nucleic acid constructs, genetically modified host cells and methods employing such constructs and host cells to increase the production of 3-methyl-2-butenol from IPP. Thus, in some aspects, the invention provides a genetically modified host cell transformed with a nucleic acid construct encoding a fusion protein comprising a phosphatase capable of catalyzing the dephosphorylation of dimethylallyl diphosphate (DMAPP) linked to an IPP isomerase capable of converting IPP to DMAPP, wherein the nucleic acid construct is operably linked to a promoter. In some embodiments, the genetically modified host cell further comprises a nucleic acid encoding a reductase that is capable of converting 3-methyl-2-butenol to 3-methyl-butanol. In some embodiments, the reductase is encoded by a nucleic acid construct introduced into the cell. In some embodiments, the IPP isomerase is a Type I isomerase. In some embodiments, the IPP isomerase is a Type II isomerase. In some embodiments, the host cell is selected from a group of taxonimcal classes consisting of 20 , and taxonomical classes. In some embodiments, the host cell is an cell. In some embodiments, the host cell is a fungal cell, such as a yeast cell. In some embodiments, the yeast cell is a sp. cell. In some embodiments, the host cell is an algal, insect or mammalian cell line. In some embodiments, the phosphatase is nudB from . In some embodiments, the IPP isomerase is encoded by an idi gene from or idil gene from 1. A genetically modified host cell transformed with a nucleic acid construct encoding a fusion protein comprising a phosphatase capable of catalyzing the dephosphorylation of dimethylallyl diphosphate (DMAPP) linked to an IPP isomerase capable of converting IPP to DMAPP , wherein the nucleic acid construct is operably linked to a promoter.2. The genetically modified host cell of claim 1 , wherein the genetically modified host cell further comprises a nucleic acid encoding a ...

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Номер записи: 35
07-02-2019 дата публикации

Novel nucleic acid molecules

Номер: US20190040378A1
Автор: Aleksandra KOWALCZYK, Katja FIEDLER, Mariola Fotin-Mleczek, Regina HEIDENREICH
Принадлежит: CureVac AG

The present invention provides novel artificial nucleic acid molecules encoding at least one antigenic peptide or protein and at least one additional sequence preferably targeting the antigenic peptides or proteins to cellular compartments of interest. Further, the invention provides (pharmaceutical) compositions or vaccines and kits comprising said nucleic acid molecules. The nucleic acid molecules, (pharmaceutical) compositions or vaccines and kits are useful for treating a variety of diseases such as cancer, infectious diseases, autoimmune diseases, allergies or graft-versus host disease.

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Номер записи: 36
07-02-2019 дата публикации

RECOMBINANT YEAST AND A METHOD FOR PRODUCING ETHANOL USING THE SAME

Номер: US20190040379A1
Автор: Hirao Rie, Ito Junji, Onishi Toru, Tada Nobuki
Принадлежит: TOYOTA JIDOSHA KABUSHIKI KAISHA

An acetic acid metabolizing ability of a recombinant yeast strain having xylose-metabolizing ability is to be improved. In such a recombinant yeast strain having xylose-metabolizing ability, the acetaldehyde dehydrogenase gene has been introduced and a gene encoding NADH dehydrogenase involved in reoxidation of cytoplasmic NADH on the mitochondrial outer membrane has been suppressed. 1. A recombinant yeast strain having xylose-metabolizing ability comprising the acetaldehyde dehydrogenase gene introduced thereinto , wherein a gene encoding NADH dehydrogenase involved in reoxidation of cytoplasmic NADH on the mitochondrial outer membrane is suppressed.2. The recombinant yeast strain according to claim 1 , wherein the gene encoding NADH dehydrogenase encodes a protein (a) or (b) below:(a) a protein comprising the amino acid sequence as shown in SEQ ID NO: 2 or 4; or{'sup': '+', '(b) a protein comprising an amino acid sequence exhibiting 70% or higher identity with the amino acid sequence as shown in SEQ ID NO: 2 or 4 and having enzymatic activity of catalyzing a reaction of converting NADH into NAD.'}3. The recombinant yeast strain according to comprising a xylose isomerase gene introduced thereinto.4. The recombinant yeast strain according to claim 3 , wherein the xylose isomerase gene encodes a protein (a) or (b) below:(a) a protein comprising the amino acid sequence as shown in SEQ ID NO: 6; or(b) a protein comprising an amino acid sequence exhibiting 70% or higher identity with the amino acid sequence as shown in SEQ ID NO: 6 and having enzymatic activity of converting xylose into xylulose.5. The recombinant yeast strain according to claim 1 , which further comprises a xylulokinase gene introduced thereinto.6. The recombinant yeast strain according to claim 1 , which comprises a gene encoding an enzyme selected from a group of enzymes constituting a non-oxidative process in the pentose phosphate pathway introduced thereinto.7. The recombinant yeast strain ...

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Номер записи: 37
16-02-2017 дата публикации

METHODS OF USING CYCLOOXYGENASE-PROSTACYCLIN SYNTHASE FUSION GENE

Номер: US20170042985A1
Автор: Chen Zhiqiang, DIXON Richard A.F., RUAN Ke-He, Vanderslice Peter, Zhou Lei
Принадлежит:

An effective amount of a composition comprising (i) a plasmid having a cyclooxygenase-prostacyclin synthase fusion gene, and (ii) a carrier fluid for use in treating an individual having a vascular disease or at risk of developing a vascular disease. A composition comprising a carrier fluid; and a DNA sequence encoding for a triple catalytic enzyme, a cDNA sequence encoding for a triple catalytic enzyme, a plasmid comprising a DNA sequence encoding for a triple catalytic enzyme, a fusion gene encoding for a triple catalytic enzyme, a cyclooxygenase-prostacyclin synthase fusion gene, or combinations thereof, for use in treating an individual having a vascular disease or at risk of developing a vascular disease. 1. An effective amount of a composition comprising (i) a plasmid having a cyclooxygenase-prostacyclin synthase fusion gene , and (ii) a carrier fluid for use in treating an individual having a vascular disease or at risk of developing a vascular disease.2. The composition of wherein the vascular disease comprises: pulmonary arterial hypertension claim 1 , peripheral arterial disease claim 1 , peripheral vascular disease claim 1 , chronic obstructive pulmonary disease claim 1 , ischemia claim 1 , limb ischemia claim 1 , critical limb ischemia claim 1 , Reynaud's syndrome claim 1 , ischemic stroke claim 1 , myocardial infarction claim 1 , systemic hypertension claim 1 , stroke claim 1 , subarachnoid hemorrhage claim 1 , or combinations thereof.3. The composition of wherein the plasmid comprises a DNA sequence encoding for a triple catalytic enzyme.4. The composition of wherein the triple catalytic enzyme is characterized by a formula COX-linker-PGIS claim 3 , wherein COX comprises a cyclooxygenase (COX) amino acid sequence; PGIS is prostacyclin synthase; and the linker comprises from about 10 to about 22 amino acid residues of a transmembrane sequence; wherein the linker is disposed between the COX and PGIS claim 3 , and wherein the linker directly connects the ...

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Номер записи: 38
03-03-2022 дата публикации

Biosynthetic methods and systems for producing monosaccharides

Номер: US20220064685A1
Автор: Tahereh Karimi
Принадлежит: Cemvita Factory Inc

The present disclosure is related to biosynthetic methods of forming monosaccharides, and systems for generating the same. A benefit of the methods and systems disclosed herein can include the sustainable production of monosaccharides in an automated process. A benefit of the methods and systems herein can be the generation of monosaccharides from renewable source materials. An additional benefit of the methods and systems herein can include the use of abundant feedstocks, such as carbon dioxide, for the efficient generation of select monosaccharides for use as nutrients and for other useful applications. Another benefit of the methods and systems disclosed herein can include reduction of excess carbon dioxide from the environment.

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Номер записи: 39
14-02-2019 дата публикации

A BACTERIAL CELL FACTORY FOR EFFICIENT PRODUCTION OF ETHANOL FROM WHEY

Номер: US20190048368A1
Автор: Dantoft Shruti Harnal, Jensen Peter Ruhdal, LIU Jianming, Solem Christian
Принадлежит:

The invention relates to a method for homo-ethanol production from lactose using a genetically modified lactic acid bacterium of the invention, where the cells are provided with a substrate comprising dairy waste supplemented with an amino nitrogen source (such as acid hydrolysed corn steep liquor). The invention further relates to genetically modified lactic acid bacterium and its use for homo-ethanol production from lactose in dairy waste. The lactic acid bacterium comprises both genes (lacABCD, LacEF, lacG) encoding enzymes catalysing the lactose catabolism pathway; and transgenes (pdc and adhB) encoding enzymes catalysing the conversion of pyruvate to ethanol. Additionally a number of genes (ldh, pta and adhE) are deleted in order to maximise homo-ethanol production as compared to production of lactate, acetoin and acetate production. 1. A method for ethanol production using a genetically engineered lactic acid bacterium comprising the steps of:a. introducing a genetically modified lactic acid bacterium into an aqueous culture medium;b. incubating the culture of (a);c. recovering ethanol produced by said culture during step (b), and optionally wherein the aqueous culture medium comprises:', 'I. whey permeate or residual whey permeate, and', wherein the genetically engineered lactic acid bacterium comprises transgenes encoding:', 'i. a polypeptide having pyruvate decarboxylase (PDC) activity (EC 4.1.1.1); and', 'wherein the genome of said lactic acid bacterium comprises genes encoding polypeptides having:', 'ii. a polypeptide having alcohol dehydrogenase B activity (EC 1.1.1.1); and'}, 'iii. lactose-specific phosphotransferase system (PTS) activity (EC 2.7.1.69)', 'iv. phospho-β-D-galactosidase activity (EC 3.2.1.85)', 'v. galactose-6-phosphate isomerase activity (EC 5.3.1.26),', 'vi. D-tagatose-6-phosphate kinase activity (EC 2.7.1.114), and', 'wherein the genome of said lactic acid bacterium is deleted for genes or lacks functional genes or genes encoding ...

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Номер записи: 40
13-02-2020 дата публикации

CULTURE MODIFIED TO CONVERT METHANE OR METHANOL TO 3-HYDROXYPROPRIONATE

Номер: US20200048639A1
Автор: CLARKE Elizabeth Jane, Greenfield Derek Lorin, Helman Noah Charles, Jones Stephanie Rhianon, Zhu Baolong
Принадлежит:

Provided are engineered organisms which can convert methane or methanol to 3-hydroxypropionate. 1. A synthetic culture comprising one or more microorganisms comprising one or more modifications that improve the production of a product from a substrate , wherein the substrate comprises methane and/or methanol.2. The synthetic culture according to claim 1 , wherein the substrate comprises methane.3. The synthetic culture according to claim 2 , wherein the product comprises 3-hydroxyproprionate.4. The synthetic culture according to claim 1 , wherein the product comprises 3-hydroxyproprionate.5. The synthetic culture according to claim 1 , wherein the product comprises a substance derived from acetyl-CoA and/or malonyl-CoA.6Escherichia coli.. The synthetic culture according to claim 1 , wherein at least one of the one or more microorganisms comprises7. The synthetic culture according to claim 1 , wherein the one or more microorganisms comprises a first at least one microorganism and a second at least one microorganism claim 1 , wherein the first at least one microorganism produces methanol from methane and the second at least one microorganism produces 3-hydroxypropionate from methanol.8. The synthetic culture according to claim 1 , wherein the one or more modifications comprise exogenous polynucleotides or deletion of one or more genes.9. The synthetic culture according to claim 8 , wherein the exogenous polynucleotides encode polypeptides selected from one or more polypeptides comprising methane monooxygenase (EC 1.14.13.25) claim 8 , malonyl-CoA reductase (EC 1.2.1.75) claim 8 , acetyl-CoA carboxylase (EC 6.4.1.2) claim 8 , methanol dehydrogenase (EC 1.1.1.244 or EC 1.1.2.7) claim 8 , 3-hexulose-6-phosphate synthase (EC 4.1.2.43) claim 8 , and/or 6-phospho-3-hexuloisomerase (EC 5.3.1.27).10Bacillus methanolicus, Bacillus stearothermophilusCorynebacterium glutamicum.. The synthetic culture according to claim 9 , wherein the methanol dehydrogenase comprises a methanol ...

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Номер записи: 41
10-03-2022 дата публикации

Agent for use in the case of fructose intolerance

Номер: US20220072111A1
Автор: Daniel Henry Wyrobnik, Isaac Harry Wyrobnik
Принадлежит: VITAMERICA UG (HAFTUNGSBESCHRANKT)

There is provided a method for treating or reducing the effects of fructose intolerance and health problems associated with excessive fructose intake by administration of glucose isomerase. Other embodiments are also disclosed.

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Номер записи: 42
10-03-2022 дата публикации

RECOMBINANT YEAST AND METHOD FOR PRODUCING ETHANOL USING SAME

Номер: US20220073896A1
Автор: Hirao Rie, Onishi Toru, Tada Nobuki
Принадлежит: TOYOTA JIDOSHA KABUSHIKI KAISHA

Provided are excellent L-arabinose metabolic genes that function in yeasts. Provided is an L-arabinose metabolic gene cluster including an L-arabinose isomerase gene specified by a predetermined SEQ ID, an L-ribulokinase gene specified by a predetermined SEQ ID, and an L-ribulose-5-phosphate-4-epimerase gene specified by a predetermined SEQ ID. 1. A recombinant yeast comprising a group L-arabinose metabolic genes including an L-arabinose isomerase gene , an L-ribulokinase gene , and an L-ribulose-5-phosphate-4-epimerase gene introduced thereinto , whereinthe L-arabinose isomerase gene is a gene encoding any one of proteins (a) to (c) below:(a) a protein comprising one amino acid sequence selected from the group consisting of SEQ ID NOs: 2, 4, and 6;(b) a protein comprising an amino acid sequence having an identity of 80% or more to one amino acid sequence selected from the group consisting of SEQ ID NOs: 2, 4, and 6 and having L-arabinose isomerase activity; and(c) a protein encoded by a nucleotide sequence that hybridizes with a nucleotide sequence complementary to one nucleotide sequence selected from the group consisting of SEQ ID NOs: 1, 3, and 5 under stringent conditions and having L-arabinose isomerase activity.2. A recombinant yeast comprising a group of L-arabinose metabolic genes including an L-arabinose isomerase gene , an L-ribulokinase gene , and an L-ribulose-5-phosphate-4-epimerase gene introduced thereinto , whereinthe L-ribulokinase gene is a gene encoding any one of proteins (a) to (c) below:(a) a protein comprising one amino acid sequence selected from the group consisting of SEQ ID NOs: 8, 10, 12, 14, and 16;(b) a protein comprising an amino acid sequence having an identity of 80% or more to one amino acid sequence selected from the group consisting of SEQ ID NOs: 8, 10, 12, 14, and 16 and having L-ribulokinase activity; and(c) a protein encoded by a nucleotide sequence that hybridizes with a nucleotide sequence complementary to one nucleotide ...

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Номер записи: 43
02-03-2017 дата публикации

CRYSTALLIZED XYLOSE ISOMERASE IN PREVENTION OF THE DEVELOPMENT OF NON-ALCOHOLIC FATTY LIVER DISEASE

Номер: US20170056485A1
Автор: Missbichler Albert
Принадлежит:

The present invention relates to the composition comprising crystalline xylose-isomerase and at least one salt of a metal and/or alkaline earth metal for the treatment and prevention of non-alcoholic fatty liver disease and other fructose-related disorders. 2. The method of claim 1 , wherein the composition is administered in an enteric form.3. The method of claim 2 , wherein the enteric form is further defined as an enteric coated pellet claim 2 , enteric coated tablet claim 2 , enteric coated capsule claim 2 , enteric coated granule claim 2 , or enteric coated powder.4. The method of claim 1 , wherein the magnesium salt in the composition has a molar ratio to xylose-isomerase ranging from 5:1 to 25:1.5. The method of claim 1 , wherein the magnesium salt is MgCl claim 1 , MgSO claim 1 , MgCO claim 1 , Mg(HCO3)2 claim 1 , or Mg(CHO).6. The method of claim 1 , wherein the xylose-isomerase is present in microcapsules claim 1 , nanoparticles claim 1 , or liposomes.7Streptomyces rubiginosus.. The method of claim 1 , wherein the xylose-isomerase of microbial origin originates from8. The method of claim 1 , wherein the composition is a pharmaceutical composition claim 1 , a food supplement claim 1 , a dietetic food claim 1 , a medicinal product claim 1 , a feeding stuff claim 1 , a supplementary feeding stuff or a dietetic feeding stuff. The present invention relates to a composition for the treatment of Non-Alcoholic Fatty Liver Disease and the treatment or prevention of fructose-related disorders.Non-alcoholic fatty liver disease (NAFLD) is a rapidly-growing and mostly silent chronic liver disease characterised by the accumulation of triglycerides in hepatocytes occurring in people who consume little or no alcohol. This condition comprises a wide spectrum of histological lesions ranging from simple steatosis to non-alcoholic steatohepatitis (NASH), a parenchymal liver inflammation which can develop further to fibrosis, cirrhosis and hepatocellular carcinoma. NAFLD is ...

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Номер записи: 44
21-02-2019 дата публикации

ULTRAPURIFIED DsbA AND DsbC AND METHODS OF MAKING AND USING THE SAME

Номер: US20190056399A1
Автор: FONG Chris B., Lim Amy, Wong Marc, YEE Liliana T.
Принадлежит: Genentech, Inc.

The present invention provides methods for producing disulfide oxidoreductase A (DsbA) and disulfide oxidoreductase C (DsbC) polypeptides at very high levels of purity. Also provided are ultrapure DsbA and DsbC and methods of using same, e.g., for use in immunoassays to show removal of DsbA and DsbC from biologics produced in bacteria. 1189-. (canceled)190. A method for quantifying disulfide oxidoreductase C (Dsb C) in a sample , comprising detecting DsbC in the sample using a detection system and comparing the amount of DsbC detected in the sample with the detection of one or more concentrations of an ultrapure DsbC reference standard.191. The method of claim 190 , wherein the ultrapure DsbC reference standard comprises at least about 95% monomeric DsbC polypeptide.192. The method of claim 190 , wherein the ultrapure DsbC reference standard is prepared by the method comprisinga) adding polyethyleneimine (PEI) to a final concentration of about 0.01% to about 1.0% to a cell lysate comprising the DsbC polypeptide,b) clarifying the cell lysate by centrifugation,c) applying the clarified cell lysate comprising the DsbC polypeptide to an anion exchange chromatography material,d) eluting the DsbC polypeptide from the anion exchange chromatography material to generate an anion exchange eluate comprising the DsbC polypeptide,e) applying the anion exchange eluate comprising the DsbC polypeptide to a hydrophobic interaction chromatography (HIC) material,f) eluting the DsbC polypeptide from the HIC material to generate a HIC eluate,g) applying the HIC eluate comprising the DsbC polypeptide to a size exclusion chromatography,h) collecting fractions from the size exclusion chromatography comprising the purified DsbC polypeptide.193. The method of claim 190 , wherein the detection system is an immunoassay.194. The method of claim 193 , wherein the immunoassay comprises antibodies that specifically binds ultrapure DsbC.195. A method for analyzing a recombinant polypeptide sample ...

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Номер записи: 45
04-03-2021 дата публикации

MICROBIAL FERMENTATION FOR THE PRODUCTION OF TERPENES

Номер: US20210062229A1
Автор: Koepke Michael
Принадлежит:

The invention provides a method for producing a terpene or a precursor thereof by microbial fermentation. Typically, the method involves culturing a recombinant bacterium in the presence of a gaseous substrate whereby the bacterium produces a terpene or a precursor thereof, such as mevalonic acid, isopentenyl pyrophosphate, dimethylallyl pyrophosphate, isoprene, geranyl pyrophosphate, farnesyl pyrophosphate, and/or farnesene. The bacterium may comprise one or more exogenous enzymes, such as enzymes in mevalonate, DXS, or terpene biosynthesis pathways. 1ClostridiumMoorella.. A recombinant C1-fixing bacteria capable of producing mevalonic acid , or a terpene precursor , from a carbon source comprising a nucleic acid encoding a group of exogenous enzymes comprising thiolase , 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) synthase , and HMG-CoA reductase , wherein the bacteria are or2. The bacteria according to claim 1 , further comprising a nucleic acid encoding a group of enzymes comprising mevalonate kinase claim 1 , phosphomevalonate kinase claim 1 , and mevalonate diphosphate decarboxylase.3. The bacteria according to claim 2 , wherein the terpene precursor is isopentenyl diphosphate.4. The bacteria according to claim 2 , further comprising a nucleic acid encoding an exogenous enzyme selected from the group consisting of isopentenyl diphosphate isomerase and geranyltranstransferase.5. The bacteria according to claim 2 , further comprising a nucleic acid encoding both exogenous enzymes isopentenyl diphosphate isomerase and geranyltranstransferase.6. The bacteria according to claim 4 , wherein the terpene precursor is dimethylallyl pyrophosphate or geranyl pyrophosphate.7. The bacteria according to claim 4 , further comprising a nucleic acid encoding an exogenous enzyme comprising isoprene synthase.8. The bacteria according to claim 4 , wherein the terpene precursor is farnesyl pyrophosphate.9. The bacteria according to claim 4 , further comprising a nucleic acid ...

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Номер записи: 46
07-03-2019 дата публикации

METHOD OF SELECTIVELY INHIBITING MPGES-1

Номер: US20190070170A1
Автор: Chen Chun-Song, Leung Elaine Lai-Han, LIU JIAN-XIN, LIU LIANG, Luo Jin-Fang, ZHOU Hua
Принадлежит:

A method of selectively inhibiting the overexpression of mPGES-1 in a subject in need thereof includes a step of administering an effective amount of a selective mPGES-1 inhibitor or a salt thereof to the subject. A method of treating a subject suffering from a disease associated with an overexpression of mPGES-1 and having a risk of cardiovascular event includes the step of administering an effective amount of a selective mPGES-1 inhibitor to the subject. 3. The method of claim 1 , wherein the subject is suffering from at least one of inflammatory disease claim 1 , neurological disease claim 1 , injury claim 1 , immune disease claim 1 , gastrointestinal disease claim 1 , or cancer.4. The method of claim 3 , wherein the subject is suffering from a cardiovascular disease.5. The method of claim 1 , wherein the subject is suffering from arthritis and is at risk of cardiovascular event.6. The method of claim 5 , wherein the cardiovascular event is selected from the group consisting of heart attack claim 5 , stroke claim 5 , myocardial infarction claim 5 , acute coronary syndrome claim 5 , arteriosclerosis claim 5 , thrombosis claim 5 , hypertension claim 5 , cardiovascular death claim 5 , and peripheral vascular disease.7. The method of claim 1 , further comprising steps of:obtaining a sample from the subject;testing the sample for the expression of mPGES-1;comparing the level of mPGES-1 expression with a reference to determine if the subject has an overexpression of mPGES-1; andoptionally determining if the subject is suffering from a cardiovascular disease or being at risk of a cardiovascular event.8. The method of claim 1 , wherein the administration of the selective mPGES-1 inhibitor suppresses the binding of nuclear factor κB to mPGES-1 promoter.9. The method of claim 1 , wherein the subject receives or received a long-term treatment of a non-steroidal anti-inflammatory drug.11. (canceled)12. (canceled)13. (canceled) The Sequence Listing file entitled “ ...

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Номер записи: 47
07-03-2019 дата публикации

MUTANT XYLOSE-METABOLIZING ENZYME AND USE THEREOF

Номер: US20190071684A1
Автор: FUJIMORI Kazuhiro, KAMAGATA Yoichi, Kobayashi Yosuke, OHGIYA Satoru, SAHARA Takehiko, Seike Taisuke
Принадлежит: NATIONAL INSTITUTE OF ADVANCED INDUSTRIAL SCIENCE AND TECHNOLOGY

The present invention provides information on a mutant xylose isomerase gene and a mutant protein with which it is possible to impart high xylose metabolic capacity to budding yeast. Also provided is a yeast strain having the mutant xylose isomerase gene. Additionally provided is an efficient method for producing a useful substance using the yeast strain. The present invention provides mutant --derived xylose isomerase (CpXI) having high xylose metabolic activity, the CpXI comprising an amino acid sequence corresponding to an amino acid sequence in which the number 63 threonine of SEQ ID NO: 11 of CpXI is substituted by isoleucine, lysine, glycine, or histidine and/or the number 162 valine is substituted by alanine. Also provided are: a transformed yeast having high ethanol productivity, the transformed yeast being obtained by transformation using a mutant CpXI gene that comprises a codon mutation corresponding to a codon mutation in which the number 63 threonine of SEQ ID NO: 11 in a CpXI gene optimized for the preferred codon of budding yeast is substituted by isoleucine, lysine, glycine, or histidine and/or the number 162 valine is substituted by alanine; and a method for producing ethanol using the transformed yeast. 1Clostridium phytofermentans. A mutant xylose isomerase (mutant CpXI) comprising an amino acid sequence wherein at least one amino acid corresponding to the threonine at position 63 and the valine at position 162 of SEQ ID NO: 11 is substituted to another amino acid in the amino acid sequence of xylose isomerase (CpXI) , the mutant CpXI having higher xylose metabolic activity than the wild type xylose isomerase (CpXI).2. The mutant CpXI according to claim 1 , wherein the substitution of the threonine at position 63 of SEQ ID NO: 11 to another amino acid is a substitution to isoleucine claim 1 , lysine claim 1 , glycine or histidine claim 1 , and the substitution of the valine at position 162 to another amino acid is a substitution to alanine.3. The ...

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Номер записи: 48
24-03-2022 дата публикации

Methods for inducible expression

Номер: US20220090093A1
Автор: Mark Valasek, Sean Mcclain
Принадлежит: AbSci LLC

The present invention is an inducible coexpression system, capable of controlled induction of expression of each gene product.

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Номер записи: 49
22-03-2018 дата публикации

METHOD FOR MANUFACTURING ALLULOSE-CONTAINING SWEETENER COMPOSITION

Номер: US20180077958A1
Автор: GULLAPALLI Pushpa Kiran, SHIMADA Kensaku, SHINTANI Tomoya, TAKAOKA Seizo
Принадлежит: MATSUTANI CHEMICAL INDUSTRY CO., LTD.

The purpose of the present invention is to provide a technology whereby, in a method for manufacturing a sweetener composition containing glucose, fructose and allulose, said method comprising treating glucose with glucose isomerase and allulose epimerase, the content of allulose in the sweetener composition is increased. A sweetener composition containing glucose, fructose and allulose and having a high allulose content can be continuously manufactured at a high efficiency by immobilizing glucose isomerase and allulose epimerase, packing the same into a column so as to give an activity ratio of the immobilized glucose isomerase to the immobilized allulose epimerase of 1.49:1-5.61:1, and then passing a glucose solution through the column. 1. A method for manufacturing a sweetener composition comprising glucose , fructose and allulose , the method comprising:1) a step A of preparing a column packed with immobilized glucose isomerase and immobilized allulose epimerase so that an activity ratio between them is 1.49:1 to 5.61:1;2) a step B of passing a glucose solution through the column to perform an enzymatic reaction; and3) a step C of collecting an outflow liquid from the column.2. The manufacturing method according to claim 1 , wherein in step B claim 1 , the glucose solution is passed with space velocity being set to 0.2 to 1.0.3. The manufacturing method according to claim 1 , wherein the immobilized glucose isomerase has a specific activity of 100 U/ml or more.4. The manufacturing method according to claim 1 , wherein the immobilized allulose epimerase has a specific activity of 20 U/ml or more.5. The manufacturing method according to claim 1 , wherein an immobilization carrier of the immobilized allulose epimerase is a polystyrene-based weakly basic anion exchange resin.6. The manufacturing method according to claim 1 , wherein the glucose solution further contains a water-soluble magnesium salt.7. The manufacturing method according to claim 1 , comprising:a ...

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Номер записи: 50
31-03-2022 дата публикации

ENZYMATIC PRODUCTION OF D-ALLULOSE

Номер: US20220098632A1
Автор: ROGERS Edwin O., WICHELECKI Daniel Joseph
Принадлежит: BONUMOSE, INC.

The current disclosure provides a process for enzymatically converting a saccharide into allulose. The invention also relates to a process for preparing allulose where the process involves converting fructose 6-phosphate (F6P) to allulose 6-phosphate (A6P), catalyzed by allulose 6-phosphate 3-epimerase (A6PE), and converting the A6P to allulose, catalyzed by allulose 6-phosphate phosphatase (A6PP). 1. A process for preparing allulose , the process comprising:converting fructose 6-phosphate (F6P) to allulose 6-phosphate (A6P), catalyzed by an epimerase; andconverting the A6P produced to allulose, catalyzed by a phosphatase.2. The process of claim 1 , further comprising a step of converting glucose 6-phosphate (G6P) to the F6P claim 1 , wherein the step is catalyzed by phosphoglucoisomerase (PGI).3. The process of claim 2 , further comprising the step of converting glucose 1-phosphate (G1P) to the G6P claim 2 , wherein the step is catalyzed by phosphoglucomutase (PGM).4. The process of claim 3 , further comprising the step of converting a saccharide to the G1P claim 3 , wherein the step is catalyzed by at least one enzyme claim 3 , wherein the saccharide is selected from the group consisting of a starch or derivative thereof claim 3 , cellulose or a derivative thereof and sucrose.5. The process of claim 4 , wherein at least one enzyme is selected from the group consisting of alpha-glucan phosphorylase (αGP) claim 4 , maltose phosphorylase claim 4 , sucrose phosphorylase claim 4 , cellodextrin phosphorylase claim 4 , cellobiose phosphorylase claim 4 , and cellulose phosphorylase.6. The process of claim 4 , wherein the saccharide is starch or a derivative thereof selected from the group consisting of amylose claim 4 , amylopectin claim 4 , soluble starch claim 4 , amylodextrin claim 4 , maltodextrin claim 4 , maltose claim 4 , and glucose.7. The process of claim 6 , further comprising the step of converting starch to a starch derivative wherein the starch derivative is ...

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Номер записи: 51
21-03-2019 дата публикации

Methanol dehydrogenase fusion proteins

Номер: US20190085303A1
Автор: Jingyi Li, Joseph R. WARNER, Nelson R. Barton, Priti Pharkya
Принадлежит: Genomatica Inc

Described herein are fusion proteins including methanol dehydrogenase (MeDH) and at least one other polypeptide such as 3-hexulose-6-phosphate dehydrogenase (HPS) or 6-phospho-3-hexuloisomerase (PHI), such as DHAS synthase or fructose-6-Phosphate aldolase or such as DHA synthase or DHA kinase. In a localized manner, the fusion protein can promote the conversion of methanol to formaldehyde and then to a ketose phosphate such as hexulose 6-phosphate or then to DHA and G3P. When expressed in cells, the fusion proteins can promote methanol uptake and rapid conversion to the ketose phosphate or to the DHA and D3P, which in turn can be used in a pathway for the production of a desired bioproduct. Beneficially, the rapid conversion to the ketose phosphate or to the DHA and G3P can avoid the undesirable accumulation of formaldehyde in the cell. Also described are engineered cells expressing the fusion protein, optionally include one or more additional metabolic pathway transgene(s), methanol metabolic pathway genes, target product pathway genes, cell culture compositions including the cells, methods for promoting production of the target product or intermediate thereof from the cells, compositions including the target product or intermediate, and products made from the target product or intermediate.

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Номер записи: 52
05-05-2022 дата публикации

Methods for Promoting Extracellular Expression of Proteins in Bacillus subtilis Using a Cutinase

Номер: US20220135957A1
Автор: Huang Yan, Su Lingqia, Wu Jing
Принадлежит: JIANGNAN UNIVERSITY

Disclosed is a method for promoting extracellular expression of proteins in using cutinase, which belongs to the technical fields of genetic engineering, enzyme engineering and microbial engineering. It teaches co-expressing a cutinase mutant and a target protein in to promote extracellular expression of the target protein which is naturally located inside cells. The target protein includes xylose isomerase, 4,6-α-glucosyltransferase, 4-α-glucosyltransferase, trehalose synthase, branching enzyme and the like. The invention can achieve extracellular expression of intracellularly localized target protein, improve the production efficiency, reduce the production cost and simplify the subsequent extraction process.

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Номер записи: 53
19-03-2020 дата публикации

A recombinant strain having modified sugar metabolic pathway and method for screening sugar isomerase using same

Номер: US20200087647A1
Автор: Dong Woo Lee, Jae Yoon Sung, Sun Mi Shin, Yun Hye Joo
Принадлежит: Industry Academic Cooperation Foundation of KNU

The present invention relates to a recombinant strain having a modified sugar metabolic pathway resulting from the introduction of an enzyme derived from a different strain to a strain, and a high-speed screening method for various mutants and variants by which useful materials can be obtained or which can produce useful materials. The use of a recombinant vector and a strain according to the present invention not only can construct a new metabolic pathway in a strain to effectively obtain D-tagatose from D-galactose, but also can introduce randomly modified sugar isomerases and then allow D-galactose isomerase variants to be rapidly screened by conducting a cell growth-associated screening system.

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Номер записи: 54
07-04-2016 дата публикации

Aldose-Ketose Transformation for Separation and/or Chemical Conversion of C6 and C5 Sugars from Biomass Materials

Номер: US20160096857A1
Автор: BIN Li, Patricia A. Relue, Sasidhar Varanasi
Принадлежит: UNIVERSITY OF TOLEDO

Systems for converting aldose sugars to ketose sugars and separating and/or concentrating these sugars using differences in the sugars' abilities to bind to specific affinity ligands are described.

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Номер записи: 55
09-04-2015 дата публикации

PROKARYOTIC XYLOSE ISOMERASE FOR THE CONSTRUCTION OF XYLOSE-FERMENTING YEASTS

Номер: US20150099276A1
Автор: BOLES Eckhard, BRAT Dawid, Keller Marco, ROTHER Beate
Принадлежит:

The present invention relates to the use of nucleic acid molecules coding for a bacterial xylose isomerase (XI), preferably coming from , for reaction/metabolization, particularly fermentation, of recombinant microorganisms of biomaterial containing xylose, and particularly for the production of bioalcohols, particularly bioethanol, by means of xylose fermenting yeasts. The present invention further relates to cells, particularly eukaryotic cells, which are transformed utilizing a nucleic acid expression construct which codes for a xylose isomerase, wherein the expression of the nucleic acid expression construct imparts to the cells the capability to directly isomerize xylose into xylulose. Said cells are preferably utilized for reaction/metabolization, particularly fermentation, of biomaterial containing xylose, and particularly for the production of bioalcohols, particularly bioethanol. The present invention also relates to methods for the production of bioethanol, and to methods for the production of further metabolization products, comprising the metabolization of media containing xylose. 1Clostridium phytofermentans. A method for the recombinant expression and production of xylose isomerase or for the conversion of xylose to xylulose by an isolated host cell , wherein said isolated host cell is a yeast cell or a filamentous fungal cell and said method consists of transforming said host cell with a nucleic acid molecule comprising a nucleic acid sequence that encodes a xylose isomerase (XI) , and wherein said nucleic acid sequence is at least 95% identical to the nucleic acid sequence SEQ ID NO: 2.2. The method according to claim 1 , wherein said method is used for:the conversion or metabolization of biomaterial containing xylose,the production of bio-based chemicals, orthe production of biobutanol, bioethanol or of both biobutanol and bioethanol.3Clostridium phytofermentans. The method according to claim 1 , wherein the nucleic acid molecule is a nucleic acid ...

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Номер записи: 56
12-05-2022 дата публикации

EPIMERASE ENZYMES AND THEIR USE

Номер: US20220145344A1
Автор: Govindarajan Sridhar, Schroeder William, Venkitasubramanian Padmesh, WELCH Mark
Принадлежит: ARCHER DANIELS MIDLAND COMPANY

This disclosure provides epimerase enzymes useful for commercial scale production of allulose from fructose. The disclosed enzymes (“epimerase variants”) are variants of CGD1 xylose isomerase engineered to have improved catalytic activity of about 1.5- to 2-fold compared with the parent enzyme. 1. A nucleic acid encoding a protein , wherein the amino acid sequence of the protein is selected from the group consisting of SEQ ID NOS:16 , 18 , 40 , 42 , 44 , 46 , 48 , 50 , 52 , 54 , 56 , 58 , 60 , 62 , 64 , 66 , 68 , 70 , 72 , 74 , 76 , 78 , 80 , 82 , 84 , 86 , 88 , 90 , 92 , 94 , 96 , 98 , and 100.2. A microorganism comprising the nucleic acid of .3Bacillus licheniformis, Saccharomyces cerevisiae, Schizosaccharomyces pombe, Pseudomonas putida, PichiaAspergillusTrichoderma reesei, Corynebacterium glutamicum, E. coliB. subtilis.. The microorganism of claim 2 , wherein the microorganism is selected from the group consisting of sp. claim 2 , sp. claim 2 , claim 2 , and4. A protein comprising an amino acid sequence selected from the group consisting of SEQ ID NOS:16 claim 2 , 18 claim 2 , 40 claim 2 , 42 claim 2 , 44 claim 2 , 46 claim 2 , 48 claim 2 , 50 claim 2 , 52 claim 2 , 54 claim 2 , 56 claim 2 , 58 claim 2 , 60 claim 2 , 62 claim 2 , 64 claim 2 , 66 claim 2 , 68 claim 2 , 70 claim 2 , 72 claim 2 , 74 claim 2 , 76 claim 2 , 78 claim 2 , 80 claim 2 , 82 claim 2 , 84 claim 2 , 86 claim 2 , 88 claim 2 , 90 claim 2 , 92 claim 2 , 94 claim 2 , 96 claim 2 , 98 claim 2 , and 100.5. A solid matrix comprising the protein of .6. A column comprising the solid matrix of and configured to receive an input solution comprising fructose over the solid matrix and to permit exit of an output solution comprising allulose.7. A method of producing a protein comprising an amino acid sequence selected from the group consisting of SEQ ID NOS:16 claim 5 , 18 claim 5 , 40 claim 5 , 42 claim 5 , 44 claim 5 , 46 claim 5 , 48 claim 5 , 50 claim 5 , 52 claim 5 , 54 claim 5 , 56 claim 5 , 58 claim ...

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Номер записи: 57
06-04-2017 дата публикации

Means and Methods for Itaconic Acid Production

Номер: US20170096690A1
Автор: Blank Lars M., Boelker Michael, Buckel Wolfgang, Geiser Elena, Przybilla Sandra, Wierckx Nick
Принадлежит:

The present invention relates to a method of producing itaconic acid. Further the present invention relates to nucleic acids encoding an aconitate-delta-isomerase (ADI) and trans-aconitate decarboxylase (TAD) and uses of such nucleic acids. Provided is additionally a recombinant host cell engineered to overexpress nucleic acids of the present invention. Furthermore an expression cassette and a vector are provided which include the respective nucleic acid. 1. A method of producing itaconic acid , comprising (i) a polynucleotide sequence having at least 30% sequence identity with the sequence of SEQ ID NO: 1, said polynucleotide sequence encoding a protein or fragment thereof having aconitate-delta-isomerase (ADI) activity; and', '(ii) a polynucleotide sequence having at least 50% sequence identity with the sequence of SEQ ID NO: 6, said polynucleotide sequence encoding a protein or fragment thereof having trans-aconitate decarboxylase (TAD) activity,', 'in comparison to a comparable host cell which has not been genetically altered under conditions to allow said host cell to overexpress said polynucleotide sequence (i) and (ii), thereby said host cell is capable of converting cis-aconitate via trans-aconitate to itaconic acid; and, '(a) culturing a recombinant host cell which is genetically engineered to overexpress'}(b) obtaining itaconic acid.2. The method of claim 1 , wherein said host cell further overexpresses a polynucleotide sequence selected from:a polynucleotide sequence having at least 50% sequence identity with the sequence of SEQ ID NO: 4, said polynucleotide sequence encoding a protein or fragment thereof having the activity of a mitochondrial citrate transporter, preferably of a mitochondrial cis-aconitate transporter;a polynucleotide sequence having at least 50% sequence identity with the sequence of SEQ ID NO: 6, said polynucleotide sequence encoding a protein or fragment thereof having trans-aconitate decarboxylase (TAD) activity; anda polynucleotide ...

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Номер записи: 58
16-04-2015 дата публикации

METHODS FOR THE TREATMENT AND DIAGNOSIS OF BONE MINERAL DENSITY RELATED DISEASES

Номер: US20150104437A1
Автор: Cormier-Daire Valerie, Munnich Arnold
Принадлежит:

The present invention relates to methods of the treatment and diagnosis of bone mineral density related disorders. More particularly, the present invention relates to a method of diagnosing or predicting a hone mineral density related disease, or a risk of a bone mineral density related disease, in a subject, which method comprises detecting a mutation in the TBXAS1 gene, wherein the presence of said mutation is indicative of a bone mineral density related disease or of a risk of a bone mineral density related disease. The invention also relates to a compound selected in the group consisting of a thromboxane synthase (TXAS) encoding polynucleotide, a TXAS, thromboxane A2 or an analog thereof for treating or preventing a disease associated with an increased bone mineral density (e.g., Ghosal hematodiaphyseal dysplasia syndrome). The invention also relates to a compound selected from the group consisting of an inhibitor of TBXAS1 gene expression or a thromboxane inhibitor for treating or preventing a disease associated with a decreased bone mineral density (e.g., osteoporosis). 1. A method of diagnosing or predicting a bone mineral density related disease , or a risk of a bone mineral density related disease , in a subject , which method comprises detecting a mutation in the TBXAS1 gene , wherein the presence of said mutation is indicative of a bone mineral density related disease or of a risk of a bone mineral density related disease , wherein said method comprises the step of detecting a TBXAS1 mutation in a nucleic acid sample obtained from said subject.2. The method according to claim 1 , wherein the bone mineral density related disease is a disease associated with an increased bone mineral density and the mutation in the TBXAS1 gene is associated with a decrease of the Thromboxane synthase activity.3. The method of wherein said disease associated with an increased bone mineral density is Ghosal hematodiaphyseal dysplasia syndrome.4. The method of or wherein the ...

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Номер записи: 59
12-04-2018 дата публикации

Novel MHC-Independent Tumor-Associated Antigens

Номер: US20180099033A1
Автор: EBERTS Daniela, ECHCHANNAOUI Hakim, FATHO Martina, LENNERZ Volker, LÜBCKE Silke, PASCHEN Annette, SCHADENDORF Dirk, WOELFEL Catherine, WOELFEL Thomas
Принадлежит:

The present invention relates to novel tumor-associated antigens, which elicit independently from a presentation via MHC a CD8-positive T-cell response. GM-CSF-Receptor alpha chain (CSF2RA) and Tyrosinase-related protein 2 (TRP-2) were found to be targets of CD8-positive T-cell clones which could detect the proteins on the surface of HLA I negative melanoma cells. Thus, the invention provides proteins, protein fragments and polypeptides of the novel antigens for use in medicine, for example for the treatment, diagnosis and prevention of a tumor disease. Furthermore provided are nucleic acids expressing the antigens of the invention, binding agents specific for the antigens of the invention, such as T-cell receptor chains and isolated T cells which are reactive against the antigens of the invention or which express the T-cell receptors of the invention. The invention further pertains to pharmaceutical compositions, especially vaccine compositions, comprising the antigens, nucleic acids, binding agents or T cells in accordance with the invention, and methods for the generation of T cells, which are specifically reactive to the antigens of the invention in an MHC-independent manner. 1. A protein , protein fragment or polypeptide comprising at least 8 contiguous amino acids from the amino acid sequence of GM-CSF-Receptor alpha chain (CSF2RA) (SEQ ID NO: 1) or tyrosinase-related protein 2 (TRP-2) (SEQ ID NO: 2) , wherein said protein , protein fragment or polypeptide is capable of inducing a T-cell response and/or binding a cognate T-cell receptor.2. The protein claim 1 , protein fragment or polypeptide according to claim 1 , which is capable of inducing a major histocompatibility complex (MHC)-independent T-cell response.3. The protein claim 1 , protein fragment or polypeptide according to claim 1 , which is capable of binding a cognate T-cell receptor expressed by a MHC class I-independent T cell or a MHC class I and II-independent T cell.4. A method for the prevention ...

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Номер записи: 60
26-03-2020 дата публикации

MICROBES & METHODS FOR IMPROVED CONVERSION OF A FEEDSTOCK

Номер: US20200095617A1
Автор: Higashide Wendy M., LI Xiaoqian, Rohlin Lars Erik Ulf
Принадлежит: NANTBIO, INC.

Genetically engineered cells and methods are presented that enhance the consumption of xylose in a medium comprising a mix of five- and six-carbon sugars. Method of using these microbes to enhance xylose utilization and methods of making value products using these microbes are also disclosed herein. 1. A microbial cell comprising (1) a non-native xylose isomerase (xylA) gene; and (2) a non-native fructose-6-phosphate phosphoketolase (xfp) gene , and/or (3) a d-xylose ABC transporter (xylFGH).2. The microbial cell of claim 1 , wherein the microbial cell further comprises: (4) a non-native xylulose kinase (xylB) gene.3. The microbial cell of claim 1 , wherein the microbial cell is a eukaryote or a prokaryote.4Saccharomyces, Pichia, CandidaAspergillus.. The microbial cell of claim 3 , wherein the eukaryote belongs to a genus selected from the group consisting of claim 3 , and5Escherichia, Bacillus, Corynebacterium, Alcaligenus, Zymomonas, Clostridium, Lactobacillus, SynechococcusSynechocystis.. The microbial cell of claim 3 , wherein the prokaryote belongs to a genus selected from the group consisting of claim 3 , and6. The microbial cell of claim 1 , wherein the xylA gene comprises a coding sequence that is a native sequence claim 1 , located on the chromosome claim 1 , and the promoter driving the xylA is heterologous to the xylA coding sequence.7. The microbial cell of claim 1 , wherein the xfp gene comprises a nucleotide sequence that encodes a protein with at least 85% sequence identity to SEQ ID NO:1 or SEQ ID NO:2.8. The microbial cell of claim 7 , wherein the encoding nucleotide sequence is SEQ ID NO:3 or SEQ ID NO:4.9. The microbial cell of claim 1 , wherein the xylFGH gene comprises a nucleotide sequence that encodes a protein with at least 85% sequence identity to SEQ ID NO:5.10. A method of improving xylose utilization in a microbial cell expressing xylose isomerase (XylA) and xylulose kinase (XylB) genes claim 1 , the method comprising genetically ...

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Номер записи: 61
03-07-2014 дата публикации

Xylose Isomerases and Their Uses

Номер: US20140186884A1
Автор: Adam Martin Burja, David Neal Nunn, Jr., John Peter Flash Bartnek, LING Li, Peter Luginbuhl
Принадлежит: BP Corp North America Inc

This disclosure relates to novel xylose isomerases and their uses, particularly in fermentation processes that employ xylose-containing media.

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Номер записи: 62
19-04-2018 дата публикации

Methods and compositions for using mhc class ii invariant chain polypeptides as a receptor for macrophage migration inhibitory factor

Номер: US20180105593A1
Автор: Christine N. Metz, Lin Leng, Richard J. Bucala
Принадлежит: Baxalta GmbH, Baxalta Inc

Methods and compositions for using the MEW class II invariant chain polypeptide, Ii (also known as CD74), as a receptor for macrophage migration inhibitory factor (MIF), are disclosed. These include methods and compositions for using this receptor, as well as agonists and antagonists of MIF which bind to this receptor, or which otherwise modulate the interaction of MIF with CD74 or the consequences of such interaction, in treatment of conditions characterized by locally or systemically altered MIF levels, particularly inflammatory conditions and cancer.

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Номер записи: 63
19-04-2018 дата публикации

PROCESS FOR DE NOVO MICROBIAL SYNTHESIS OF TERPENES

Номер: US20180105838A1
Автор: Brüser Heike, Buchhaupt Markus, KRONER Cora, PELZER Ralf, Schrader Jens, Schröder Hartwig, SONNTAG FRANK
Принадлежит:

The invention relates to microbial terpene production. Known methods for microbial production of terpenes are mostly based on the direct conversion of sugars. Therefore alternative substrates, in particular alternative carbon sources, for use in microbial terpene production were desirable. The invention relates to a methylotrophic bacterium containing recombinant DNA coding for at least one polypeptide with enzymatic activity for heterologous expression in said bacterium, wherein said at least one polypeptide with enzymatic activity is selected from the group consisting an enzyme of a heterologous mevalonate pathway, a heterologous terpene synthase and optionally a heterologous synthase of a prenyl diphosphate precursor. The invention further relates in particular to a method for de novo microbial synthesis of sesquiterpenes or diterpenes from methanol and/or ethanol. 1. A methylotrophic bacterium containing a heterologous terpene synthase and recombinant DNA coding for at least one polypeptide with enzymatic activity for expression in said bacterium , characterized in that said at least one polypeptide with enzymatic activity is selected from the group consisting ofat least one enzyme of a heterologous mevalonate pathway selected from the group consisting of hydroxymethylglutaryl-CoA synthase (HMG-CoA synthase), hydroxymethylglutaryl-CoA reductase (HMG-CoA reductase), mevalonate kinase, phosphomevalonate kinase, pyrophosphomevalonate decarboxylase and isopentenyl pyrophosphate isomerase; anda synthase of a prenyl diphosphate precursor.2. A methylotrophic bacterium containing a heterologous hydroxymethylglutaryl-CoA synthase (HMG-CoA synthase) and a hydroxymethylglutaryl-CoA reductase (HMG-CoA reductase) as enzymes of a heterologous mevalonate pathway and recombinant DNA coding for at least one polypeptide with enzymatic activity for expression in said bacterium , characterized in that said at least one polypeptide with enzymatic activity is selected from the group ...

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Номер записи: 64
29-04-2021 дата публикации

CELL-FREE PRODUCTION OF SUGARS

Номер: US20210123082A1
Автор: Blake William Jeremy, Cunningham Drew S., MacEachran Daniel, Moura Matthew Eduardo
Принадлежит: GreenLight Biosciences, Inc.

Provided herein, in some embodiments, are systems, methods, and compositions (e.g., cells and cell lysates) for enzymatically converting a polymeric glucose carbohydrate (e.g., starch) to sugar. 1. A method for producing an allulose compound comprising the steps of:converting a polymeric glucose carbohydrate to glucose 1-phosphate (G1P) catalyzed by an α-glucan or a cellodextrin phosphorylase; converting said glucose 1-phosphate (G1P) to produce glucose 6-phosphate (G6P) catalyzed by a phosphoglucomutase; converting said glucose 6-phosphate (G6P) to fructose 6-phoshpate (F6P) catalyzed by a phosphoglucoisomerase; converting said fructose 6-phosphate (F6P) to produce allulose 6-phosphate (A6P) catalyzed by an allulose 6-phosphate epimerase (A6PE); and converting said allulose 6-phosphate epimerase (A6P) to allulose catalyzed by an allulose 6-phosphate phosphatase (A6PP).2. The method of claim 1 , wherein the polymeric glucose carbohydrate is starch claim 1 , cellodextrin claim 1 , or glycogen.3Aquifex aeolicus, Thermocrinis minervae, Thermosulfidibacter takaii, Thermosulfurimonas dismutans, Thermococcus litoralis, Palaeococcus pacificus, Thermotoga neapolitana, Ruminiclostridium thermocellum, Pyrococcus abyssi, Thermococcus thioreducens, Deinococcus radiodurans, Sulfolobus acidocaldarius, Thermus caldophilus, Meiothermus silvanus, Oceanithermus profundus, Ardenticatena maritima, Thermococcus barophilus, Pseudothermotoga thermarum, Hydrogenobacter thermophilus, Thermus oshimai, Meiothermus ruberMarinitoga piezophila. The method of claim 1 , wherein the α-glucan phosphorylase is selected from the group consisting of: claim 1 , and α-glucan phosphorylases.4Clostridium thermocellum, Clostridium straminisolvens, Thermotoga; Ignisphaera aggregans, Thermotoga maritima, Spirochaeta thermophila, Caldicellulosiruptor bescii, Dictyoglomus thermophilum, Thermoanaerobacterium thermosaccharolyticum, Thermosipho africanus, Caldisalinibacter kiritimatiensis, Defluviitalea ...

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Номер записи: 65
02-04-2020 дата публикации

YEAST STRAIN WITH XYLOSE UTILIZING CAPACITY

Номер: US20200102549A1
Автор: GONG Gyeongtaek, KIM Jiwon, Lee Sun Mi, UM Youngsoon, Yook Sangdo
Принадлежит: KOREA INSTITUTE OF SCIENCE AND TECHNOLOGY

Disclosed herein are a yeast strain capable of utilizing xylose as a carbon source and a method for producing lipids using the same. The yeast strain is obtained by adaptively evolving a wild-type yeast strain which cannot utilize xylose as a carbon source so that it can produce high density lipids and then transforming the adaptively evolved strain to obtain the ability to metabolize xylose. Since the strain does not have the xylose metabolic pathway based on oxidoreductase, it can produce biodiesel and biomaterials based on lipid and lignocellulosic biomass at a high yield without a problem of cofactor imbalance and can greatly improve the economic feasibility and sustainability of the production processes of biodiesel and biomaterials. 1. A transformed and adaptively evolved yeast strain , comprising the following mutations in at least one gene selected from the group consisting of YALI0_A15642g , YALI0_A15796g , YALI0_C11165g , YALI0_C16247g , YALI0_D24849g , YALI0_D27016g , YALI0_E14388g1 , YALI0_E23969g , YALIO_F04906g , and YALI0_F17468g , comprising at least one gene selected from the group consisting of a gene encoding an enzyme that interconverts D-xylose and D-xylulose and a gene encoding an enzyme that produces D-xylulose-5-phosphate from D-xylulose and capable of utilizing xylose as the sole carbon source:147G>A mutation in the YALI0_A15642g gene;567_568insACA and 576T>G mutations in the YALI0_A15796g gene;1523T>C mutation in the YALI0_C11165g gene;T1412A, G1441A, A1513G, A1534G, G1535T, T1544A, and C1847T mutations in the YALI0_C16247g gene;103G>A mutation in the YALI0_D24849g gene;446T>C mutation in the YALI0_D27016g gene;2525C>G, 2531T>G, 2534A>G, and 2558T>C mutations in the YALI0_E14388g1 gene;480_481insTCCTCTACCCCCGAG, 526_527insCCTCCACCACCGAGC, and 497A>C mutations in the YALI0_E23969g gene;2702T>A mutation in the YALIO_F04906g gene; or482_482insGCACCA mutation in the YALI0_F17468g gene.2. The transformed and adaptively evolved yeast strain ...

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Номер записи: 66
11-04-2019 дата публикации

Recombinant yeast and method for producing ethanol using the same

Номер: US20190106719A1
Автор: Junji Ito, Nobuki Tada, Rie Hirao, Toru Onishi
Принадлежит: Toyota Motor Corp

This invention is aimed at improving an ethanol fermentation ability of a recombinant yeast strain having an ability of assimilating pentose, such as xylose or arabinose. The recombinant yeast strain haying an ability of assimilating pentose is obtained by lowering activity of a gene involved in upstream of glyceraldehyde-3-phosphate in the Embden-Meyerhof pathway.

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Номер записи: 67
28-04-2016 дата публикации

HYBRID PROTEIN THAT CONVERTS ARACHIDONIC ACID INTO PROSTACYCLIN

Номер: US20160114005A1
Автор: RUAN Ke-He
Принадлежит:

A recombinant 130-kDa protein is constructed by linking together human cyclooxygenase (COX) isoform-2 (COX-2) and prostacyclin synthase (PGIS), via a 10-20 amino acid residues of a transmembrane sequence. The engineered protein is expressed in cells, and adopts the functions of COX and PGIS, to continually convert arachidonic acid (AA) into prostaglandin G(catalytic step 1), prostaglandin H(catalytic step 2) and prostacyclin (PGI; catalytic step 3). 1. An isolated hybrid protein molecule comprising a cyclooxygenase (COX) amino acid sequence and an eicosanoid-synthesizing (ES) enzyme amino acid sequence with a linker sequence disposed there between and directly connecting said COX enzyme sequence to said ES enzyme sequence.2. The hybrid protein molecule of claim 1 , wherein said linker sequence is about 10 to 22 amino acids long.3. The hybrid protein molecule of wherein said linker sequence is His-Ala-Ile-Met-Gly-Val-Ala-Phe-Thr-Trp (SEQ ID NO. 1) or His-Ala-Ile-Met-Gly-Val-Ala-Phe-Thr-Trp-Val-Met-Ala-Leu-Ala-Cys-Ala-Ala-Pro-Pro-Leu-Val (SEQ ID NO. 2) or residues 1-11 claim 2 , 1-12 claim 2 , 1-13 claim 2 , 1-14 claim 2 , 1-15 claim 2 , 1-16 claim 2 , 1-17 claim 2 , 1-18 claim 2 , 1-19 claim 2 , 1-20 or 1-21 of SEQ ID NO. 2.4. The hybrid protein of claim 1 , comprising cyclooxygenase (COX) claim 1 , a transmembrane linker claim 1 , and a prostacyclin synthase (PGIS) claim 1 , wherein said hybrid protein is either chemically synthesized or recombinantly produced.5. A pharmaceutical composition comprising:{'claim-ref': {'@idref': 'CLM-00001', 'claim 1'}, 'the hybrid protein of ; and'}a pharmaceutically acceptable carrier.6. A method of treating an individual having a vascular disease claim 5 , or at risk of developing a vascular disease claim 5 , said method comprising microinjecting an effective amount of the pharmaceutical composition of into at least one vascular cell in said individual claim 5 , to cause the production of at least one biologically active compound ...

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Номер записи: 68
28-04-2016 дата публикации

Method of diagnosing laryngeal cancer or diagnosing prognosis in radioresistance of laryngeal cancer

Номер: US20160116473A1
Автор: Jae-Sung Kim, Sang-Gu Hwang, Young-hoon Han
Принадлежит: Korea Institute of Radiological and Medical Sciences

Disclosed are increased expression of ERp57, ERp57-STAT3 complex, and ERp57-STAT3-Mcl-1 in laryngeal cancer, especially in radioresistant laryngeal cancer and their regulations on radioresistance of laryngeal cancer. As such, the efficacy of radiotherapy can be enhanced by diagnosing prognosis in laryngeal cancer and radioresistance of laryngeal cancer. Furthermore, provided are a method of screening a therapeutic agent for laryngeal cancer including selecting a candidate drug that inhibits the expression of ERp57 or inactivates ERp57, and a therapeutic method for inhibiting or treating laryngeal cancer or radioresistant laryngeal cancer, thereby being useful in the treatment of laryngeal cancer.

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Номер записи: 69
09-06-2022 дата публикации

ENGINEERED MICROORGANISMS WITH G3P -> 3PG ENZYME AND/OR FRUCTOSE-1,6-BISPHOSPHATASE INCLUDING THOSE HAVING SYNTHETIC OR ENHANCED METHYLOTROPHY

Номер: US20220177895A1
Автор: Khodayari Ali, NAGARAJAN Harish, YANG Tae Hoon
Принадлежит:

Described herein are engineered cells including ones having synthetic methylotrophy which include an NADH-dependent enzyme capable of converting G3P to 3PG (e.g., gapN) and/or fructose-1,6-bisphosphatase, along with hexulose-6-phosphate synthase, 6-phospho-3-hexuloisomerase, a phosphoketolase, or a combination thereof. Engineered cells of the disclosure beneficially maintain adequate pool sizes of phosphorylated C3 and/or C4 compounds, and/or provide increased levels of NADPH. As such, the modifications allow for the generation of C6 compounds from C1 (e.g., a methanol feedstod) and C5 compounds, the regeneration of C5 compounds from C6 compounds by carbon rearrangement, and an improved balance between regeneration of C5 compounds and lower glycolysis. In turn, this allows the engineered microorganism to generate sufficient quantities of metabolic precursors (e.g., acetyl-CoA) which can be used in a bioproduct pathway, and the engineered cells can include further modifications to those pathway enzymes allowing for production of a desired bioproduct. 1. An engineered microorganism having synthetic or enhanced methylotrophy comprising:{'i': 'B. methanolicus', '(a) exogenous enzyme A that (ai) is capable of converting glyceraldehyde 3-phosphate (G3P) to 3-phosphoglycerate (3PG), (aii) has at least 50% sequence identity to SEQ ID NO:1 (gapN), wherein (ai) or (aii) is capable of reducing NADP to NADPH, or (aiii) that is a fructose-1,6-bisphosphatase; and'}(b) an exogenous enzyme B which is (bi) a phosphoketolase, (bii) a hexulose-6-phosphate synthase, (biii) 6-phospho-3-hexuloisomerase, or any combination of (bi), (bii) and (biii).2. The engineered microorganism of comprising the (a) exogenous enzyme A claim 1 , and the (bi) exogenous phosphoketolase claim 1 , and optionally the (bii) exogenous hexulose-6-phosphate synthase claim 1 , and the (biii) exogenous 6-phospho-3-hexuloisomerase.3. (canceled)4. (canceled)5B. methanolicus. An engineered microorganism comprising an ...

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Номер записи: 70
09-06-2022 дата публикации

COMPOSITION FOR PRODUCING TAGATOSE AND METHOD OF PRODUCING TAGATOSE USING THE SAME

Номер: US20220177936A1
Автор: CHO Hyun Kug, Kim Seong Bo, Lee Young Mi, YANG Sung Jae
Принадлежит:

Provided are a composition for producing tagatose, comprising fructose-6-phosphate 4-epimerase, and a method of producing tagatose using the same. 1. A composition for producing tagatose-6-phosphate , comprising tagatose-6-phosphate kinase , a microorganism expressing the tagatose-6-phosphate kinase , or a culture of the microorganism.2. The composition of claim 1 , further comprising fructose-6-phosphate.3. The composition of claim 1 , wherein the tagatose-6-phosphate kinase consists of an amino acid sequence of SEQ ID NO: 1 claim 1 , 3 claim 1 , or 5.4. A composition for producing tagatose claim 1 , comprising tagatose-6-phosphate kinase claim 1 , a microorganism expressing the tagatose-6-phosphate kinase claim 1 , or a culture of the microorganism; and tagatose-6-phosphate phosphatase claim 1 , a microorganism expressing the tagatose-6-phosphate phosphatase claim 1 , or a culture of the microorganism.5. The composition of claim 4 , further comprising fructose-6-phosphate.6. The composition of claim 4 , further comprising glucose-6-phosphate isomerase claim 4 , a microorganism expressing the glucose-6-phosphate isomerase claim 4 , or a culture of the microorganism.7. The composition of claim 6 , further comprising phosphoglucomutase claim 6 , a microorganism expressing the phosphoglucomutase claim 6 , or a culture of the microorganism.8. The composition of claim 7 , further comprising α-glucan phosphorylase claim 7 , starch phosphorylase claim 7 , maltodextrin phosphorylase claim 7 , or sucrose phosphorylase claim 7 , a microorganism expressing the α-glucan phosphorylase claim 7 , starch phosphorylase claim 7 , maltodextrin phosphorylase claim 7 , or sucrose phosphorylase claim 7 , or a culture of the microorganism.9. The composition of claim 6 , further comprising glucokinase claim 6 , a microorganism expressing the glucokinase claim 6 , or a culture of the microorganism.10. The composition of claim 9 , further comprising α-amylase claim 9 , pullulanase claim 9 , ...

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Номер записи: 71
27-04-2017 дата публикации

EXPRESSION CARTRIDGE FOR THE TRANSFORMATION OF EUKARYOTIC CELLS, METHOD FOR TRANSFORMING EUKARYOTIC CELLS, GENETICALLY MODIFIED ORGANISM, METHOD FOR PRODUCING BIOFUELS AND/OR BIOCHEMICALS, AND THUS PRODUCED BIOFUEL AND/OR BIOCHEMICAL

Номер: US20170114350A1
Автор: dos Santos Leandro Vieira, Pereira Gonçalo Amarante Guimarães
Принадлежит: Bioclere Agroindustrial Ltda.

The present invention describes the expression cassette for transforming eukaryotic cell which comprises the peptide encoding non-natural sequence of nucleotides with xylose isomerase feature (SEQ ID NO: 1), optionally also comprising other genes of pentose phosphate route. Additionally, it is described the microorganism filed under the number DSM28739, which, in addition to the above-mentioned modifications, also present genetic modifications from adaptive evolution. The described microorganism shows efficient consumption of xylose and conversion of ethanol when compared to its correspondent without said genetic modifications and mutations from evolution. It is also described the process for producing biofuels e biochemicals, preferably ethanol, mainly from the lignocellulosic portion of the vegetal biomass. Biofuels, preferably ethanol, and biochemicals produced by the process of the invention are also described. 1. An expression cassette for transforming eukaryotic cell , comprising:a) at least one nucleotide sequence selected from the group consisting of: xylose isomerase (SEQ ID NO: 1), transaldolase (SEQ ID NO: 5), ribose 5-phosphate isomerase (SEQ ID NO: 7), xylulokinase (SEQ ID NO: 9), transcetolase (SEQ ID NO: 11) and ribose 5-phosphate epimerase (SEQ ID NO: 12);b) at least one promoter nucleotide sequence selected from the group consisting of: promoter glyceraldehyde 3-phosphate dehydrogenase (SEQ ID NO: 2), promoter 3-phosphate kinase (SEQ ID NO: 6), promoter of the alcohol dehydrogenase 1 enzyme (SEQ ID NO: 8); andc) at least one terminator nucleotide sequence selected from the group consisting of: terminator glyceraldehyde 3-phosphate dehydrogenase (SEQ ID NO: 3), terminator of alcohol dehydrogenase (SEQ ID NO: 10), terminator 3-phosphate kinase (SEQ ID NO: 13);wherein the nucleotide sequence defined in a) is functionally linked to the promoter nucleotide sequence defined in b) and to the terminator nucleotide sequence defined in c), being heterologous ...

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Номер записи: 72
18-04-2019 дата публикации

ARABINOSE ISOMERASES FOR YEAST

Номер: US20190112590A1
Автор: Chen Zhongqiang, Qi Min, RICE Barbara, Yang Jianjun
Принадлежит:

A group of arabinose isomerases are disclosed that provide effective amounts of activity for use of arabinose in production of ethanol, when expressed in yeast cells expressing the other enzymes of an arabinose utilization pathway. The group of arabinose isomerases represents a clade of a phylogenetic tree, having a distinguishing conserved amino acid sequence motif. Other useful arabinose isomerases are also disclosed. 1. A recombinant yeast cell comprising an arabinose utilization pathway that comprises a polypeptide having arabinose isomerase activity ,wherein the yeast cell comprises a heterologous polynucleotide encoding said polypeptide,wherein the polypeptide comprises a motif that is at least 90% identical to SEQ ID NO:67,to and wherein the position of the motif in the polypeptide corresponds with positions 237-269 of SEQ ID NO:7.2. The recombinant yeast cell of claim 1 , wherein the motif comprises at least seventeen amino acids selected from the group consisting of:(a) I at position 237;(b) R or K at position 238;(c) Y at position 239;(d) R or K at position 242;(e) E at position 243;(f) I at position 245;(g) A at position 246;(h) I or M at position 247;(i) K at position 249;(j) I or M at position 250;(k) R or A at position 253;(l) E or N at position 254;(m) G at position 255;(n) A or C at position 256;(o) F at position 259;(p) N at position 261;(q) T at position 262;(r) Q or E at position 264; and(s) M at position 269.3. The recombinant yeast cell of claim 1 , wherein the polypeptide comprises a motif that is SEQ ID NO:67.4. The recombinant yeast cell of claim 1 , wherein the polypeptide comprises a motif that is at least 90% identical to SEQ ID NO:66.5. The recombinant yeast cell of claim 4 , wherein the polypeptide comprises a motif that is SEQ ID NO:66.6. The recombinant yeast cell of claim 1 , wherein the polypeptide comprises an amino acid sequence that is at least 85% identical to SEQ ID NO:7 claim 1 , 8 claim 1 , 10 claim 1 , 17 claim 1 , 18 claim 1 ...

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Номер записи: 73
05-05-2016 дата публикации

Recombinant yeast and method for producing ethanol using the same

Номер: US20160122784A1
Автор: Nobuhiro Ishida, Nobuki Tada, Risa Nagura, Satoshi Katahira, Toru Onishi
Принадлежит: Toyota Motor Corp

The invention is intended to improve xylose assimilation ability and ethanol fermentation ability in a xylose-assimilating yeast into which a xylose isomerase gene has been introduced. The amount of NADH produced by the recombinant yeast into which the xylose isomerase gene had been introduced as a result of the enzymatic reaction of acetohydroxy acid reductoisomerase is lowered.

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Номер записи: 74
04-05-2017 дата публикации

METHOD FOR INDUCING PRODUCTION OF VASCULAR ENDOTHELIAL GROWTH FACTOR

Номер: US20170119829A1
Автор: Hukuda Keiichi, Kawakami Takashi, Tanabe Tadashi
Принадлежит:

The present invention relates to a method for inducing production of vascular endothelial growth factor (VEGF). The method includes administering, to an individual, a composition including adeno-associated virus (AAV) carrying a hPGIS gene coding for human prostacyclin synthase (hPGIS) which synthesizes prostaglandin 1. A method for inducing production of vascular endothelial growth factor (VEGF) , the method comprising: administering , to an individual , a composition comprising an adeno-associated virus (AAV) carrying a hPGIS gene coding for human prostacyclin synthase (hPGIS) which synthesizes prostaglandin I(PGI).2. The method according to claim 1 , wherein the AAV is of a type selected from the group consisting of type 1 claim 1 , 2 claim 1 , 5 and 83. The method according to claim 1 , wherein the AAV is of a type selected from the group consisting of type 1 and 2.4. The method according to claim 1 , wherein the AAV induces one or more activities selected from the group containing of vasodilation claim 1 , anti-platelet aggregation and angiogenesis.5. The method according to claim 1 , wherein the composition further comprises a pharmaceutically permissible carrier containing the AAV claim 1 , the carrier being selected from the group consisting of water claim 1 , a water-propylene glycol mixed solution claim 1 , a buffered solution claim 1 , and 0.4% saline.6. The method according to claim 1 , wherein the AAV further carries a second gene coding for an angiogenesis factor selected from the group consisting of genes coding for vascular endothelial growth factor (VEGF) and VEGF-2.7. The method according to claim 6 , wherein the second gene coding for an angiogenesis factor is a VEGF.8. The method according to claim 6 , wherein the AAV induces one or more activities selected from the group containing of vasodilation claim 6 , anti-platelet aggregation and angiogenesis.9. The method according to claim 6 , wherein the composition further comprises a pharmaceutically ...

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Номер записи: 75
03-05-2018 дата публикации

Heterologous Pathway to Produce Terpenes

Номер: US20180119176A1
Автор: Christopher B. Eiben, Jay D. Keasling
Принадлежит: UNIVERSITY OF CALIFORNIA

Cells comprising a heterologous metabolic pathway are configured to produce a terpene product containing non-multiples of five carbon, particularly wherein the pathway comprises heterologous Lepidoptera insect juvenile hormone biosynthetic pathway enzymes of the insect's mevalonate pathway.

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Номер записи: 76
04-05-2017 дата публикации

METHOD OF PRODUCING TERPENES OR TERPENOIDS

Номер: US20170121749A1
Автор: BAUCHART Philippe, CASTANG Sandra, Chabot Nicolas, Leonetti Jean-Paul
Принадлежит: DEINOVE

The present invention relates to a recombinant bacterium exhibiting enhanced 2-C-methyl-D-erythritol 4-phosphate/1-deoxy-D-xylulose 5-phosphate (MEP/DXP) pathway, and its use for producing terpene or terpenoid compounds. 122-. (canceled)23Deinococcus. A method of producing a terpene or terpenoid comprising (i) culturing a recombinant bacterium that is genetically modified to increase 1-deoxyxylulose 5-phosphate synthase (DXS) activity and/or isopentenyl pyrophosphatase isomerase (IPP isomerase) activity , under conditions suitable to produce the terpene or terpenoid and optionally (ii) recovering the terpene or terpenoid.24Deinococcus. The method of claim 23 , wherein the recombinant bacterium overexpresses a native claim 23 , homologous or heterologous idi gene.25Deinococcus. The method of claim 23 , wherein the recombinant bacterium overexpresses a native claim 23 , homologous or heterologous dxs gene.26Deinococcus. The method of claim 23 , wherein the recombinant bacterium expresses an improved DXS enzyme.27. The method of claim 26 , wherein the improved DXS enzyme is a mutant DXS enzyme comprising a cysteine at position corresponding to position 244 of SEQ ID NO: 52.28DeinococcusD. radiopugnansD. yunweiensisD. geothermalis. The method of claim 26 , wherein the recombinant bacterium expresses a gene encoding the R244C mutant of the DXP synthase from (SEQ ID NO: 8) claim 26 , a gene encoding the R238C mutant of the DXP synthase from (SEQ ID NO: 14) or a gene encoding the R241C mutant of the DXP synthase from (SEQ ID NO: 56).29Deinococcus. The method of claim 23 , wherein the recombinant bacterium expresses an improved DXS enzyme and overexpresses a native claim 23 , homologous or heterologous idi gene.30Deinococcus. The method of claim 23 , wherein the recombinant bacterium overexpresses a native claim 23 , homologous or heterologous gene encoding FPP synthase.31. The method of claim 30 , wherein the gene encoding FPP synthase encodes a polypeptide selected from ...

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Номер записи: 77
25-04-2019 дата публикации

TRANSFORMED SYNECHOCOCCUS ELONGATUS STRAINS HAVING IMPROVED PRODUCTIVITY OF FARNESENE AND USE THEREOF

Номер: US20190119703A1
Автор: LEE Hyun-Jeong, Woo Han-Min
Принадлежит: RESEARCH & BUSINESS FOUNDATION SUNGKYUNKWAN UNIVERSITY

The present disclosure relates to the transformed strain of capable of mass production of farnesene. The transformed strain of the present disclosure is characterized by having the ability to mass produce farnesene using carbon dioxide as an independent carbon source. In particular, the strain is economically effective because it uses carbon dioxide present in light and air as a carbon source. There is an eco-friendly effect since it can be used for eliminating or reducing carbon dioxide in the atmosphere using microorganisms. Further, the strain of the present disclosure has a rapid growth rate and excellent ability to fix carbon dioxide compared with other microorganisms, thereby being utilized in various fields such as food, medicine, pharmacy, biofuel, and chemistry. 1Synechococcus elongatus. A strain comprising a farnesene synthase gene (FS) consisting of the nucleotide sequence represented by SEQ ID NO: 4.2Synechococcus elongatus. The strain according to claim 1 , the strain further comprising a deoxyxylulose-5-phosphate synthase gene (dxs) consisting of the nucleotide sequence represented by SEQ ID NO: 1.3Synechococcus elongatus. The strain according to claim 2 , the strain further comprising an isopentenyl-diphosphate delta isomerase (idi) gene consisting of the nucleotide sequence represented by SEQ ID NO: 2 and a farnesyl diphosphate synthase (ispA) gene consisting of the nucleotide sequence represented by SEQ ID NO: 3.4Synechococcus elongatus. The strain according to claim 3 , wherein the strain is a strain of Accession No. KCCM 12133P.5Synechococcus elongatus. The strain according to claim 1 , wherein the strain is transformed with a pSe2Bb1k-AFS recombinant vector having the vector map of .6Synechococcus elongatus. The strain according to claim 2 , wherein the strain is further transformed with a pSe1Bb1s-dxs recombinant vector having the vector map of .7Synechococcus elongatus. The strain according to claim 3 , wherein the strain is further transformed ...

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Номер записи: 78
16-04-2020 дата публикации

MUTATIONS IN IRON-SULFUR CLUSTER PROTEINS THAT IMPROVE XYLOSE UTILIZATION

Номер: US20200115697A1
Автор: Covalla Sean, Froehlich Allan, Henningsen Brooks, Zelle Rintze M.
Принадлежит:

There is provided an engineered host cells comprising (a) one or more mutations in one or more endogenous genes encoding a protein associated with iron metabolism; and (b) at least one gene encoding a polypeptide having xylose isomerase activity, and methods of their use thereof. 1. A recombinant yeast cell comprising (a) at least one heterologous gene encoding a protein associated with iron metabolism and/or one or more mutations in one or more endogenous gene encoding a protein associated with iron metabolism; and (b) at least one heterologous gene encoding a polypeptide having xylose isomerase activity.2. The recombinant yeast cell of claim 1 , wherein the one or more mutations in an endogenous gene is in a gene of ISU1 claim 1 , YFH1 claim 1 , NFS1 claim 1 , AFT1 claim 1 , AFT2 claim 1 , YAP5 claim 1 , FRA1 claim 1 , FRA2 claim 1 , GREX3 claim 1 , GREX4 claim 1 , CCC1 claim 1 , or any combination thereof.3. The recombinant yeast cell of claim 2 , wherein the recombinant yeast cell comprises one or more mutations in the endogenous ISU1 gene that results in a polypeptide comprising at least one amino acid substitution selected from the group consisting of D71N claim 2 , D71G claim 2 , and S98F claim 2 , wherein the position of the substitution is relative to the amino acid positions of SEQ ID NO:29.4. The recombinant yeast cell of claim 2 , wherein the recombinant yeast cell comprises one or more mutations in the endogenous YFH1 gene that results in a polypeptide comprising a T163P substitution claim 2 , wherein the position of the substitution is relative to the amino acid positions of SEQ ID NO:31.5. The recombinant yeast cell of claim 2 , wherein the recombinant yeast cell comprises one or more mutations in the endogenous NFS1 gene that results in a polypeptide comprising at least one amino acid substitution selected from the group consisting of L115W and E458D claim 2 , wherein the position of the substitution is relative to the amino acid positions of SEQ ID ...

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Номер записи: 79
27-05-2021 дата публикации

METHODS FOR STABILIZING PRODUCTION OF ACETYL-COENZYME A DERIVED COMPOUNDS

Номер: US20210155939A1
Автор: JIANG Hanxiao, Meadows Adam
Принадлежит:

The present disclosure relates to the use of a switch for the production of heterologous non-catabolic compounds in microbial host cells. In one aspect, provided herein are genetically modified microorganisms that produce non-catabolic compounds more stably when serially cultured under aerobic conditions followed by microaerobic conditions, and methods of producing non-catabolic compounds by culturing the genetically modified microbes under such culture conditions. In another aspect, provided herein are genetically modified microorganisms that produce non-catabolic compounds more stably when serially cultured in the presence of maltose followed by the reduction or absence of maltose, and methods of producing non-catabolic compounds by culturing the genetically modified microbes under such culture conditions. 1. A method for producing a heterologous non-catabolic compound in a genetically modified host cell , the method comprising:(a) culturing a population of genetically modified host cells in a culture medium comprising a carbon source under aerobic conditions, wherein the host cell comprises one or more heterologous nucleic acids encoding one or more enzymes of an enzymatic pathway for making the heterologous non-catabolic compound, wherein expression of the one or more enzymes is positively regulated by the activity of a microaerobic-responsive promoter, wherein the aerobic conditions limit the amount of heterologous non-catabolic compound produced by the host cells; and(b) culturing said population or a subpopulation thereof in a culture medium comprising a carbon source under microaerobic conditions, wherein said microaerobic conditions increases the production of the non-catabolic compound by said population or subpopulation thereof.236.-. (canceled)37. A fermentation composition comprising a population of genetically modified host cells in a culture medium comprising a carbon source , wherein the host cell comprises one or more heterologous nucleic acids ...

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Номер записи: 80
27-05-2021 дата публикации

ACETATE TOXICITY TOLERANCE IN RECOMBINANT MICROBIAL HOST CELLS

Номер: US20210155944A1
Автор: Covalla Sean, Froehlich Allan, Henningsen Brooks, Zelle Rintze
Принадлежит:

Acetate is a potent microbial inhibitor which can affect the performance of yeast in ethanolic fermentation. The present disclosure provides a recombinant microbial host cell having (i) a first genetic modification for increasing the activity of one or more proteins that function in a first metabolic pathway to convert acetate into an alcohol in the microbial host cell; (ii) a second genetic modification for increasing the activity of one or more proteins that function in a second metabolic pathway to import glycerol in the recombinant microbial host cell (iii) a third genetic modification for increasing the activity of one or more proteins that function in a third metabolic pathway to convert a C5 carbohydrate into ethanol in the microbial host cell. The recombinant microbial host cell comprises and natively expresses native proteins that function in a fourth native metabolic pathway to produce glycerol in the microbial host cell. 1. A recombinant microbial host cell having:a first genetic modification for increasing the activity of one or more proteins that function in a first metabolic pathway to convert acetate into an alcohol in the microbial host cell;a second genetic modification for increasing the activity of one or more proteins that function in a second metabolic pathway to import glycerol in the recombinant microbial host cell; anda third genetic modification for increasing the activity of one or more proteins that function in a third metabolic pathway to convert a C5 carbohydrate into the alcohol in the microbial host cell;wherein the recombinant microbial host cell comprises and natively expresses native proteins that function in a fourth native metabolic pathway to produce glycerol in the microbial host cell.2. The recombinant microbial host cell of claim 1 , wherein the alcohol is ethanol.3. The recombinant microbial host cell of claim 1 , wherein the one or more proteins that function in the first claim 1 , second or third metabolic pathway are ...

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Номер записи: 81
12-05-2016 дата публикации

BACTERIAL XYLOSE ISOMERASES ACTIVE IN YEAST CELLS

Номер: US20160130590A1
Автор: Chen Zhongqiang, Kelly Kristen J, Ye Rick W
Принадлежит:

Specific polypeptides were identified as bacterial xylose isomerases that are able to provide xylose isomerase activity in yeast cells. The xylose isomerase activity can complete a xylose utilization pathway so that yeast can use xylose in fermentation, such as xylose in biomass hydrolysate. 1. A recombinant yeast cell comprising a complete xylose utilization pathway including a codon optimized heterologous nucleic acid molecule encoding a polypeptide comprising SEQ ID NO:7 , wherein the codon optimization is for expression in a yeast cell , wherein the codon optimized heterologous nucleic acid molecule includes an operably linked promoter and is expressed producing xylose isomerase activity in the yeast cell , and wherein the heterologous nucleic acid molecule is chimeric.2. The recombinant yeast cell of claim 1 , further having the ability to grow on xylose as a sole carbon source.3. The recombinant yeast cell of claim 2 , further comprising a metabolic pathway that produces a target compound.4. The recombinant yeast cell of claim 3 , wherein the target compound is selected from the group consisting of ethanol claim 3 , butanol claim 3 , and 1 claim 3 ,3-propanediol.59-. (canceled)10. The recombinant yeast cell of claim 3 , wherein the target compound is ethanol.11. The recombinant yeast cell of claim 10 , wherein the metabolic pathway that produces the target compound comprises genes encoding the following enzymes: xylulokinase claim 10 , transaldolase claim 10 , transketolase 1 claim 10 , D-ribulose-5-phosphate 3-epimerase claim 10 , and ribose 5-phosphate ketol-isomerase.12. (canceled)13Kluyveromyces, Candida, Pichia, Hansenula, Schizosaccharomyces, Kloeckera, Schwanniomyces, YarrowiaSaccharomyces.. The recombinant yeast cell of claim 1 , wherein the yeast cell is of the genus claim 1 , or14Saccharomyces.. The recombinant yeast cell of claim 13 , wherein the yeast cell is of the genus15Saccharomyces cerevisiae.. The recombinant yeast cell of claim 14 , wherein ...

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Номер записи: 82
10-05-2018 дата публикации

ACETATE CONSUMING YEAST CELL

Номер: US20180127763A1
Автор: BOUMA ARJEN, DE WAAL Paulus Petrus, Klaassen Paul, SCHMITZ PETRUS JOHANNES
Принадлежит:

The present invention relates to a yeast cell that is genetically modified comprising: 1. A yeast cell that is genetically modified comprising:a) a disruption of one or more aldehyde dehydrogenase (E.C:1.2.1.4) native to the yeast;{'sub': '+', 'b) one or more nucleotide sequence encoding a heterologous NAD-dependent acetylating acetaldehyde dehydrogenase (E.C. 1.2.1.10);'}c) one or more nucleotide sequence encoding a homologous or heterologous acetyl-CoA synthetase (E.C. 6.2.1.1); andd) a modification that leads to reduction of glycerol 3-phosphate phosphohydrolase (E.C. 3.1.3.21) and/or glycerol 3-phosphate dehydrogenase (E.C. 1.1.1.8 or E.C. 1.1.5.3) activity, native to the yeast.2. The yeast cell according to claim 1 , wherein the one or more aldehyde dehydrogenase (E.C:1.2.1.4) native to the yeast in a) is an acetaldehyde dehydrogenase-6 (ALD6).3. The yeast cell according to claim 1 , wherein the yeast cell comprisese) one or more nucleotide sequence encoding a heterologous xylose isomerase (E.C. 5.3.1.5).4. The yeast cell according to claim 1 , wherein the yeast cell comprises a disruption of one or more of the genes gpp1 claim 1 , gpp2 claim 1 , gpd1 and gpd2 native to the yeast.5. The yeast cell according to claim 1 , wherein the yeast cell comprises further:f) one or more nucleotide sequence encoding a heterologous glycerol dehydrogenase (E.C. 1.1.1.6); andg) one or more nucleotide sequence encoding a homologous or heterologous dihydroxyacetone kinase (E.C. 2.7.1.28 or E.C. 2.7.1.29).6. The yeast cell according to claim 1 , wherein the yeast cell is a pentose and glucose fermenting yeast cell that is capable of anaerobic simultaneous pentose and glucose consumption.7. The process for the fermentation of a yeast cell according to claim 1 , wherein the fermentation time for substantially complete fermentation of acetate claim 1 , pentose and hexose is reduced relative to the corresponding fermentation of wild-type yeast.8. The process according to claim 7 , ...

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Номер записи: 83
01-09-2022 дата публикации

CAPSULE PROTEIN AND MULTIMERIC COMPLEX COMPOSITION THEREOF, AND PHARMACEUTICAL COMPOSITION USING SAME

Номер: US20220275357A1
Автор: INUI Takashi
Принадлежит: UNIVERSITY PUBLIC CORPORATION OSAKA

There has been an idea to load a pharmaceutical agent in a barrel structure of a lipocalin-type prostaglandin D synthase, and to seal the pharmaceutical agent in the barrel structure by introducing a disulfide bond between H-helix and E-F loop. 1. A capsule protein including human lipocalin-type prostaglandin D synthase , wherein the synthase has substitution of alanine (A) for cysteine (C) , at the active center of the synthase; and substitution of at least one barrier amino acid residues for amino acid residues in β-strand D of the synthase.22. The capsule protein according to claim 1 , wherein a disulfide bond has been introduced between E-F loop and α-helix H.3. The capsule protein according to claim 1 , wherein a targeting peptide is bound to N-terminus or C-terminus of the capsule protein.4. The capsule protein according to claim 1 , wherein the barrier amino acid is at least one amino acid selected from the group consisting of lysine (K) claim 1 , histidine (H) claim 1 , tryptophan (W) claim 1 , tyrosine (Y) claim 1 , and phenylalanine (F).5. A multimeric composition containing a plurality of capsule proteins claim 1 , each of the capsule proteins is the capsule protein according to .6. The multimeric composition of a capsule protein according to claim 5 , wherein the multimeric composition is a tetramer or an octamer.7. The multimeric composition of a capsule protein according to claim 6 , wherein the capsule protein is bound to a tetramer of streptavidin via biotin in the multimeric composition.8. A pharmaceutical composition comprising a drug in the capsule protein according to .9. The pharmaceutical composition according to claim 8 , wherein the composition is lyophilized.10. A processed food comprising a complex having non-drug compound contained in the capsule protein according to . The present invention relates to a capsule protein and a multimeric composition thereof that can be used as a drug delivery system (DDS). Specifically, it is directed to a ...

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Номер записи: 84
21-05-2015 дата публикации

GENETICALLY ENGINEERED YEAST CELL CAPABLE OF PRODUCING LACTATE, METHOD OF PRODUCING THE SAME, AND METHOD OF PRODUCING LACTATE BY USING THE CELL

Номер: US20150140625A1
Автор: Cho Kwangmyung, Kang Changduk, LEE Juyoung, LEE SEUNGHYUN, LEE Soyoung, PARK Youngkyoung, Song Jiyoon
Принадлежит:

A genetically engineered yeast cell capable of producing lactate having increased TPI activity, a method of preparing the yeast cell, and a method of producing lactate by using the yeast cell. 1. A genetically engineered yeast cell capable of producing lactate , wherein the yeast cell has an exogenous gene encoding triose-phosphate isomerase (TPI) and an increased triose-phosphate isomerase (TPI) activity compared to a parent yeast cell.2SaccharomycesKluyveromycesCandidaPichiaIssatchenkiaDebaryomycesZygosaccharomycesSaccharomycopsis. The genetically engineered yeast cell of claim 1 , wherein the yeast cell is genus claim 1 , genus claim 1 , genus claim 1 , genus claim 1 , ) genus claim 1 , ) genus claim 1 , ) genus claim 1 , or ) genus.3. The genetically engineered yeast cell of claim 1 , wherein the yeast cell comprises an increased copy number of a gene encoding TPI as compared to a parent yeast cell claim 1 , or modification of an expression-regulation sequence of the gene.4. The genetically engineered yeast cell of claim 3 , wherein the TPI gene is an endogenous gene.5. The genetically engineered yeast cell of claim 1 , wherein the TPI gene is a heterologous gene.6Saccharomyces cerevisiae, Trypanosoma brucei. The genetically engineered yeast cell of claim 5 , wherein the TPI is from claim 5 , a rabbit claim 5 , or a combination thereof.7. The genetically engineered yeast cell of claim 1 , wherein the TPI has 60% or more sequence identity with any one of SEQ ID NOS: 1 to 9.8. The genetically engineered yeast cell of claim 1 , wherein the gene encoding TPI comprises a nucleotide sequence selected from SEQ ID NOS: 10 to 13.9. The genetically engineered yeast cell of claim 1 , wherein the genetically engineered yeast cell has reduced activity of a polypeptide that converts pyruvate to acetaldehyde claim 1 , a polypeptide that converts lactate to pyruvate claim 1 , a polypeptide that converts dihydroxyacetone phosphate (DHAP) to glycerol-3-phosphate claim 1 , or a ...

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Номер записи: 85
18-05-2017 дата публикации

L-arabinose Isomerase Variants with Improved Conversion Activity and Method for Production of D-tagatose Using them

Номер: US20170137856A1
Автор: CHO Kyong Yeon, CHO Seung Hyun, KIM Chang Gyeom, KIM Jin Ha, Kim Seong Bo, KIM Yang Hee, OH In Seok, YANG Sung Jae
Принадлежит:

The present invention relates to the development of an L-arabinose isomerase variant from DSM 5068, which is a kind of thermophile, on the basis of protein molecular modeling. Moreover, the present invention relates to a method of producing D-tagatose from D-galactose by using the enzyme or a microorganism of the genus expressing the enzyme. 1. A method for producing D-tagatose , the method comprising converting D-galactose into D-tagatose by the arabinose isomerase variant having an increased activity of converting D-galactose into D-tagatose , the arabinose isomerase variant having a substitution of an amino acid other than phenylalanine for an amino acid at position 275 and a substitution of proline for an amino acid at position 469 of the amino acid sequence set forth in SEQ ID NO: 1.2. The method for producing D-tagatose of claim 1 , wherein the substitution of the amino acid for the amino acid at position 275 is any one amino acid selected from the group consisting of valine claim 1 , methionine and isoleucine.3. The method for producing D-tagatose of claim 1 , the method comprising reacting a solution containing D-galactose according to with a metal ion source selected from the group consisting of manganese ions claim 1 , magnesium ions and zinc ions in the presence of the arabinose isomerase variant according to .4. The method for producing D-tagatose of claim 3 , wherein the metal ion source is contained at a concentration of 0.1 mM to 10 mM. This application is a continuation of U.S. application Ser. No. 15/112,232, filed Jul. 18, 2016. U.S. application Ser. No. 15/112,232 is a National Stage Entry of International Application No. PCT/KR2014/003658 filed on Apr. 25, 2014 (WO 2015/133678), and claims the benefit of PCT/KR2014/001789, filed on Mar. 5, 2014, which is hereby incorporated by reference in its entirety for all purposes as if fully set forth herein.The present invention relates to an L-arabinose isomerase variant from DSM 5068, which is produced ...

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Номер записи: 86
08-09-2022 дата публикации

NOVEL FUCOSE ISOMERASE AND FUCOSE PRODUCTION METHOD USING SAME

Номер: US20220282237A1
Автор: Kim Do Hyoung, KIM In Jeong, Kim Kyoung Heon, Nam Ki Hyun
Принадлежит: KOREA UNIVERSITY RESEARCH AND BUSINESS FOUNDATION

The present invention relates to a novel fucose isomerase and a fucose production method using same. More specifically, in a reversible reaction between L-fucose and L-fuculose, an L-fucose isomerase, derived from a sp. KDH 14 strain isolated from abalone intestines, favors the reaction progressing from L-fuculose to L-fucose, and thus the present invention provides the effect of applying same to the production of L-fucose. 1. An L-fucose isomerase which comprises the amino acid sequence of SEQ ID NO: 1 and favors a conversion reaction from L-fuculose to L-fucose in a reversible reaction between L-fucose and L-fuculose.2Raoultella. The L-fucose isomerase of claim wherein the L-fucose isomerase is derived from a sp. KDH 14 strain.3. The L-fucose isomerase of claim 1 , wherein activity of the L-fucose isomerase is increased by one or more metal ions selected from the group consisting of Mn claim 1 , Mg claim 1 , Co claim 1 , Cdand Zn.4. The L-fucose isomerase of claim 1 , wherein activity of the L-fucose isomerase is inhibited by one or more metal ions selected from the group consisting of Fe claim 1 , Caand Cu.5. A nucleic acid molecule encoding the L-fucose isomerase of .6. The nucleic acid molecule of claim 5 , wherein the nucleic acid molecule comprises the base sequence of SEQ ID NO: 2.7. A recombinant vector comprising the nucleic acid molecule of .8. A host cell transformed with the recombinant vector of .9. A method for preparing an L-fucose isomerase claim 8 , the method comprising: expressing an L-fucose isomerase by culturing the host cell of ; and obtaining the expressed L-fucose isomerase.10. A composition for producing L-fucose comprising the fucose isomerase of ; and one or more substrates selected from the group consisting of L-fuculose and D-ribulose.11. The composition of claim 10 , further comprising one or more metal ions selected from the group consisting of Mn claim 10 , Mg claim 10 , Co claim 10 , Cdand Zn.12. A method for producing L-fucose ...

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Номер записи: 87
08-09-2022 дата публикации

Cell-free production of sugars

Номер: US20220282291A1
Автор: Daniel MacEachran, Drew S. Cunningham, Matthew Eduardo Moura, William Jeremy Blake
Принадлежит: Greenlight Biosciences Inc

Provided herein, in some embodiments, are systems, methods, and compositions (e.g., cells and cell lysates) for enzymatically converting a polymeric glucose carbohydrate (e.g., starch) to sugar.

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Номер записи: 88
09-05-2019 дата публикации

RECOMBINANT KOMAGATAEIBACTER GENUS MICROORGANISM HAVING ENHANCED CELLULOSE PRODUCTIVITY, METHOD OF PRODUCING CELLULOSE USING THE SAME, AND METHOD OF PRODUCING THE MICROORGANISM

Номер: US20190135877A1
Автор: Chung Soonchun, Park Jinhwan, Shim Wooyong
Принадлежит:

A recombinant microorganism of the genus having enhanced cellulose productivity and yield, a method of producing cellulose using the recombinant microorganism, and a method of producing the recombinant microorganism are provided. 1Komagataeibacter. A recombinant microorganism having enhanced cellulose productivity , the microorganism comprising a genetic modification that increases activity of 6-phosphogluconate dehydrogenase (GND).2. The recombinant microorganism of claim 1 , wherein the genetic modification increases expression of a gene that encodes GND.3. The recombinant microorganism of claim 1 , wherein the genetic modification is an increase in the copy number of a gene that encodes GND claim 1 , or modification of an expression regulatory sequence of a gene that encodes GND.4. The recombinant microorganism of claim 1 , wherein GND belongs to EC 1.1.1.44.5. The recombinant microorganism of claim 1 , wherein GND has about 85% or more sequence identity with SEQ ID NO: 1.6. The recombinant microorganism of claim 1 , further comprising at least one of a genetic modification that increases activity of phosphofructose kinase (PFK) and a genetic modification that increases activity of phosphoglucose isomerase (PGI).7. The recombinant microorganism of claim 1 , further comprising at least one of a genetic modification that increases expression of a gene that encodes PFK and a genetic modification that increases expression of a gene that encodes PGI.8. The recombinant microorganism of claim 1 , further comprising at least one of a genetic modification that increases a copy number of a gene that encodes PFK claim 1 , a genetic modification that increases a copy number of a gene that encodes PGI claim 1 , a modification of an expression regulatory sequence of a gene that encodes PFK claim 1 , and a modification of an expression regulatory sequence of a gene that encodes PGI.9. The recombinant microorganism of claim 6 , wherein PFK and PGI belong to EC 2.7.1.11 and EC 5. ...

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Номер записи: 89
30-04-2020 дата публикации

ENZYMATIC PRODUCTION OF HEXOSES

Номер: US20200131499A1
Автор: ROGERS Edwin O., WICHELECKI Daniel Joseph
Принадлежит: BONUMOSE LLC

Disclosed herein are methods of producing hexoses from saccharides by enzymatic processes. The methods utilize fructose 6-phosphate and at least one enzymatic step to convert it to a hexose. 1. An enzymatic process for preparing fructose from sucrose , the process comprising the steps of:(i) a step of converting sucrose to glucose 1-phosphate (G1P) using sucrose phosphorylase;(ii) a step of converting G1P to glucose 6-phosphate (G6P), wherein the step is catalyzed by phosphoglucomutase (PGM)(iii) a step of converting G6P to fructose 6-phosphate (F6P), wherein the step is catalyzed by phosphoglucoisomerase (PGI)(iv) a step of converting F6P to fructose catalyzed by fructose 6-phosphate phosphatase (F6PP).2. The process of claim 1 , wherein the process steps are conducted under at least one of the following process conditions:at a temperature ranging from about 37° C. to about 85° C.,at a pH ranging from about 5.0 to about 9.0, orfor about 0.5 hours to about 48 hours.3. The process of claim 1 , wherein the process steps are conducted under at least one of the following process conditions:without adenosine triphosphate (ATP) as a source of phosphate,without nicotinamide adenosine dinucleotide,at a phosphate concentration from about 0.1 mM to about 150 mM,where phosphate is recycled, orwhere step (iv) involves an energetically favorable chemical reaction.4. The process of claim 3 , wherein phosphate is recycled claim 3 , and the phosphate produced by F6PP dephosphorylation of F6P is used in the process step of converting sucrose to G1P.5. The process of claim 3 , wherein the step of converting F6P to fructose is an energetically favorable claim 3 , irreversible phosphatase reaction.6. The process of claim 1 , wherein the process steps are conducted in a single reaction vessel. This application is a Divisional Application of U.S. application Ser. No. 16/542,560, filed Aug. 16,2019; which is a Continuation Application of PCT International Application No. PCT/US2018/022185 ...

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Номер записи: 90
10-06-2021 дата публикации

RECOMBINANT MICROORGANISM CAPABLE OF SIMULTANEOUS FERMENTATION OF MIXED SUGARS AND METHOD FOR PRODUCING DIOL USING SAME

Номер: US20210171960A1
Автор: PARK Jong-Myoung, RATHNASINGH Chelladurai, SONG Hyo-Hak
Принадлежит:

The present invention relates to a recombinant microorganism which is capable of simultaneously fermenting at least two sugars in a lignocellulosic saccharified liquid, and also capable of generating diol. 1. A recombinant microorganism having:simultaneous fermentation ability of at least two sugars in lignocellulosic hydrolysate; anddiol production ability.2klebsiella.. The recombinant microorganism of claim 1 , wherein the microorganism is a3. The recombinant microorganism of claim 1 , wherein the lignocellulosic hydrolysate comprises pentose and hexose claim 1 , wherein the recombinant microorganism has simultaneous fermentation ability of pentose and hexose.4. The recombinant microorganism of claim 1 , wherein a catabolite repression mechanism is more inhibited in the recombinant microorganism than in a wild-type microorganism.5. The recombinant microorganism of claim 1 , wherein a glucose-specific phosphotransferase enzyme IIBC component or a glucose-specific phosphotransferase enzyme IIA component of a phosphotransferase system (PTS) is more inhibited in the recombinant microorganism than in a wild-type microorganism.6. The recombinant microorganism of claim 1 , wherein a pathway along which xylose is converted to xylulose and then to xylulose-5-P or ribulose-5-P or ribose-5-P or fructose-6-P or erythrose-4-P or glyceraldehyde-3-P is more activated in the recombinant microorganism than in a wild-type microorganism.7. The recombinant microorganism of claim 1 , wherein the recombinant microorganism has enhanced activity of at least one enzyme selected from a group consisting of xylose isomerase claim 1 , xylulokinase claim 1 , D-ribulose-5-phosphate 3-epimerase claim 1 , ribose 5-phosphate isomerase claim 1 , transaldolase claim 1 , and transketolase.8. The recombinant microorganism of claim 1 , wherein the recombinant microorganism has inhibited activity of a receptor protein of cyclic adenosine monophosphate (cAMP).9. The recombinant microorganism of claim 1 , ...

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Номер записи: 91
24-05-2018 дата публикации

Microbial fermentation for the production of terpenes

Номер: US20180142265A1
Автор: Fungmin Liew, Michael Koepke, Wendy Yiting Chen
Принадлежит: Lanzatech New Zealand Ltd

The invention provides a method for producing a terpene or a precursor thereof by microbial fermentation. Typically, the method involves culturing a recombinant bacterium in the presence of a gaseous substrate whereby the bacterium produces a terpene or a precursor thereof, such as mevalonic acid, isopentenyl pyrophosphate, dimethylallyl pyrophosphate, isoprene, geranyl pyrophosphate, farnesyl pyrophosphate, and/or farnesene. The bacterium may comprise one or more exogenous enzymes, such as enzymes in mevalonate, DXS, or terpene biosynthesis pathways.

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Номер записи: 92
24-05-2018 дата публикации

ELECTRON CONSUMING ETHANOL PRODUCTION PATHWAY TO DISPLACE GLYCEROL FORMATION IN S. CEREVISIAE

Номер: US20180142267A1
Автор: Argyros Aaron, Barrett Trisha, IV Arthur J., Shaw
Принадлежит:

The present invention provides for a mechanism to completely replace the electron accepting function of glycerol formation with an alternative pathway to ethanol formation, thereby reducing glycerol production and increasing ethanol production. In some embodiments, the invention provides for a recombinant microorganism comprising a down-regulation in one or more native enzymes in the glycerol-production pathway. In some embodiments, the invention provides for a recombinant microorganism comprising an up-regulation in one or more enzymes in the ethanol-production pathway. 160-. (canceled)61. A co-culture comprising at least two host cells wherein (i) a heterologous nucleic acid encoding a phosphoketolase;', '(ii) at least one heterologous nucleic acid encoding an enzyme in an acetyl-CoA production pathway;', '(iii) a heterologous nucleic acid encoding a bifunctional acetaldehyde-alcohol dehydrogenase; and,', '(iv) at least one genetic modification that leads to the down-regulation of an enzyme in a glycerol-production pathway; and,, '(a) one of the host cells comprises(b) another host cell that is genetically distinct from (a).62. The co-culture of claim 61 , wherein the host cell is a yeast and the genetically distinct host cell is a yeast or bacterium.63. The recombinant microorganism of claim 61 , wherein said phosphoketolase is a single-specificity phosphoketolase with the Enzyme Commission Number 4.1.2.9.64. The recombinant microorganism of claim 61 , wherein said phosphoketolase is dual-specificity phosphoketolase with the Enzyme Commission Number 4.1.2.22.65Aspergillus, Neurospora, Lactobacillus, Bifidobacterium, Penicillium, LeuconostocOenococcus.. The recombinant microorganism of claim 61 , wherein said phosphoketolase is from a genus selected from the group consisting of claim 61 , and66. The recombinant microorganism of claim 61 , wherein said phosphoketolase corresponds to a polypeptide selected from a group consisting of SEQ ID NOs: 9 claim 61 , 11 claim ...

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Номер записи: 93
25-05-2017 дата публикации

METHODS, HOSTS, AND REAGENTS RELATED THERETO FOR PRODUCTION OF UNSATURATED PENTAHYDROCARBONS, DERIVATIVES AND INTERMEDIATES THEREOF

Номер: US20170145441A1
Автор: Conradie Alex Van Eck
Принадлежит:

This application describes methods, including non-naturally occurring methods, for biosynthesizing unsaturated pentahydrocarbons, such as isoprene and intermediates thereof, via the mevalonate pathway, as well as non-naturally occurring hosts for producing isoprene. 1. A method for synthesizing isoprene in a chemolithotrophic host comprising:enzymatically converting acetoacetyl-CoA to 3-hydroxy-3-methylglutaryl-CoA using a polypeptide having the activity of a hydroxymethylglutaryl-CoA synthase enzyme having the amino acid sequence set forth in SEQ ID No: 2 or 10 or a functional fragment of said enzyme; andenzymatically converting 3-hydroxy-3-methylglutaryl-CoA to (R)-mevalonate using a polypeptide having the activity of a hydroxymethylglutaryl Co-A reductase enzyme having the amino acid sequence set forth in SEQ ID No: 3 or 9 or a functional fragment of said enzyme.2. (canceled)3. The method of claim 1 , further comprising at least one of:enzymatically converting acetyl-CoA to acetoacetyl-CoA using a polypeptide having the activity of an acetyl-CoA acetyltransferase enzyme having the amino acid sequence set forth in SEQ ID No: 1 or 9 or a functional fragment of said enzyme;enzymatically converting (R)-mevalonate to (R)-5-phosphomevalonate using a polypeptide having the activity of a mevalonate-kinase enzyme having the amino acid sequence set forth in SEQ ID No: 4 or 11 or a functional fragment of said enzyme;enzymatically converting (R)-5-phosphomevalonate to (R)-5-diphosphomevalonate using a polypeptide having the activity of a phosphomevalonate kinase enzyme having the amino acid sequence set forth in SEQ ID No: 5 or 12 or a functional fragment of said enzyme;enzymatically converting (R)-5-diphosphomevalonate to isopentenyl diphosphate using a polypeptide having the activity of a diphosphomevalonate decarboxylase enzyme having the amino acid sequence set forth in SEQ ID No: 6 or 13 or a functional fragment of said enzyme;enzymatically converting isopentenyl ...

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Номер записи: 94
02-06-2016 дата публикации

METHOD OF INHIBITING BINDING OR ACTIVITY OF MIF BY ADMINISTERING A MIF ANTAGONIST

Номер: US20160152708A1
Автор: Bucala Richard J., Leng Lin, Metz Christine N.
Принадлежит:

Methods and compositions for using the MHC class II invariant chain polypeptide, Ii (also known as CD74), as a receptor for macrophage migration inhibitory factor (MIF), are disclosed. These include methods and compositions for using this receptor, as well as agonists and antagonists of MIF which bind to this receptor, or which otherwise modulate the interaction of MIF with CD74 or the consequences of such interaction, in treatment of conditions characterized by locally or systemically altered MIF levels, particularly inflammatory conditions and cancer. 1. A method for screening compounds for an agonist or antagonist of MIF comprising:contacting an MHC class II invariant chain (Ii) polypeptide with MIF in the presence and absence of a candidate compound, and a candidate compound that enhances the interaction of said MIF with said Ii polypeptide is identified as an agonist of MIF, and', 'a candidate compound that inhibits the interaction of said MIF with said Ii polypeptide is identified as an antagonist of MIF;, 'comparing the interaction of the MIF and said Ii polypeptide in the presence of said candidate compound with their interaction in the absence of said candidate compound, whereby'}{'figref': {'@idref': 'DRAWINGS', 'FIG. 5'}, 'wherein said Ii polypeptide comprises the complete Ii amino acid sequence of (SEQ ID. NO:2) or an MIF-binding fragment thereof.'}2. An agonist or antagonist of MIF identified by the method of .3. An agonist or antagonist according to which is an antibody or antigen-binding fragment thereof.4. The agonist or antagonist according to wherein said antibody is an anti-CD74 antibody.5. An anti-CD74 antibody of selected from the group consisting of a monoclonal antibody claim 4 , a human antibody claim 4 , a humanized antibody and a chimeric antibody.6. A method of inhibiting an effect of MIF on a cell comprising on its surface an MHC class II invariant chain (Ii) polypeptide which binds MIF and thereby mediates said effect of MIF claim 4 , ...

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Номер записи: 95
15-09-2022 дата публикации

ENZYMATIC PRODUCTION OF HEXOSES

Номер: US20220290117A1
Автор: ROGERS Edwin O., WICHELECKI Daniel Joseph
Принадлежит: BONUMOSE, INC.

Disclosed herein are methods of producing hexoses from saccharides by enzymatic processes. The methods utilize fructose 6-phosphate and at least one enzymatic step to convert it to a hexose. 1. A process for preparing mannose from a saccharide , the process comprising:converting fructose 6-phosphate (F6P) to mannose 6-phosphate (M6P) catalyzed by mannose 6-phosphate isomerase (M6PI) or phosphoglucose/phosphomannose isomerase (PGPMI); andconverting the M6P to mannose catalyzed by mannose 6-phosphate phosphatase (M6PP).2. The process of claim 1 , further comprising a step of converting glucose 6-phosphate (G6P) to the F6P claim 1 , wherein the step is catalyzed by a phosphoglucoisomerase (PGI) or PGPMI.3. The process of claim 2 , further comprising the step of converting glucose 1-phosphate (G1P) to the G6P claim 2 , wherein the step is catalyzed by a phosphoglucomutase (PGM).4. The process of claim 3 , further comprising the step of converting a saccharide to the G1P claim 3 , wherein the step is catalyzed by at least one enzyme claim 3 , wherein the saccharide is starch claim 3 , a starch derivative claim 3 , or sucrose.5. The process of claim 4 , wherein the at least one enzyme in the step of converting a saccharide to the G1P is selected from the group consisting of an alpha-glucan phosphorylase (αGP) claim 4 , a sucrose phosphorylase claim 4 , and mixtures thereof.6. The process of claim 4 , wherein the saccharide is starch or a derivative thereof selected from the group consisting of amylose claim 4 , amylopectin claim 4 , soluble starch claim 4 , amylodextrin claim 4 , maltodextrin claim 4 , maltose claim 4 , and glucose claim 4 , and mixtures thereof.7. The process of claim 6 , further comprising the step of converting starch to a starch derivative wherein the starch derivative is prepared by enzymatic hydrolysis of starch or by acid hydrolysis of starch.8. The process of claim 6 , wherein 4-glucan transferase (4GT) is added to the process.9. The process of ...

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Номер записи: 96
16-05-2019 дата публикации

Recombinant Bacillus Subtilis for Increasing Production of Acetylglucosamine and Construction Method Thereof

Номер: US20190144875A1
Автор: Chen Jian, Du Guocheng, Li Jianghua, Liu Long, NIU Tengfei
Принадлежит:

The invention discloses a method for improving the yield of acetylglucosamine, which belongs to the technical field of genetic engineering. In the invention, the recombinant S5 (S5-PxylA-glmS-P43-GNA1) is taken as a starting strain, and the glmS ribozyme is integrated into the mid of rbs and the promoter sequence of the glmM and pfkA gene, respectively. The ribozyme mutant has the advantage of prolonging the stability of the mRNA and integrated into the mid of rbs and the promoter sequence of the pgi gene. The yield of GlcNAc of the recombinant strain reaches 11.79-20.05 g/L. This laid the foundation for the further metabolic engineering of to produce GlcNAc. 1Bacillus subtilisBacillus subtilis. A recombinant strain of for producing acetylglucosamine , wherein the recombinant is competent to dynamically regulate glmM , pfkA and pgi expression using a glmS ribozyme and/or a glmS ribozyme mutant.2Bacillus subtilisBacillus subtilis. The recombinant strain of of claim 1 , wherein the recombinant is competent to dynamically downregulate glmM and pfkA expression using the glmS ribozyme and claim 1 , and dynamically upregulate pgi expression using the glmS ribozyme mutant.3Bacillus subtilisBacillus subtilisBacillus subtilis. The recombinant strain of of claim 1 , wherein the recombinant is constructed by homologous recombination to integrate a gene encoding glmS ribozyme into a genome of between a promoter and a rbs sequence of glmM and pfkA claim 1 , respectively claim 1 , and integrate a gene encoding a mutant of glmS ribozyme into the genome between a promoter and a rbs sequence of pgi.4Bacillus subtilisBacillus subtilis. The recombinant strain of of claim 3 , wherein the is used as a host.5Bacillus subtilisBacillus subtilisBacillus subtilisBacillus subtilis. The recombinant strain of of claim 4 , wherein the is 168 claim 4 , and the 168 is used as a host.6Bacillus subtilis. The recombinant strain of of claim 3 , wherein a sequence of the gene encoding glmS ribozyme is ...

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Номер записи: 97
07-05-2020 дата публикации

CELLS WITH IMPROVED PENTOSE CONVERSION

Номер: US20200140900A1
Автор: De Jong Rene Marcel, JONKERS Maria Bernedina Elizabeth, Klaassen Paul, TEUNISSEN Aloysius Wilhelmus Rudolphus Hubertus
Принадлежит:

The invention relates to a cell capable of converting one or more pentose sugar and one or more hexose sugar into fermentation product constitutively expressing one or more heterologous or homologous polypeptide having the amino acid sequence set out in SEQ ID NO: 20, or a variant polypeptide thereof having at least 45% identity to SEQ ID NO 20. In an embodiment the heterologous polypeptide has glyoxalase activity. 1. A cell capable of converting one or more pentose sugar and one or more hexose sugar into fermentation product constitutively expressing one or more heterologous or homologous polypeptide having the amino acid sequence set out in SEQ ID NO: 20 or a variant polypeptide thereof , having at least 45% identity to SEQ ID NO 20.2. A cell according to claim 1 , wherein the heterologous polypeptide has glyoxalase activity claim 1 , optionally comprising glyoxalase I activity.3. An cell capable of converting one or more pentose sugar and or one or more hexose sugar into fermentation product comprising a constitutively expressed heterologous or homologous polynucleotide which comprises:(a) the nucleotide sequence as set out in SEQ ID NO: 27;(b) a nucleotide sequence having at least about 50% sequence identity with the nucleotide sequence of SEQ ID NO: 27;(c) a fragment of a nucleotide sequence as defined in (a), (b) or (c) having at least 100 nucleotides;(d) a sequence which is degenerate as a result of the genetic code to a sequence as defined in any one of (a), (b), or (c);(e) a nucleotide sequence which is the reverse complement of a nucleotide sequence as defined in (a), (b), (c), or (d).4. A cell according to claim 1 , comprising a nucleotide sequence encoding a xylose isomerase.5. A cell according to claim 1 , wherein the cell comprises one or more genetic modifications resulting in:(a) an increase in transport of xylose in the cell;(b) an increase in xylulose kinase activity;(c) an increase in flux through the pentose phosphate pathway;(d) a decrease in ...

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Номер записи: 98
07-05-2020 дата публикации

CELL-FREE PRODUCTION OF SUGARS

Номер: US20200140907A1
Автор: Blake William Jeremy, Cunningham Drew S., MacEachran Daniel, Moura Matthew Eduardo
Принадлежит: GreenLight Biosciences, Inc.

Provided herein, in some embodiments, are systems, methods, and compositions (e.g., cells and cell lysates) for enzymatically converting a polymeric glucose carbohydrate (e.g., starch) to sugar. 168.-. (canceled)69. A method for producing allulose , the method comprising:{'i': 'Brevibacillus thermoruber', 'converting fructose 6-phosphate (F6P) to allulose-6-phosphate (A6P), catalyzed by a allulose 6-phosphate epimerase (A6PE); and'}converting A6P to allulose, catalyzed by an allulose 6-phosphate phosphatase (A6PP), wherein the A6PP is encoded by a nucleic acid sequence expressed in a microbial cell.70. The method of claim 69 , wherein the A6PE is claim 69 , the A6PP is claim 69 , or both the A6PE and A6PP are thermostable or engineered to be thermostable.71. The method of claim 69 , further comprising converting glucose 6-phosphate (G6P) to the F6P claim 69 , catalyzed by a phosphoglucoisomerase encoded by a nucleic acid sequence expressed in a microbial cell.72. The method of claim 69 , further comprising converting glucose 1-phosphate (G1P) to the G6P claim 69 , catalyzed by a phosphoglucomutase encoded by a nucleic acid sequence expressed in a microbial cell.73. The method of claim 72 , further comprising converting a polymeric glucose carbohydrate to the G1P claim 72 , catalyzed by an α-glucan phosphorylase or a cellodextrin phosphorylase encoded by a nucleic acid sequence expressed in a microbial cell.74. The method of claim 73 , wherein the polymeric glucose carbohydrate is selected from starches claim 73 , cellodextrins claim 73 , maltodextrins claim 73 , and glycogens.75. The method of claim 73 , further comprising treating the polymeric glucose carbohydrate with a debranching enzyme.76. The method of claim 75 , wherein the debranching enzyme is selected from isoamylases and pullulanases encoded by a nucleic acid sequence expressed in a microbial cell.77Thermoanaerobacter wiegeliiThermoanaerobacter ethanolicusThermus islandicusDeinococcus ...

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Номер записи: 99
17-06-2021 дата публикации

NEW IMPROVED GLUCOSE ISOMERASES

Номер: US20210180039A1
Автор: Birikh Klara, Suonpaa Anu Minna Maaret
Принадлежит:

The invention is in the field of enzymology. More in particular, it provides a method for the isomerization of glucose into fructose wherein the glucose is derived from lignocellulosic material. More in particular, the invention provides polypeptides encoding mutant glucose isomerase enzymes with improved glucose isomerase activity as compared to the corresponding wild type enzyme. The disclosed polypeptides are particularly suited for converting glucose to fructose in the presence of xylose. 1. A polypeptide with glucose isomerase activity , the polypeptide comprising:an amino acid sequence that is at least 90% identical to the full length of the amino acid sequence of SEQ ID NO: 1 or SEQ ID NO: 2,wherein the polypeptide comprises a Glycine, Serine, Alanine or Cysteine residue at a position corresponding to position 104 in SEQ ID NO: 1 or SEQ ID NO: 2.2. The polypeptide of claim 1 , wherein the polypeptide comprises a Glycine residue at a position corresponding to position 104 in SEQ ID NO: 1 or SEQ ID NO: 2.3. The polypeptide of claim 1 , wherein the polypeptide comprises an amino acid sequence that is at least 90% identical to the full length of the amino acid sequence of SEQ ID NO: 1.4. The polypeptide of claim 1 , wherein the polypeptide is an isolated polypeptide.5. (canceled)6. A nucleic acid encoding the polypeptide of .7. The nucleic acid of claim 6 , wherein the nucleic acid is comprised in a vector.8. (canceled)9. The nucleic acid of claim 6 , wherein the nucleic acid is comprised in a recombinant host cell.10Escherichia coli, Bacillus, Corynebacterium, Pseudomonas, Pichia pastoris, Saccharomyces cerevisiae, Yarrowia lipolytica. The nucleic acid of claim wherein the host cell is selected from the group consisting of claim 6 , filamentous fungi claim 6 , yeast claim 6 , and insect cells.11. A method for producing the polypeptide of claim 1 , the method comprising:{'claim-ref': {'@idref': 'CLM-00006', 'claim 6'}, 'culturing a recombinant host cell ...

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