КОМПОЗИЦИЯ ДЛЯ ПОЛУЧЕНИЯ ТАГАТОЗЫ И СПОСОБ ПОЛУЧЕНИЯ ТАГАТОЗЫ ИЗ ФРУКТОЗЫ

Группа изобретений относится к получению тагатозы из фруктозы. Предложен белок для получения тагатозы из фруктозы, имеющий аминокислотную последовательность, представленную в SEQ ID NO:1-7. Предложен также рекомбинантный микроорганизм для получения тагатозы из фруктозы, экспрессирующий указанный белок. Предложен также способ получения тагатозы из фруктозы, включающий приведение в контакт вышеуказанных белка или микроорганизма с фруктозой и получение тагатозы. Изобретение обеспечивает получение тагатозы из фруктозы с высоким выходом. 3 н. и 18 з.п. ф-лы, 42 ил., 2 табл., 3 пр.

PRODUCTION METHOD FOR TAGATOSE

The present invention relates to a production method for tagatose.

METHOD OF PRODUCTION OF MONOSACCHARIDES

The present invention is directed towards genetic modification of native gene encoding for D-tagatose 3-epimerase and rhamnose isomerase to substantially increase the expression level of these enzymes and use of said enzymes in a process to produce rare monosaccharides such as psicose and allose. Also disclosed in the present invention is expression constructs comprising the modified genes and a host cells to express the same.

COMPOSITION FOR PREPARING TAGATOSE AND METHOD FOR PREPARING TAGATOSE FROM FRUCTOSE

Novel D - psicose 3 - epimerase and application thereof

D-PSICOSE 3-EPIMERASE MUTANT WITH IMPROVED THERMAL STABILITY, AND CONTINUOUS PRODUCTION OF D-PSICOSE USING SAME

The present invention relates to a D-psicose 3-epimerase mutant of which the thermal stability is improved by substituting an amino acid of a specific sequence number. In addition, the present invention relates to a recombinant vector comprising the gene of the D-psicose 3-epimerase mutant, and a recombinant strain transformed with the recombinant vector. Further, the present invention relates to an immobilized reactor prepared using the enzyme mutant or the recombinant vector, and a method for producing D-psicose using the immobilized reactor.

METHOD FOR PRODUCING PSICOSE FROM FRUCTOSE-CONTAINING SUBSTRATE

The present invention relates to a method of obtaining a psicose-containing product from a fructose-containing substrate with high productivity in a short time on an industrial scale by an immobilization reaction using a biocatalyst for producing a psicose, and a method of preparing a liquid type or powder type of psicose by isolating the psicose-containing product obtained by the method and preparing a psicose continuously by inputting a byproduct of isolation process into a process of production of psicose-containing product.

НОВАЯ D-ПСИКОЗО-3-ЭПИМЕРАЗА И СПОСОБ ПОЛУЧЕНИЯ D-ПСИКОЗЫ С ЕЕ ИСПОЛЬЗОВАНИЕМ

Изобретение относится к биотехнологии. Описано применение фермента D-псикозо-3-эпимеразы для получения D-псикозы из D-фруктозы, а также способ получения последней с использованием этого фермента или микроорганизма, его продуцирующего. Изобретение позволяет получить моносахарид D-псикозу из D-фруктозы с использованием указанного фермента. 6 н. и 3 з.п. ф-лы, 5 ил., 4 табл., 4 пр.

ФЕРМЕНТАТИВНОЕ ПОЛУЧЕНИЕ D-АЛЛЮЛОЗЫ

D-Ketohexose-3-Epimerase, und seine Herstellung und Verwendung

Ketose 3-epimerase proteins

Ketose 3-epimerase proteins comprise a polypeptide sequence having at least 70% sequence identity to SEQ ID NO: 6, SEQ ID NO: 2 or SEQ ID NO: 4, these sequences being derived from Desmospora sp 8437, Clostridium scindens and Clostridium hylemonae respectively. Nucleic acids encoding these proteins are provided, and the proteins (or host cells comprising the encoding nucleic acids) may be used for the production of allulose (D-psicose) from fructose.

METHOD FOR PRODUCING D-PSICOSE FROM D-PSICOSE BORATE COMPLEX USING CHROMATOGRAPHY AND COMPOSITION CONTAINING D-PSICOSE

The present application relates to a method for producing D-psicose, the method comprising the steps of: putting a composition containing a D-psicose borate complex into chromatography comprising a divalent cation; and separating the composition containing the D-psicose borate complex into a fraction comprising D-psicose (i) and a fraction comprising a borate (ii).

PSICOSE EPIMERASE MUTANT AND METHOD FOR PREPARING PSICOSE BY USING SAME

The present invention relates to: a D-psicose 3-epimerase mutant from Agrobacterium tumefaciens with improved thermal stability; a recombinant vector comprising a gene encoding the mutant; and a microorganism comprising the mutant. In addition, the present invention relates to a method for producing D-psicose by using the epimerase mutant or the microorganism.

ENSIFER SP. STRAIN AND METHOD FOR PRODUCING PSICOSE USING SAME

A novel the strain isolated from soil and a method of producing psicose using the same are provided. 1Ensifer. A method of producing psicose from fructose by using sp. strain.2EnsiferEnsifer adhaerens.. The method of claim 1 , wherein the sp. strain is3EnsiferEnsifer. The method of claim 1 , wherein the sp. strain is at least one selected from the group consisting of a cell claim 1 , a cell culture claim 1 , and a cell lysate of sp. strain.4Ensifer. The method of claim 1 , wherein the method comprises a step of reacting sp. with fructose.5EnsiferEnsifer. The method of claim 4 , wherein the step of reacting sp. strain with fructose is performed by culturing sp. strain on the culture medium containing fructose.6EnsiferEnsifer. The method of claim 4 , wherein the step of reacting sp. strain with fructose comprise a step of mixing the fructose with at least one selected from the group consisting of cell claim 4 , cell culture claim 4 , and cell lysate of sp. strain.7EnsiferEnsifer. The method of claim 4 , wherein the step of reacting sp. strain with fructose comprise a step of contacting the fructose with a support immobilized with at least one selected from the group consisting of cell claim 4 , cell culture claim 4 , and cell lysate of sp. strain.8. The method of claim 4 , wherein the method further comprises a step of adding at least one metal ion selected from the group consisting of Cu claim 4 , Mn claim 4 , Ca claim 4 , Mg claim 4 , Zn claim 4 , Ni claim 4 , Co claim 4 , Fe and Al ions.9. The method of claim 1 , wherein the method is performed without using a buffer solution.10. The method of claim 1 , wherein the fructose is used at an concentration of 40 to 75% (w/w).11. The method of claim 1 , wherein the method is performed at pH of 6 to 9 and at a temperature of 40 to 80° C.12Ensifer. A composition for producing psicose from fructose claim 1 , comprising sp strain.13EnsiferEnsifer adhaerens.. The composition of claim 12 , wherein the sp. strain ...

КОМПОЗИЦИЯ ДЛЯ ПОЛУЧЕНИЯ ТАГАТОЗЫ И СПОСОБ ПОЛУЧЕНИЯ ТАГАТОЗЫ ИЗ ФРУКТОЗЫ

ФЕРМЕНТАТИВНОЕ ПОЛУЧЕНИЕ ГЕКСОЗ

НОВАЯ ПСИКОЗО-6-ФОСФАТ ФОСФАТАЗА, КОМПОЗИЦИЯ ДЛЯ ПОЛУЧЕНИЯ ПСИКОЗЫ, СОДЕРЖАЩАЯ УКАЗАННЫЙ ФЕРМЕНТ, СПОСОБ ПОЛУЧЕНИЯ ПСИКОЗЫ С ИСПОЛЬЗОВАНИЕМ УКАЗАННОГО ФЕРМЕНТА

Enzymatic production of tagatose

Disclosed herein are improved processes for making tagatose including the steps of converting F6P to T6P, catalyzed by a F6PE; and converting the T6P to tagatose, catalyzed by a T6PP, using enzymes with higher activities compared to F6PEs and T6PPs previously used in a process to produce tagatose.

Epimerase enzymes and their use

This disclosure provides epimerase enzymes useful for commercial scale production of allulose from fructose. The disclosed enzymes ("epimerase variants") are variants of ...

3-EPIMERASE

A protein comprising a polypeptide sequence having at least 70% sequence identity to SEQ ID NO:6, SEQ ID NO:2or SEQ ID NO:4. The protein hasketose 3-epimerase activity.

PSICOSE EPIMERASE MUTANT AND METHOD FOR PREPARING PSICOSE BY USING SAME

The present invention relates to: a psicose epimerase mutant derived from Agrobacterium tumefaciens with improved thermal stability; a recombinant vector comprising a gene encoding the mutant; and a microorganism comprising the mutant. In addition, the present invention relates to a method for preparing psicose by using the epimerase mutant or the microorganism.

ENZYMATIC PRODUCTION OF D-ALLULOSE

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).

ФЕРМЕНТАТИВНОЕ ПОЛУЧЕНИЕ D-АЛЛЮЛОЗЫ

Изобретение относится к биотехнологии. Предложен способ получения аллюлозы, включающий превращение фруктозо-6-фосфата (F6P) в аллюлозо-6-фосфат (A6P), катализируемое с помощью аллюлозо-6-фосфат-3-эпимеразы(A6PE); и превращение получаемого A6P в аллюлозу, катализируемое с помощью аллюлозо-6-фосфат-фосфатазы(A6PP). При этом А6РЕ содержит аминокислотную последовательность, имеющую по меньшей мере 55% идентичность последовательности SEQ ID NO: 3 или 6, и А6РР содержит аминокислотную последовательность, имеющую по меньшей мере 55% идентичность последовательности SEQ ID NO: 9. Изобретение обеспечивает эффективное получение аллюлозы. 16 з.п. ф-лы, 7 ил., 2 табл., 21 пр.

СПОСОБ ДЛЯ ПРОИЗВОДСТВА D-ПСИКОЗЫ ИЗ БОРАТНОГО КОМПЛЕКСА D-ПСИКОЗЫ С ИСПОЛЬЗОВАНИЕМ ХРОМАТОГРАФИИ И СОДЕРЖАЩАЯ D-ПСИКОЗУ КОМПОЗИЦИЯ

Изобретение относится к биотехнологии и представляет собой способ производства D–псикозы, содержащий: стадию помещения композиции, содержащей боратный комплекс D–псикозы, в хроматографическую систему, содержащую двухвалентные катионы; истадию разделения композиции, содержащей боратный комплекс D–псикозы, на содержащую D–псикозу фракцию (i) и содержащую борат фракцию (ii), где двухвалентные катионы представляют собой один или более из ионов кальция, ионов бария и ионов стронция. Изобретение позволяет получать D–псикозу с высокой степенью эффективности. 11 з.п. ф-лы, 4 ил., 3 табл., 2 пр.

3-epimerase

A protein comprising a polypeptide sequence having at least 70% sequence identity to SEQ ID NO:6, SEQ ID NO:2or SEQ ID NO:4. The protein hasketose 3-epimerase activity.

ENZYMATIC PRODUCTION OF D-ALLULOSE

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).

НОВАЯ ПСИКОЗО-6-ФОСФАТ ФОСФАТАЗА, КОМПОЗИЦИЯ ДЛЯ ПОЛУЧЕНИЯ ПСИКОЗЫ, СОДЕРЖАЩАЯ УКАЗАННЫЙ ФЕРМЕНТ, СПОСОБ ПОЛУЧЕНИЯ ПСИКОЗЫ С ИСПОЛЬЗОВАНИЕМ УКАЗАННОГО ФЕРМЕНТА

Изобретение относится к биотехнологии и представляет собой применение псикозо-6-фосфат фосфатазы для получения D-псикозы, где псикозо-6-фосфат фосфатаза содержит мотив A, представленный Xa1-Xa2-Xa3-DPLDG-Xa4или Xa1-Xa2-Xa3-DPIDG-Xa4, причем Xa1представляет W, F, V, I или A, Xa2представляет I, F, V, A или отсутствует, Xa3представляет V, I или L, а Xa4представляет T или S, и мотив B, представленный Ya1-D-Ya2-Wa1-Ya3-Wa2-Ya4-Wa3, причем Ya1представляет W, Y, T, L или V, Ya2представляет V, I, C, F или A, Wa1представляет AAG, AAS, SAG, APG, APF, AGG, APL или AGA, Ya3представляет W, I, P, M, V, Y, F, R, L, T или S, Wa2представляет LLV, LIV, LLI, LII, ILI, FIA, ALV, IIA, VLV, VIL, TIG, NFC или PIF, Ya4представляет E, R, S, T, L, K или P, а Wa3представляет EАGG, EGGG, EAKG, KAGG, AAGG, YVDG, EAGA или RLGV. Изобретение позволяет повысить выход D-псикозы. 5 н. и 11 з.п. ф-лы, 4 ил., 1 табл., 5 пр.

A protein

A protein

A protein comprising a polypeptide sequence having at least 90% sequence identity to SEQ ID NO. 6, wherein the protein has psicose 3-epimerase activity and the polypeptide sequence is not identical to SEQ ID NO. 6. A nucleic acid encoding this protein is provided as well as vectors and host cells comprising such a nucleic acid and protein. The protein may be useful in the production of allulose.

Microorganisms and methods for the co-production of ethylene glycol and three carbon compounds

The present application relates to recombinant microorganisms useful in the biosynthesis of monoethylene glycol (MEG) and one or more three-carbon compounds such as acetone, isopropanol or propene. The MEG and one or more three-carbon compounds described herein are useful as starting material for production of other compounds or as end products for industrial and household use. The application further relates to recombinant microorganisms co-expressing a C2 branch pathway and a C3 branch pathway for the production of MEG and one or more three-carbon compounds. Also provided are methods of producing MEG and one or more three-carbon compounds using the recombinant microorganisms, as well as compositions comprising the recombinant microorganisms and/or optionally the products MEG and one or more three-carbon compounds.

MICROORGANISMS AND METHODS FOR THE CO-PRODUCTION OF ETHYLENE GLYCOL AND ISOBUTENE

The present application relates to recombinant microorganisms useful in the biosynthesis of monoethylene glycol (MEG) and isobutene. The application further relates to recombinant microorganisms co-expressing a C2 branch pathway and a C3 branch pathway for the production of MEG and isobutene. Also provided are methods of producing MEG and isobutene using the recombinant microorganisms, as well as compositions comprising the recombinant microorganisms and/or optionally the products MEG and isobutene. 3. The recombinant microorganism of or , wherein the recombinant microorganism further comprises one or more modifications selected from the group consisting of:(a) a deletion, insertion, or loss of function mutation in a gene encoding a D-xylulose-5-kinase that catalyzes the conversion of D-xylulose to D-xylulose-5-phosphate;(b) a deletion, insertion, or loss of function mutation in a gene encoding a glycolaldehyde dehydrogenase that catalyzes the conversion of glycolaldehyde to glycolic acid; and(c) a deletion, insertion, or loss of function mutation in a gene encoding a lactate dehydrogenase that catalyzes the conversion of pyruvate to lactate.4. The recombinant microorganism of any one of - , wherein an endogenous or exogenous xylose isomerase catalyzes the conversion of D-xylose to D-xylulose.5. The recombinant microorganism of any one of - , wherein the recombinant microorganism further expresses at least one exogenous nucleic acid molecule encoding a xylose reductase or aldose reductase that catalyzes the conversion of D-xylose to xylitol and at least one exogenous nucleic acid molecule encoding a xylitol dehydrogenase that catalyzes the conversion of xylitol to D-xylulose.7. The recombinant microorganism of claim 6 , wherein the recombinant microorganism further comprises one or more modifications selected from the group consisting of:(a) a deletion, insertion, or loss of function mutation in a gene encoding a D-xylose isomerase that catalyzes the conversion of D ...

Enzymatic production of D-allulose

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).

Production method for tagatose

A method for producing tagatose comprises: a) performing epimerization of fructose using hexuronate C4-epimerase to obtain an epimerized product comprising tagatose; b) purifying the epimerized product; and c) crystallizing the purified epimerized product. The hexuronate C4-epimerase is an enzyme derived from Thermotoga maritima, Thermotoga neapolitana, Thermotoga thermarum or mutants thereof. The hexuronate C4-epimerase is produced from strains Escherichia coli, Corynebacterum glutamicum, Aspergillus oryzae, or Bacillus subtilis.

ENGINEERING MICROBES AND METABOLIC PATHWAYS FOR THE PRODUCTION OF ETHYLENE GLYCOL

The invention relates to recombinant cells and their use in the production of ethylene glycol.

Способ получения D-псикозы с использованием микроорганизма рода kaistia

Изобретение относится к области биотехнологии. Отражена композиция для получения D-псикозы, содержащая микроорганизмы рода Kaistia и D-фруктозу, способ получения D-псикозы с ее использованием, а также штаммы микроорганизмов рода Kaistia для получения D-псикозы. Изобретение позволяет получить моносахарид – D-псикозу из D-фруктозы с использованием различных микроорганизмов рода Kaistia. 5 н. и 2 з.п. ф-лы, 10 ил., 1 табл., 2 пр.

Method for producing d-psicose from D-psicose borate complex using chromatography and composition containing D-psicose

The present application relates to a method for producing D-psicose, the method comprising the steps of: putting a composition containing a D-psicose borate complex into chromatography comprising a divalent cation; and separating the composition containing the D-psicose borate complex into a fraction comprising D-psicose (i) and a fraction comprising a borate (ii).

3-Epimerase

METHOD OF PRODUCTION OF MONOSACCHARIDES

The present invention is directed towards genetic modification of native gene encoding for D-tagatose 3-epimerase and rhamnose isomerase to substantially increase the expression level of these enzymes and use of said enzymes in a process to produce rare monosaccharides such as psicose and allose. Also disclosed in the present invention is expression constructs comprising the modified genes and a host cells to express the same.

호열균 유래 당 에피머화효소를 포함하는, 비인산헥소오스의 에피머화용 조성물

... 본 발명은 호열균 유래 당 에피머화효소를 포함하는, 비인산헥소오스의 에피머화용 조성물 및 이 조성물을 이용한 비인산헥소오스 에피머의 제조 방법에 관한 것이다. 본 발명에 따른 호열균 유래 당 에피머화효소는 비인산헥소오스의 에피머화 반응을 효과적으로 유도하며, 비인산헥소오스의 에피머 형태, 특히 희귀헥소오스당을 용이하게 수득할 수 있는바, 제약 및 식품산업에서 유용하게 활용될 수 있다.

A protein

A protein

Enzymatic production D- psicose

VARIANT OF D-PSICOSE 3-EPIMERASE AND USES THEREOF

The present invention relates to an improved variant of a D-psicose 3-epimerase and its uses. 125-. (canceled)26. A variant of a parent D-psicose 3-epimerase , wherein the variant comprises a substitution of a Glycine residue by a Serine residue at a position corresponding to position 211 in SEQ ID NO: 2 compared to the parent D-psicose 3-epimerase , said variant comprising , D-psicose 3-epimerase activity to modify D-fructose into D-psicose with greater catalysis efficiency than parent D-psicose 3-epimerase , the parent D-psicose 3-epimerase having an amino acid sequence with at least 70% identity with a sequence selected from the group consisting of SEQ ID NO: 2 and 5-10 , and said variant has an amino acid sequence having at least 60% identity with a sequence selected from the group consisting of SEQ ID NO: 2 and 5-10.27. The variant according to claim 26 , wherein the variant has one or several of the following features: a) a lower pH optimum compared to the parent D-psicose 3-epimerase claim 26 , preferably in the range of 6 to 7; and/or b) a higher catalysis efficiency to the substrate D-fructose compared to the parent-psicose 3-epimerase; and/or c) a longer half-life at 60° C. compared to the parent-psicose 3-epimerase.28. The variant according to claim 26 , wherein the variant has an amino acid sequence having at least 70% identity with a sequence selected from the group consisting of SEQ ID NO: 2 and 5-10.29Pseudomonas cichoriiAgrobacterium tumefaciensClostridiumClostridium scindensClostridium bolteaeRuminococcusClostridium cellulolyticum.. The variant according to claim 26 , wherein the parent D-psicose 3-epimerase is selected from a D-tagatose 3-epimerase from claim 26 , a D-psicose 3-epimerase from claim 26 , a D-psicose 3-epimerase from sp. claim 26 , a D-psicose 3-epimerase from claim 26 , a D-psicose 3-epimerase from claim 26 , a D-psicose 3-epimerase from sp. claim 26 , and a D-psicose 3-epimerase from30Clostridium cellulolyticum.. The variant ...

ENZYMATIC PRODUCTION OF TAGATOSE

Disclosed herein are improved processes for making tagatose including the steps of converting F6P to T6P, catalyzed by a F6PE; and converting the T6P to tagatose, catalyzed by a T6PP, using enzymes with higher activities compared to F6PEs and T6PPs previously used in a process to produce tagatose.

KETOSE 3-EPIMERASE WITH IMPROVED THERMAL STABILITY

It is found that by substituting a specific amino acid among amino acid sequences of a ketose 3-epimerase derived from Arthrobacter globiformis, a mutant enzyme with improved thermal stability is obtained, and D-psicose can be efficiently produced.

ENZYMATIC PRODUCTION OF HEXOSES

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.

3-EPIMERASE

A protein comprising a polypeptide sequence having at least 70% sequence identity to SEQ ID NO:6, SEQ ID NO:2or SEQ ID NO:4. The protein hasketose 3-epimerase activity.

PRODUCTION METHOD FOR TAGATOSE

The present invention relates to a production method for tagatose.

Improved variant of d-psicose 3-epimerase and uses thereof

Polynucleotide encoding psicose epimerase and method of producing psicos using the same

... 사이코스 3-에피머화 효소, 상기 효소를 암호화하는 폴리뉴클레오타이드, 상기 폴리뉴클레오타이드를 포함하는 재조합 벡터, 상기 재조합 벡터를 포함하는 재조합 균주, 및 이들의 사이코스 제조에 있어서의 용도가 제공된다.

NOVEL HEAT-RESISTANT FRUCTOSE-6-PHOSPHATE-3-EPIMERASE AND METHOD FOR PRODUCING ALLULOSE BY USING SAME

D-Ketohexose-3-Epimerase, und seine Herstellung und Verwendung

A protein

3-Epimerase

A protein comprising a polypeptide sequence having at least 70% sequence identity to SEQ ID NO:6, SEQ ID NO:2or SEQ ID NO:4. The protein hasketose 3-epimerase activity.

A BACILLUS SUBTILIS STRAIN, CULTURE METHOD AND USE THEREOF

A Bacillus subtilis strain or a descendant thereof, and a culture method therefor and application thereof. The present invention further relates to a culture material and a lysate of the Bacillus subtilis strain or descendant thereof, and a method for preparation of D-psicose epimerase and preparation of D-psicose using the Bacillus subtilis strain or a descendant thereof.

KETOSE 3-EPIMERASE WITH IMPROVED THERMAL STABILITY

It is found that by substituting a specific amino acid among amino acid sequences of a ketose 3-epimerase derived from Arthrobacter globiformis, a mutant enzyme with improved thermal stability is obtained, and D-psicose can be efficiently produced.

ENGINEERING MICROBES AND METABOLIC PATHWAYS FOR THE PRODUCTION OF ETHYLENE GLYCOL

The invention relates to recombinant cells and their use in the production of ethylene glycol. The cells in some embodiments have reduced or eliminated activity or expression of aldehyde dehydrogenase A relative to a wild type cell. In-some embodiments, the aldehyde dehydrogenase A is encoded by an aldA gene, and the cell includes a deletion of the aldA gene.

Expression system for psicose epimerase and production for psicose using the same

A gene expression cassette capable of producing psicose at high yield with high stability, a GRAS (Generally recognized as safe) microorganism, a method of producing the enzyme by using the GRAS microorganism, and a method of producing the psicose by using the GRAS microorganism and enzyme are provided.

NOVEL PSICOSE-6-PHOSPHATE PHOSPHATASE, COMPOSITION FOR PRODUCING D-PSICOSE COMPRISING THE ENZYME AND METHODS FOR PRODUCING D-PSICOSE USING THE ENZYME

The present application relates to: a psicose-6phosphate phosphatase including motif A and motif B; a composition which is for producing psicose and includes said enzyme; and a method for producing psicose using said enzyme.

CELL-BASED PRODUCTION OF NONULOSONATES

The present invention relates to the cell-based production of bacterial nonulosonates and their biosynthetic precursors. Specifically, the present invention provides recombinant cells for the production of pseudaminic acid, legionaminic acid, UDP-2,4-diacetamido-2,4,6-trideoxy-ß-L-altropyranose, and UDP-2,4-diacetamido-2,4,6-trideoxy-a-D-glucopyranose. Methods for producing the sugars are also provided.

Production method of tagatose, Escherichia coli and hexulose C4 - epimerase mutant

A d-psicose 3-epimerase, methods for preparing d-psicose using the same, a polynucleotide encoding the same, a recombinant vector, a microorganism and a composition

3-epimerase

A protein comprising a polypeptide sequence having at least 70% sequence identity to SEQ ID NO:6, SEQ ID NO:2 or SEQ ID NO:4. The protein has ketose 3-epimerase activity.

Method of production of monosaccharides

The present invention is directed towards genetic modification of native gene encoding for D-tagatose 3-epimerase and rhamnose isomerase to substantially increase the expression level of these enzymes and use of said enzymes in a process to produce rare monosaccharides such as psicose and allose. Also disclosed in the present invention is expression constructs comprising the modified genes and a host cells to express the same.

D-타가투로네이트 에피머화효소를 포함하는, 비인산헥소오스의 에피머화 방법

... 본 발명은 호열균 유래 당 에피머화효소인 D-타카투로네이트 에피머라아제를 포함하는, 비인산헥소오스의 에피머화용 조성물 및 이 조성물을 이용한 비인산헥소오스 에피머의 제조 방법에 관한 것이다. 본 발명에 따른 D-타카투로네이트 에피머라아제는 비인산헥소오스의 에피머화 반응을 효과적으로 유도하며, 비인산헥소오스의 에피머 형태, 특히 희귀헥소오스당을 용이하게 수득할 수 있는바, 제약 및 식품산업에서 유용하게 활용될 수 있다.

타가토스 제조용 조성물 및 과당으로부터 타가토스를 제조하는 방법

... 본 발명은 서열번호 1 내지 서열번호 7 중 어느 하나의 아미노산 서열로 이루어진 단백질 또는 상기 단백질을 발현하는 균주를 포함하는, 과당으로부터 타가토스를 제조하기 위한, 타가토스 제조용 조성물에 관한 것이다. 또한, 본 발명은 상기 조성물을 과당과 반응시키는 단계를 포함하는, 과당으로부터 타가토스를 제조하는 방법에 관한 것이다.

D-사이코스 3-에피머라제의 개선된 변이체 및 그의 용도

... 본 발명은 D-사이코스 3-에피머라제의 개선된 변이체 및 그의 용도에 관한 것이다.

MICROORGANISMS AND METHODS FOR THE CO-PRODUCTION OF ETHYLENE GLYCOL AND ISOBUTENE

D-PSICOSE 3-EPIMERASE MUTANT WITH IMPROVED THERMAL STABILITY, AND CONTINUOUS PRODUCTION OF D-PSICOSE USING SAME

Psicose-6-phosphate phosphatase, nucleic acid encoding the enzyme,composition for producing d-psicose comprising the enzyme and methods for producing d-psicose using the enzyme

CELL IMMOBILIZED BEADS HAVING EXCELLENT CONVERSION ACTIVITY AND METHOD FOR PREPARING SAME

The present disclosure relates to cell immobilized beads and a method for preparing the same and, more specifically, to cell-immobilized beads wherein the conversion activity of cells contained in the immobilized beads is excellent and wherein the conversion activity is maintained even during distribution and storage processes, a method for preparing the cell-immobilized beads, and a use of the conversion activity of the beads.

Novel psicose-6-phosphate phosphatase, composition for producing psicose including said enzyme, method for producing psicose using said enzyme

D-프럭토스를 D-알룰로스로 생물전환시키기 위한 D-알룰로스 3-에피머라제

... 본 명세서에서는 광범위한 미생물로부터 D-알룰로스 3-에피머라제 활성을 갖는 폴리펩타이드를 코딩하는 폴리뉴클레오타이드를 식별하고 단리시키는 방법이 제공된다. 또한 D-알룰로스 3-에피머라제 활성을 코딩하는 폴리뉴클레오타이드를 포함하는 핵산 작제물, 벡터 및 재조합 숙주 세포뿐만 아니라, D-알룰로스 3-에피머라제 활성을 갖는 상기 재조합 숙주 세포 또는 D-알룰로스 3-에피머라제 활성을 갖는 상기 재조합 숙주 세포의 D-알룰로스 3-에피머라제 효소를 사용해서 프럭토스로부터 알룰로스를 생산하는 방법이 제공된다.

Engineering microbes and metabolic pathways for the production of ethylene glycol

The invention relates to recombinant cells and their use in the production of ethylene glycol.

MICROORGANISMS AND METHODS FOR THE CO-PRODUCTION OF ETHYLENE GLYCOL AND THREE CARBON COMPOUNDS

The present application relates to recombinant microorganisms useful in the biosynthesis of monoethylene glycol (MEG) and one or more three-carbon compounds such as acetone, isopropanol or propene. The MEG and one or more three-carbon compounds described herein are useful as starting material for production of other compounds or as end products for industrial and household use. The application further relates to recombinant microorganisms co-expressing a C2 branch pathway and a C3 branch pathway for the production of MEG and one or more three-carbon compounds. Also provided are methods of producing MEG and one or more three-carbon compounds using the recombinant microorganisms, as well as compositions comprising the recombinant microorganisms and/or optionally the products MEG and one or more three-carbon compounds. 2. The recombinant microorganism of claim 1 , wherein the recombinant microorganism further comprises at least one endogenous or exogenous nucleic acid molecule encoding a secondary alcohol dehydrogenase that catalyzes the conversion of acetone to isopropanol.3. The recombinant microorganism of claim 1 , wherein the recombinant microorganism further comprises: at least one endogenous or exogenous nucleic acid molecule encoding a secondary alcohol dehydrogenase that catalyzes the conversion of acetone to isopropanol; and at least one endogenous or exogenous nucleic acid molecule encoding a dehydratase that catalyzes the conversion of isopropanol to propene.4. The recombinant microorganism of claim 1 , wherein the recombinant microorganism further comprises one or more modifications selected from the group consisting of:(a) a deletion, insertion, or loss of function mutation in a gene encoding a D-xylose isomerase that catalyzes the conversion of D-xylose to D-xylulose;(b) a deletion, insertion, or loss of function mutation in a gene encoding a glycolaldehyde dehydrogenase that catalyzes the conversion of glycolaldehyde to glycolic acid; and(c) a deletion, ...

Method for producing d-psicose from D-psicose borate complex using chromatography and composition containing D-psicose

The present application relates to a method for producing D-psicose, the method comprising the steps of: putting a composition containing a D-psicose borate complex into chromatography comprising a divalent cation; and separating the composition containing the D-psicose borate complex into a fraction comprising D-psicose (i) and a fraction comprising a borate (ii).

Enzymatic production of D-allulose

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).

Enzymatic production of D-allulose

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).

A novel d-psicose 3-epimerase and method for producing d-psicose using the same

IMPROVED VARIANT OF D-PSICOSE 3-EPIMERASE AND USES THEREOF

The present invention relates to an improved variant of a D-psicose 3-epimerase and its uses. 125-. (canceled)26. A variant of a parent D-psicose 3-epimerase , wherein the variant comprises a substitution of a Glycine residue by a Serine residue at a position corresponding to position 211 in SEQ ID No 2 compared to the parent D-psicose 3-epimerase , and wherein the variant has a D-psicose 3-epimerase activity , the parent D-psicose 3-epimerase having an amino acid sequence having at least 60% identity with a sequence selected from the group consisting of SEQ ID No 2 and 5-10.27. The variant according to claim 26 , wherein the variant has one or several of the following features:a) a lower pH optimum compared to the parent D-psicose 3-epimerase, preferably in the range of 6 to 7; and/orb) a higher catalysis efficiency to the substrate D-fructose compared to the parent-psicose 3-epimerase; and/or{'claim-ref': {'@idref': 'CLM-00026', 'claim 26'}, 'c) a longer half-life at 60° C. compared to the parent-psicose 3-epimerase. 28 (new). The variant according to , wherein the variant has an amino acid sequence having at least 60% identity with a sequence selected from the group consisting of SEQ ID No 2 and 5-10.'}29Pseudomonas cichorii,Agrobacterium tumefaciens,ClostridiumClostridium scindens,Clostridium bolteae,RuminococcusClostridium cellulolyticum.. The variant according to claim 26 , wherein the parent D-psicose 3-epimerase is selected from a D-tagatose 3-epimerase from a D-psicose 3-epimerase from a D-psicose 3-epimerase from sp. claim 26 , a D-psicose 3-epimerase from a D-psicose 3-epimerase from a D-psicose 3-epimerase from sp. claim 26 , and a D-psicose 3-epimerase from30Clostridium cellulolyticum.. The variant according to claim 29 , wherein the parent D-psicose 3-epimerase is the D-psicose 3-epimerase from31. The variant according to claim 30 , wherein the variant comprises SEQ ID No 4 or an amino acid sequence having at least 90% identity with SEQ ID No 4 with a ...

D-ALLULOSE 3-EPIMERASES FOR BIOCONVERSION OF D-FRUCTOSE TO D-ALLULOSE

D-psicose 3-epimerase mutant with improved thermal stability, and continuous production of D-psicose using same

The present invention relates to a D-psicose 3-epimerase variant with improved thermostability by substituting an amino acid at a specific position of an amino acid sequence of a wild type D-psicose 3-epimerase. Further, the present invention provides a recombinant expression vector including a gene of the D-psicose 3-epimerase variant, and a recombinant strain transformed with the recombinant expression vector. Furthermore, the present invention provides an immobilized reactor prepared using the D-psicose 3-epimerase variant or the recombinant strain, and a method of continuously producing D-psicose using the immobilized reactor.

알룰로오스 함유 감미료 조성물의 제조 방법

... 본 발명의 목적은, 글루코오스에 대하여, 글루코오스 이소메라아제 및 알룰로오스 에피메라아제를 작용시켜, 글루코오스, 프룩토오스 및 알룰로오스를 포함하는 감미료 조성물을 제조하는 방법에 있어서, 그 감미료 조성물에서의 알룰로오스의 함유 비율을 높이는 기술을 제공하는 것이다. 글루코오스 이소메라아제 및 알룰로오스 에피메라아제를 고정화 해, 고정화 글루코오스 이소메라아제와 고정화 알룰로오스 에피메라아제의 활성 비율이 1.49 : 1 ~ 5.61 : 1이 되도록 칼럼에 충진해, 그 칼럼에 글루코오스 용액을 통액함으로써, 글루코오스, 프룩토오스 및 알룰로오스를 포함하고, 한편 알룰로오스의 함유 비율이 높은 감미료 조성물을 연속적이고 효율적으로 제조할 수 있다.

Allulose epimerase variant, method for preparing the same, and method for preparing allulose using the same

The present invention provides: a novel allulose epimerase variant in which an amino acid residue present at a specific position of an amino acid sequence of a wild-type D-allulose 3-epimerase derived from Flavonifractor plautii is substituted with another amino acid residue; and various uses of the novel allulose epimerase variant. The novel allulose epimerase variant according to the present invention has a higher conversion rate of fructose to allulose compared to that of the wild-type D-allulose 3-epimerase derived from Flavonifractor plautii, and has excellent thermal stability especially under high temperature conditions of 60° C. or higher, and thus can prevent contamination during an industrial-scale enzymatic conversion reaction for the mass production of allulose, shorten production time, and reduce production costs.

Composition for preparing tagatose and method for preparing tagatose from fructose

D-psicose 3-epimerase, manufacturing method thereof and manufacturing method of D-psicose using the same

본 발명은 플라보니프랙터 플라우티( Flavonifractor plautii )에서 유래하고, 과당을 사이코스로 전환시킬 수 있는 신규 사이코스 에피머화 효소를 제공한다. 본 발명에 따른 신규한 사이코스 에피머화 효소는 과당의 3번째 탄소 위치를 에피머화하여 사이코스를 생산하는 활성을 보유한 효소로서, 상대적으로 높은 온도와 중성 이하의 pH에서 과당의 사이코스로의 전환에 대한 최대 활성을 가지고, 열 안정성이 우수하고, 짧은 시간 동안에 높은 수율로 과당으로부터 사이코스의 대량 생산이 가능하다. 따라서, 본 발명에 따른 사이코스 에피머화 효소는 사이코스를 산업적으로 제조하는데에 유리하고, 이렇게 생산된 사이코스는 기능성 당 산업뿐만 아니라 이를 이용한 건강식품 소재, 의약용, 화장품용 소재 등 유용하게 사용될 것으로 기대된다.

Psicose epimerase and method of psicose using the same

Manufacturing method for tagatose

... 본 발명은 타가토스의 제조방법에 관한 것이다.

ENZYMATIC PRODUCTION OF HEXOSES

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.

ALLULOSE EPIMERASE VARIANT WITH EXCELLENT THERMAL STABILITY, PREPARATION METHOD THEREFOR, AND PREPARATION METHOD FOR ALLULOSE USING SAME

The present invention provides a novel allulose epimerase variant in which an amino acid residue present at a specific position of an amino acid sequence of wild-type D-allulose 3-epimerase derived from Flavonifractor plautii is substituted with another amino acid residue, and various uses thereof. The novel allulose epimerase variant according to the present invention has a higher conversion activity of fructose to allulose than that of the wild-type D-allulose 3-epimerase derived from Flavonifractor plautii or a D-allulose epimerase variant W29K/G216S/M234I, and has excellent thermal stability especially under high temperature conditions of 60° C. or higher, thereby preventing contamination during an industrial-scale enzymatic conversion reaction for the mass production of allulose, shortening the production time, and reducing the production costs.

D-PSICOSE 3-EPIMERASE MUTANT WITH IMPROVED THERMAL STABILITY, AND CONTINUOUS PRODUCTION OF D-PSICOSE USING SAME

The present invention relates to a D-psicose 3-epimerase mutant of which the thermal stability is improved by substituting an amino acid of a specific sequence number. In addition, the present invention relates to a recombinant vector comprising the gene of the D-psicose 3-epimerase mutant, and a recombinant strain transformed with the recombinant vector. Further, the present invention relates to an immobilized reactor prepared using the enzyme mutant or the recombinant vector, and a method for producing D-psicose using the immobilized reactor.

프럭토오스 6-포스페이트 4-에피머화 효소 및 이의 용도

... 본 발명은 산업적으로 유용한 범위의 pH, 온도에서 활성을 가지며, 전분 또는 말토덱스트린등의 경제적 원료를 사용하여 높은 수율의 케토헥소스를 생산할 수 있는 프럭토오스 6-포스페이트 4-에피머화 효소, 케토헥소스 생산용 조성물, 및 이를 이용한 케토헥소스의 제조방법에 관한 것이다.

PSICOSE EPIMERASE AND MANUFACTURING METHOD OF PSICOSE USING SAME

Provided are a psicose 3-epimerase, a polynucleotide encoding the enzyme, a strain producing the enzymes, and a use thereof in producing psicose. One example of the present invention provides a psicose epimerase protein of a Microbacterium sp. strain. The enzyme protein may be a protein having activities of converting fructose into psicose. COPYRIGHT KIPO 2019 (AA) Time (min) ...

COMPOSITIONS AND METHODS FOR INCREASED ETHANOL PRODUCTION FROM BIOMASS

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 ...

METHODS FOR SYNTHESIZING ANTICOAGULANT POLYSACCHARIDES

The present invention includes methods for preparing anticoagulant polysaccharides using several non-naturally occurring, engineered sulfotransferase enzymes that are designed to react with aryl sulfate compounds instead of the natural substrate, PAPS, to facilitate sulfo group transfer to polysaccharide sulfo group acceptors. Suitable aryl sulfate compounds include, but are not limited to, p-nitrophenyl sulfate or 4-nitrocatechol sulfate. Anticoagulant polysaccharides produced by methods of the present invention comprise N-, 3-O-, 6-O-sulfated glucosamine residues and 2-O sulfated hexuronic acid residues, have comparable anticoagulant activity compared to commercially-available anticoagulant polysaccharides, and can be utilized to form truncated anticoagulant polysaccharides having a reduced molecular weight. 1. A method of enzymatically synthesizing an N- , 2-O , 3-O , 6-O sulfated , heparan sulfate (N ,2 ,3 ,6-HS) product in the absence of 3′-phosphoadenosine 5′-phosphosulfate (PAPS) , the method comprising the following steps:a. providing a starting polysaccharide mixture comprising N-sulfated heparosan;b. combining the starting polysaccharide mixture with a first sulfotransferase reaction mixture comprising a hexuronyl 2-O sulfotransferase enzyme (2OST) and a sulfo group donor, the sulfo group donor consisting of an aryl sulfate compound, to form a first product mixture, the first product mixture comprising an N-, 2-O sulfated heparan sulfate (N,2-HS) product;c. combining the first product mixture with a second sulfotransferase reaction mixture comprising a glucosaminyl 6-O sulfotransferase enzyme (6OST) and a sulfo group donor, the sulfo group donor consisting of an aryl sulfate compound, to form a second product mixture, the second product mixture comprising an N-, 2-O, 6-O sulfated heparan sulfate (N,2,6-HS) product;d. combining the second product mixture with a third sulfotransferase reaction mixture comprising a glucosaminyl 3-O sulfotransferase enzyme ( ...

SURFACE EXPRESSION VECTOR FOR CONSTITUTIVE HIGH-EXPRESSION USING PROMOTER OF GALACTOSE MUTAROTASE GENE DERIVED FROM LACTOBACILLUS CASEI, AND USE THEREOF

Provided is a galactose mutarotase gene promoter derived from and the use thereof, and more particularly, to a -derived galactose mutarotase gene promoter having the nucleotide sequence of SEQ ID NO: 1, an expression vector containing the promoter, and a microorganism transformed with the expression vector. A microorganism transformed with an expression vector containing the promoter may effectively express a target protein on the cell surface, and thus is useful as a vaccine vehicle or the like. Moreover, provided is a surface expression vector having pgsA, which is a gene encoding poly-gamma-glutamate synthetase, and a method of expressing a target protein on the microbial surface using the vector. The vector containing foreign genes inserted therein is transformed into a microorganism and allows a foreign protein is to be stably expressed on the surface of the microorganism. 1Lactobacillus casei.. A promoter of galactose mutarotase gene derived from2. The promoter of claim 1 , having the nucleotide sequence of SEQ ID NO: 1.3. An expression vector comprising: the promoter of ; and a gene encoding a target protein.4. A microorganism transformed with the expression vector of .5. A microbial surface expression vector in which the promoter of claim 1 , a gene encoding a poly-gamma-glutamate synthetase complex claim 1 , and a gene encoding a target protein are linked to one another.6. The microbial surface expression vector of claim 5 , wherein the target protein is an antigen.7. The microbial surface expression vector of claim 5 , wherein the poly-gamma-glutamate synthetase complex gene is any one or more of pgsA claim 5 , pgsB and pgsC.8. A microorganism transformed with the microbial surface expression vector of .9. The microorganism of claim 8 , which is lactic acid bacteria.10. The microbial surface expression vector of claim 5 , wherein the gene encoding the poly-gamma-glutamate synthetase complex is pgsA and has the nucleotide sequence of any one of SEQ ID NOs: ...

NON-CO2 EVOLVING METABOLIC PATHWAY FOR CHEMICAL PRODUCTION

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 ...

L-ARABINOSE ASSIMILATION PATHWAY AND USES THEREOF

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 ...

Strain ptoducing allose from fructose and method for producing allose using same

The present invention relates to a recombinant strain for producing an allose from a fructose, a composition for producing an allose which produces an allose from a fructose-containing raw material comprising the strain, and a method for preparing an allose using the same.

HEXURONATE C4-EPIMERASE VARIANT HAVING IMPROVED D-TAGATOSE CONVERSION ACTIVITY, AND D-TAGATOSE PRODUCTION METHOD USING SAME

Provided are a hexuronate C4-epimerase variant with improved activity in converting D-fructose by D-tagatose of hexuronate C4-epimerase and a method for production of D-tagatose using them. 1. A hexuronate C4-epimerase variant in which one or more amino acid residue selected from the group consisting of leucine (L) as an amino acid residue at position 77 , serine (S) residue at position 125 , alanine (A) residue at position 158 , and proline (P) residue at position 351 , from the N-terminus of a hexuronate C4-epimerase consisting of the amino acid sequence set forth in SEQ ID NO: 1 are mutated.2. The hexuronate C4-epimerase variant according to claim 1 , wherein the leucine (L) residue at position 77 is replaced by proline (P) or arginine (R).3. The hexuronate C4-epimerase variant according to claim 1 , wherein the alanine (A) residue at position 158 is replaced by threonine (T).4. The hexuronate C4-epimerase variant according to claim 1 , wherein the serine (S) residue at position 125 is replaced by aspartic acid (D) claim 1 , glutamine (Q) claim 1 , glutamic acid (E) claim 1 , threonine (T) claim 1 , asparagine (N) claim 1 , cysteine (C) claim 1 , or tyrosine (Y).5. The hexuronate C4-epimerase variant according to claim 1 , wherein the proline (P) residue at position 351 is replaced by serine (S).6. The hexuronate C4-epimerase variant according to claim 1 , wherein one or more amino acid residue selected from the group consisting of glutamine (Q) residue at position 149 claim 1 , lysine (K) residue at position 164 claim 1 , aspartic acid (D) residue at position 168 claim 1 , glutamic acid (E) residue at position 175 claim 1 , and valine (V) residue at position 267 claim 1 , from the N-terminus of the hexuronate C4-epimerase are further mutated.7. The hexuronate C4-epimerase variant according to claim 1 , wherein in case the leucine (L) residue at position 77 is replaced by proline (P) or arginine (R) claim 1 , one or more amino acid residue selected from the group ...

NOVEL PSICOSE-6-PHOSPHATE PHOSPHATASE, COMPOSITION FOR PRODUCING PSICOSE COMPRISING THE SAME, AND METHOD FOR PRODUCING PSICOSE USING THE SAME

The present application relates to a psicose-6-phosphate phosphatase, a microorganism comprising the same, and a method for producing psicose using the same. 118-. (canceled)19Alicyclobacillus, Amycolatopsis, Anaerolinea, Archaeoglobus, Bacillus, Caldicellulosiruptor, Caldilinea, Caldithrix, Carboxydocella, Carboxydothermus, Chloroflexi, Defluviitoga, Deinococcus, Desulfurococcus, Dictyoglomus, Effusibacillus, Fervidobacterium, Geobacillus, Halococcus, Hydrogenivirga, Hydrogenobacter, Hyperthermus, Kosmotoga, Marinitoga, Meiothermus, Mesotoga, Metallosphaera, Methanocella, Methanococcoides, Methanohalobium, Methanolobus, Methanosarcina, Methanothermus, Petrotoga, Picrophilus, Pseudonocardia, Pyrococcus, Pyrodictium, Rhodothermus, Slackia, Staphylothermus, Sulfolobus, Thermanaerothrix, Thermoanaerobacter, Thermoanaerobacterium, Thermobifida, Thermococcus, Thermocrinis, Thermoflexus, Thermotoga, ThermusTruepera.. A method for producing psicose , comprising converting psicose-6-phosphate into psicose by bringing psicose-6-phosphate into contact with a psicose-6-phosphate phosphatase , a microorganism expressing the same , or a culture of the microorganism , wherein the psicose-6-phosphate phosphatase is derived from any one selected from the group consisting of the genus , and20. The method of claim 19 , wherein the method further comprises converting fructose-6-phosphate into psicose-6-phosphate by bringing fructose-6-phosphate into contact with fructose-6-phosphate-3-epimerase claim 19 , a microorganism expressing the same claim 19 , or a culture of the microorganism claim 19 , prior to the converting psicose-6-phosphate into psicose.21. The method of claim 20 , wherein the method further comprises converting glucose-6-phosphate into fructose-6-phosphate by bringing glucose-6-phosphate into contact with glucose-6-phosphate-isomerase claim 20 , a microorganism expressing the same claim 20 , or a culture of the microorganism claim 20 , prior to the converting fructose- ...

RECOMBINANT YEAST AND METHOD FOR PRODUCING ETHANOL USING SAME

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 ...

A NOVEL D-PSICOSE 3-EPIMERASE AND METHOD FOR PREPARING D-PSICOSE USING THE SAME

Provided are a novel D-psicose 3-epimerase and a method for preparing psicose using the same. 1. A D-psicose 3-epimerase consisting of amino acid sequence of SEQ ID NO: 1.2. The D-psicose 3-epimerase of claim 1 , wherein the D-psicose 3-epimerase is encoded by a polynucleotide sequence of SEQ ID NO: 2.3. A polynucleotide encoding the D-psicose 3-epimerase of .4. A recombinant vector comprising the polynucleotide of .5. A microorganism into which the recombinant vector of is introduced.6. A composition for preparing D-psicose comprising:{'claim-ref': {'@idref': 'CLM-00001', 'claim 1'}, 'the D-psicose 3-epimerase of , a microorganism expressing the D-psicose 3-epimerase, or a culture of the microorganism.'}7. The composition of claim 6 , further comprising:D-fructose.8. A method for preparing D-psicose claim 6 , comprising:{'claim-ref': {'@idref': 'CLM-00001', 'claim 1'}, 'contacting the D-psicose 3-epimerase of , a microorganism expressing the D-psicose 3-epimerase, or a culture of the microorganism with D-fructose.'}9. The method of claim 8 , wherein the contacting is performed at pH of 5.0 to 9.0 claim 8 , at a temperature of 40° C. to 90° C. claim 8 , or for 0.5 to 48 hours.10. The method of claim 8 , further comprising: before claim 8 , after or simultaneously with the contacting of the D-fructose claim 8 , contacting the D-psicose 3-epimerase of claim 8 , the microorganism expressing the D-psicose 3-epimerase claim 8 , or the culture of the microorganism with a metal. The following disclosure relates to a D-psicose 3-epimerase and a method for preparing D-psicose using the same.D-psicose (hereinafter referred to as “psicose”) is a monosaccharide known as a rare sugar present in a very small amount in the natural world. It has almost zero calorie while having nearly 70% sweetness of sugar and has received a lot of attention as a new food ingredient due to its functionalities such as inhibition of blood glucose, and inhibition of lipid synthesis, etc.Due to these ...

Biosynthetic production of udp-rhamnose

The present disclosure relates to the biosynthesis of UDP-Rhamnose and recombinant polypeptides having enzymatic activity useful in the relevant biosynthetic pathways for producing UDP-Rhamnose. The present invention also provides a method for preparing a steviol glycoside composition comprising at least one rhamnose-containing steviol glycoside.

METHOD FOR MANUFACTURING ALLULOSE-CONTAINING SWEETENER COMPOSITION

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 ...

ENZYMATIC PRODUCTION OF D-ALLULOSE

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 ...

Method for producing psicose by using psicose epimerase producing microorganism

The present invention relates to a method for culturing a strain having high psicose conversion activity and a method for producing psicose comprising thereof, and by confirming the batch, fed-batch culture optimization by establishing the optimal C/N ratio and the metal ion requirement, it is possible to maintain the high psicose conversion activity and mass-produce psicose efficiently.

RECOMBINANT MICROORGANISM HAVING INCREASED ABILITY TO PRODUCE HYDROPHOBIC MATERIAL AND CELL-MEMBRANE ENGINEERING METHOD FOR PREPARATION THEREOF

Disclosed are a recombinant microorganism for producing a hydrophobic material, which is subjected to cell-membrane engineering in order to be imparted with at least one characteristic among an increase in a cell-membrane area, an increase in formation and secretion of an outer membrane vesicle, and an increase in formation of an inner membrane vesicle, and a cell-membrane engineering method for preparation thereof, whereby an insoluble hydrophobic material can be produced with high efficiency, the recombinant microorganism for high-efficiency production of carotenoids or violacein analogues is useful for producing natural pigments, antioxidants, antibiotics, cosmetic additives, anticancer agents, food additives, or nutritional supplements, and the natural pigment production technology developed herein achieves a great increase in production ability. Therefore, the present invention is effective at preparing a recombinant strain for efficient production of a variety of industrially and medically useful metabolites and at establishing an efficient preparation method.

RECOMBINANT YEAST STRAINS

This invention relates to genetically engineered strains of yeast and methods for producing recombinant protein (e.g., collagen). Recombinant protein of the present invention is used to produce biofabricated leather or a material having leather-like properties containing recombinant or engineered collagen. The yeast strains are engineered to produce ascorbate and/or increased production of α ketoglutarate. 1. A recombinant yeast cell , comprising at least one polynucleotide encoding one or more polypeptides that enable an ascorbate synthesis pathway to function such that the recombinant yeast cell produces ascorbate.2. The recombinant yeast cell of claim 1 , wherein the at least one polynucleotide is heterologous to the yeast cell.3. The recombinant yeast cell of claim 1 , wherein the at least one polynucleotide encodes for GDP-L-Gal phosphorylase claim 1 , Inositol-phosphate phosphatase claim 1 , and for GDP-Mannose-3 claim 1 ,5-epimerase.4. The recombinant yeast cell of claim 1 , wherein the at least one polynucleotide encodes L-gulono-1 claim 1 ,4-lactone oxidase claim 1 , glucurono lactone reductase claim 1 , aldonolactonase claim 1 , D-glucuronate reductase claim 1 , uranolactonase claim 1 , D-glucurono kinase claim 1 , glucuronate-1-phosphate uridylyltransferase claim 1 , UDP-D-glucose dehydrogenase claim 1 , UTP-glucose-1-phosphate uridylyltransferase claim 1 , phosphoglucomutase claim 1 , and/or hexokinase.5. The recombinant yeast cell of claim 3 , wherein the GDP-L-Gal phosphorylase claim 3 , Inositol-phosphate phosphatase claim 3 , and GDP-Mannose-3 claim 3 ,5-epimerase are each encoded by individual polynucleotides or a single polynucleotide molecule.6. The recombinant yeast cell of claim 4 , wherein the at least one polynuceleotide encodes L-gulono-1 claim 4 ,4-lactone oxidase claim 4 , glucurono lactone reductase claim 4 , aldonolactonase claim 4 , D-glucuronate reductase claim 4 , uronolactonase claim 4 , D-glucurono kinase claim 4 , glucuronate-1- ...

Methods and Compositions Related to Improved Nitrogen Utilization Efficiency in Tobacco

The present disclosure provides metabolic signatures and genetic markers for tracking enhanced nitrogen utilization efficiency phenotypes in tobacco plants and for introgressing enhanced nitrogen utilization efficiency phenotypes into tobacco plants. The disclosure also provides tobacco plants comprising enhanced nitrogen utilization efficiency and methods to the creation of tobacco plants comprising enhanced nitrogen utilization efficiency. The disclosure also provides recombinant polynucleotides and polypeptides for enhancing nitrogen utilization efficiency in modified tobacco plants and tobacco plants comprising the provided recombinant polynucleotides and polypeptides. 1. A method of producing a tobacco plant comprising an enhanced nitrogen utilization efficiency (NUE) trait comprising:a. providing a first population of tobacco plants comprising an enhanced NUE trait;b. genotyping said first population of tobacco plants for the presence of one or more molecular markers located within 20 cM of a SNP marker selected from the group consisting of SEQ ID NOs:57, 58, 59, 60, 61, 62, 63, and 64;c. selecting a tobacco plant comprising said one or more molecular markers;d. crossing said tobacco plant selected in step (c) with a second tobacco plant; ande. obtaining progeny seed from the cross of step (d) wherein a plant grown from said progeny seed comprises said enhanced NUE trait.2. The method of claim 1 , wherein said enhanced NUE trait is selected from the group consisting of an increased partial factor productivity (PFP) claim 1 , an increased agronomic efficiency (AE) claim 1 , an increased recovery efficiency (RE) claim 1 , an increased physiological efficiency (PE) claim 1 , and an increased internal efficiency (IE) claim 1 , when compared to a tobacco plant lacking said enhanced NUE trait when grown in the same conditions.3. The method of claim 1 , wherein said first population of tobacco plants is selected from the group consisting of MD609 claim 1 , MD601 ...

Mutant Yarrowia Strain Capable of Degrading Galactose

The invention relates to a method for obtaining a mutant yeast strain capable of growing on D-galactose as sole carbon source, comprising over expressing in said strain a galactokinase, a galactose-1-phosphate uridyl transferase, an UDP-glucose-4 epimerase and a galactose mutarotase. The invention also relates to a mutant strain obtained by said method. 1Yarrowia. A method for obtaining a strain capable of growing on D-galactose as sole carbon source , wherein said method comprises overexpressing in said strain a galactokinase (E.C 2.7.1.6) having at least 75% identity with the polypeptide of sequence SEQ ID NO: 2 , a galactose-1-phosphate uridyl transferase (E.C 2.7.7.12) having at least 65% identity with the polypeptide of sequence SEQ ID NO: 4 , an UDP-glucose-4 epimerase (E.C5.1.3.2) having at least 85% identity with the polypeptide of sequence SEQ ID NO: 6 and a galactose mutarotase (E.C5.1.3.3) having at least 45% identity with the polypeptide of sequence SEQ ID NO: 8.2Yarrowia. The method according to claim 1 , wherein 1 claim 1 , 2 claim 1 , 3 or 4 of said enzymes galactokinase claim 1 , galactose-1-phosphate uridyl transferase claim 1 , UDP-glucose-4 epimerase and galactose mutarotase claim 1 , are from a strain.3. The method according to claim 1 , wherein said galactokinase has the consensus amino acid sequence SEQ ID NO: 9.4. The method according to claim 1 , wherein said galactokinase is selected from the group consisting of SEQ ID NO: 2 claim 1 , 10 claim 1 , 11 claim 1 , 12 and 13.5. The method according to claim 1 , wherein said galactose-1-phosphate uridyl transferase has the consensus amino acid sequence SEQ ID NO: 14.6. The method according to claim 1 , wherein said galactose-1-phosphate uridyl transferase is selected from the group consisting of SEQ ID NO: 4 claim 1 , 15 claim 1 , 16 claim 1 , 17 and 18.7. The method according to claim 1 , wherein said UDP-glucose-4 epimerase has the consensus amino acid sequence SEQ ID NO: 19.8. The method ...

Psicose Epimerase and Psicose Production Method Using Same

The present invention provides a novel psicose epimerase derived from Flavonifractor plautii and capable of converting fructose to psicose. The novel psicose epimerase according to the present invention possesses an activity producing psicose by epimerizing the carbon-3 position of fructose, and has maximal activity for the conversion of fructose to psicose at a relatively high temperature and a pH less than or equal to neutral, has excellent thermal stability, and can mass-produce psicose from fructose in a high yield for a short amount of time. Therefore, the psicose epimerase according to the present invention is advantageous in the industrial production of psicose, and it is expected that the psicose produced thereby can be usefully utilized in the functional sugar industry and also as materials for health food, medicine, cosmetics, and the like using the psicose.

Recombinant yeast and method for producing ethanol using the same

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.

HEPAROSAN-GLUCURONIC ACID-5-EPIMERASE, AND METHOD FOR PRODUCING POLYSACCHARIDE USING SAME

To provide a polypeptide having heparosan-glucuronate 5-epimerase activity, whereby means for producing a polysaccharide in which hexuronic acid residues has been epimerized is provided. Through screening of cDNA library, a DNA encoding a polypeptide of heparosan-glucuronate 5-epimerase is obtained. The epimerase acts on glucuronic acid residues of N-acetyl heparosan and/or iduronic acid residues of completely desulfated N-acetylated heparin. The polypeptide encoded by the DNA is expressed by insect cells, to thereby yield the polypeptide having heparosan-glucuronate 5-epimerase activity. By bringing the polypeptide into contact with N-acetyl heparosan or completely desulfated N-acetylated heparin, a polysaccharide in which hexuronic acid residues has been epimerized is yielded. 1. (canceled)2. A polypeptide selected from the group consisting of the following (A) to (E): [{'i': 'Achatina fulica,', '(a1) the enzyme being derived from'}, '(a2) the enzyme having activity of epimerizing glucuronic acid residues of N-acetyl heparosan to iduronic acid residues and/or activity of epimerizing iduronic acid residues of completely desulfated N-acetylated heparin to glucuronic acid residues, and', '(a3) the enzyme having substantially no activity of epimerizing glucuronic acid residues of N-sulfated heparosan to iduronic acid residues and/or substantially no activity of epimerizing iduronic acid residues of completely desulfated N-resulfated heparin to glucuronic acid residues;, '(A) a polypeptide, wherein the polypeptide is an enzyme having the following characteristics (a1) to (a3) (b1) the amino acid sequence defined by amino acid NOs: 1 to 601 in SEQ ID NO: 2, and', '(b2) the amino acid sequence defined by amino acid NOs: 34 to 601 in SEQ ID NO: 2;, '(B) a polypeptide comprising the amino acid sequence (b1) or (b2)(C) a polypeptide comprising the amino acid sequence equivalent to that of the polypeptide (B), except that one or a small number of amino acid residues are ...

Microbial production of renewable glycolate

Some aspects provide engineered microbes for glycolate production. Methods for microbe engineering and culturing are also provided herein. Such engineered microbes exhibit greatly enhanced capabilities for glycolate production.

ACETATE TOXICITY TOLERANCE IN RECOMBINANT MICROBIAL HOST CELLS

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 ...

RHAMNOSE SYNTHASE DERIVED FROM STEVIA AND GENE

The purpose of the present invention is to provide a protein, said protein having an activity of synthesizing rhamnose from glucose, and a polynucleotide encoding the same. Provided are a rhamnose synthase derived from stevia and a method for producing rhamnose from glucose using a gene. Also provided is a method for producing a steviol glycoside using the rhamnose synthase derived from stevia. 1. A protein according to any one selected from the group consisting of the following (a) to (c):(a) a protein consisting of the amino acid sequence of SEQ ID NO: 2, 4, 6, 8 or 10;(b) a protein consisting of an amino acid sequence wherein 1 to 33 amino acids are deleted, substituted, inserted, and/or added in the amino acid sequence of SEQ ID NO: 2, 4, 6, 8 or 10 and having an activity to produce rhamnose from glucose;(c) a protein having an amino acid sequence having a sequence identity of 95% or more to the amino acid sequence of SEQ ID NO: 2, 4, 6, 8 or 10 and having an activity to produce rhamnose from glucose.2. The protein according to claim 1 , wherein the glucose is in the form of uridine diphosphate glucose.3. The protein according to or claim 1 , wherein the rhamnose is in the form of uridine diphosphate rhamnose.4. A polynucleotide selected from the group consisting of the following (a) to (d):(a) a polynucleotide comprising the nucleotide sequence of SEQ ID NO: 1, 3, 5, 7 or 9;(b) a polynucleotide encoding a protein consisting of the amino acid sequences of SEQ ID NO: 2, 4, 6, 8 or 10;(c) a polynucleotide encoding a protein consisting of an amino acid sequence wherein 1 to 33 amino acids are deleted, substituted, inserted, and/or added in the amino acid sequence of SEQ ID NO: 2, 4, 6, 8 or 10 and having an activity to produce rhamnose from glucose;(d) a polynucleotide encoding a protein having an amino acid sequence having a sequence identity of 95% or more to the amino acid sequence of SEQ ID NO: 2, 4, 6, 8 or 10 and having an activity to produce rhamnose from ...

Expression system for psicose epimerase and production for psicose using the same

A gene expression cassette capable of producing psicose at high yield with high stability, a GRAS (Generally recognized as safe) microorganism, a method of producing the enzyme by using the GRAS microorganism, and a method of producing the psicose by using the GRAS microorganism and enzyme are provided. 1Corynebacterium. A gene expression cassette , producing a psicose epimerase in sp. , and comprising:{'i': 'Corynebacterium', 'a nucleotide sequence encoding the psicose epimerase; and a regulating sequence being operably connected to the nucleotide sequence in the upstream and regulating the expression of the nucleotide sequence in sp, wherein the regulating sequence comprising a promoter including a nucleotide sequence of SEQ ID NO: 1.'}2. The gene expression cassette according to claim 1 , wherein the regulating sequence comprises further at least a sequence selected from the group consisting of a ribosome binding site (RBS) sequence claim 1 , spacer sequence and linker sequence.3. The gene expression cassette according to claim 2 , wherein the ribosome binding site sequence is a nucleotide sequence in a size of 7 to 20 bp which including a nucleotide sequence of SEQ ID NO: 2.4. The gene expression cassette according to claim 2 , wherein the regulating sequence comprises at least one to five copy of RBS sequence.5. The gene expression cassette according to claim 2 , wherein the linker sequence is a nucleotide sequence in a size of 5 to 100 bp.6. The gene expression cassette according to claim 2 , wherein the spacer sequence include a first spacer sequence selected from the group of the nucleotide sequences of SEQ ID NO: 3 to SEQ ID NO: 6.7. The gene expression cassette according to claim 2 , wherein the spacer sequence include a second spacer sequence selected from the group of the nucleotide sequences of SEQ ID NO: 7 to SEQ ID NO: 11.8. The gene expression cassette according to claim 2 , wherein the regulating sequence comprises the promoter claim 2 , a first ...

PRODUCTION METHOD FOR TAGATOSE

A method for producing tagatose comprises: a) performing epimerization of fructose using hexuronate C4-epimerase to obtain an epimerized product comprising tagatose; b) purifying the epimerized product; and c) crystallizing the purified epimerized product. The hexuronate C4-epimerase is an enzyme derived from or mutants thereof. The hexuronate C4-epimerase is produced from strains , or 1. A method for producing tagatose , comprising:a) performing epimerization of fructose using hexuronate C4-epimerase to obtain an epimerized product comprising tagatose; andb) purifying the epimerized product.2Thermotoga maritima, Thermotoga neapolitana, Thermotoga thermarum. The method for producing tagatose according to claim 1 , wherein the hexuronate C4-epimerase is an enzyme derived from or mutants thereof.3Escherichia. coli, Corynebacterum glutamicum, Aspergillus oryzaeBacillus subtilis.. The method for producing tagatose according to claim 1 , wherein the hexuronate C4-epimerase is produced from strains claim 1 , or4E. coliE. coliE. coli. The method for producing tagatose according to claim 3 , wherein the hexuronate C4-epimerase production strain is BL21(DE3) pET21a-TM (accession number: KCCM11542P) claim 3 , BL21(DE3) pET21a-TN (accession number: KCCM11543P) claim 3 , or BL21(DE3) pET28a-TN(m) (accession number: KCCM11544P).5. The method for producing tagatose according to claim 1 , wherein the epimerization step comprises reacting fructose and hexuronate C4-epimerase at a temperature ranging from 60° C. to 90° C. and pH 5 to 8.6. The method for producing tagatose according to claim 5 , wherein the epimerization step is performed in the presence of a metal salt.7. The method for producing tagatose according to claim 6 , wherein the metal salt comprises at least one of NiSO claim 6 , NiCl claim 6 , CoCl claim 6 , MnCl claim 6 , and ZnSO.8. The method for producing tagatose according to claim 1 , wherein the epimerized product comprises tagatose in an amount of 0.05 wt % or ...

3-EPIMERASE AND POLYNUCLEOTIDE ENCODING SAME

Provided are a 3-epimerase, an encoding polynucleotide therefor, a nucleic acid construct, vector, and host cell comprising the polynucleotide, a method for producing the 3-epimerase, and use of the 3-epimerase. 1. A composition comprising a 3-epimerase , comprising a polypeptide or protein selected-from a group consisting of:(a) having an amino acid sequence which is at least 70% identical to a sequence as shown in SEQ ID No: 2; (i) a sequence encoding a polypeptide as shown in SEQ ID No: 1,', '(ii) a genomic DNA sequence comprising the sequence encoding a polypeptide as shown in SEQ ID No: 1, or', '(iii) a full-length complement strand of (i) or (ii);, '(b) encoded by a polynucleotide hybridized to'}(c) encoded by a polynucleotide having a sequence at least 70% identical to the sequence encoding a polypeptide as shown in SEQ ID No: 1;(d) a variant of the polypeptide or protein as shown in SEQ ID No: 2, comprising one or more amino acid substitutions, deletions and/or insertions;(e) any polypeptide or protein of (a), (b) or (c), having an amino acid sequence comprising or consisting of the sequence as shown in SEQ ID No: 2; and(f) a fragment of the polypeptide or protein of (a), (b), (c), (d), or (e), having the 3-epimerase activity.22. The composition of is an isolated polypeptide or protein according to , having a sequence which is at least 70% polypeptide or protein as shown in SEQ ID No: .3. The composition of is an isolated polypeptide or protein according to , having an amino acid sequence comprising or consisting of the sequence as shown in SEQ ID No: 2.4. The composition of is an isolated polynucleotide , encoding a polypeptide or protein according to .5. The composition of claim 4 , wherein the isolated polynucleotide is part of a nucleic acid construct or expression vector claim 4 , and the polynucleotide is operatively linked to one or more (several) regulatory sequences that direct the production of the polypeptide or protein in an expression vector.6. ...

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

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 , ...

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

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 ...

Cell-Based Production of Nonulosonates

The present invention relates to the cell-based production of bacterial nonulosonates and their biosynthetic precursors. Specifically, the present invention provides recombinant cells for the production of pseudaminic acid, legionaminic acid, UDP-2,4-diacetamido-2,4,6-trideoxy-β-L-altropyranose, and UDP-2,4-diacetamido-2,4,6-trideoxy-α-D-glucopyranose. Methods for producing the sugars are also provided.

PSICOSE EPIMERASE MUTANT AND METHOD FOR PREPARING PSICOSE BY USING SAME

The present invention relates to: a D-psicose 3-epimerase mutant from with improved thermal stability; a recombinant vector comprising a gene encoding the mutant; and a microorganism comprising the mutant. In addition, the present invention relates to a method for producing D-psicose by using the epimerase mutant or the microorganism. 1Agrobacterium tumefaciens. A D-psicose 3-epimerase mutant comprising an amino acid sequence in which glutamic acid at position 77 of the amino acid sequence of a wild type D-psicose 3-epimerase from is substituted with proline.2. The D-psicose 3-epimerase mutant according to claim 1 , wherein isoleucine at position 33 of the amino acid sequence is substituted with an amino acid selected from the group consisting of leucine claim 1 , cysteine and valine claim 1 , or serine at position 213 of the amino acid sequence is substituted with cysteine.3. The D-psicose 3-epimerase mutant according to claim 1 , wherein isoleucine at position 33 of the amino acid sequence is substituted with leucine claim 1 , and serine at position 213 of the amino acid sequence is substituted with cysteine.4. A polynucleotide encoding the D-psicose 3-epimerase mutant of .5. A recombinant vector comprising the gene encoding D-psicose 3-epimerase mutant of .6. A recombinant microorganism transformed to produce the D-psicose 3-epimerase mutant of .7Corynebacterium glutamicum.. The recombinant microorganism according to claim 6 , wherein the microorganism is8. A method for producing D-psicose claim 6 , comprising:{'claim-ref': [{'@idref': 'CLM-00001', 'claim 1'}, {'@idref': 'CLM-00006', 'claim 6'}], 'providing D-fructose with the D-psicose 3-epimerase mutant of or a recombinant microorganism of thereby causing an enzyme reaction; and'}recovering D-psicose after purifying the enzyme reaction product.9. The method according to claim 8 , wherein a metal ion is further added in the enzyme reaction.10. The method according to claim 9 , wherein the metal is manganese.11. ...

CELLS WITH IMPROVED PENTOSE CONVERSION

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 ...

New tagatose-6-phosphate 4-epimerase and application thereof

Disclosed is a new tagatose 6-phosphate 4-epimerase, which is capable of converting fructose 6-phosphate into tagatose 6-phosphate and vice versa. Also disclosed is an application of the enzyme in tagatose production.

IMPROVED OLIGOSACCHARIDE PRODUCTION IN YEAST

Provided herein are genetically modified yeast cells capable of producing one or more human milk oligosaccharides (HMOs) and methods of making such cells. The yeast cells are engineered to comprise a heterologous nucleic acid encoding a transporter protein and one or more heterologous nucleic acids that encode enzymes of a HMO biosynthetic pathway. Also provided are fermentation compositions including the disclosed genetically modified yeast cells, and related methods of producing and recovering HMOs generated by the yeast cells. 1. A yeast cell genetically modified to produce one or more human milk oligosaccharides , wherein the yeast cell comprises (i) a heterologous nucleic acid encoding a human milk oligosaccharide (HMO) ABC transporter polypeptide; and (ii) one or more heterologous nucleic acids that each independently encode at least one enzyme of a human milk oligosaccharide biosynthetic pathway.2. The yeast cell of claim 1 , wherein the ABC transporter exports the human milk oligosaccharide 2′-fucosyllactose.3. The yeast cell of or claim 1 , wherein the ABC transporter has at least 95% identity to any one of SEQ ID NOS: 1-27.4. The yeast cell of claim 3 , wherein the ABC transporter comprises the amino acid sequence of any one of SEQ ID NOS: 1-27.5. The yeast cell of claim 3 , wherein the ABC transporter has at least 95% identity to SEQ ID NO: 1 claim 3 , SEQ ID NO: 2 claim 3 , or SEQ ID NO: 3.6. The yeast cell of claim 5 , wherein the ABC transporter comprises the amino acid sequence of SEQ ID NO: 1 claim 5 , SEQ ID NO: 2 claim 5 , or SEQ ID NO: 3.7. The yeast cell of claim 1 , wherein the ABC transporter exports the human milk oligosaccharide lacto-N-neotetraose.8. The yeast cell of or claim 1 , wherein the ABC transporter has at least 95% identity to any one of SEQ ID NOS: 28-98.9. The yeast cell of claim 8 , wherein the ABC transporter comprises the amino acid sequence of any one of SEQ ID NOS: 28-98.10. The yeast cell of claim 8 , wherein the ABC ...

CELL-FREE SYSTEM FOR CONVERTING METHANE INTO FUEL AND CHEMICAL COMPOUNDS

The present disclosure relates, in some aspects, to cell-free methods and systems for large-scale conversion of methane to isobutanol, comprising combining, in a bioreactor at elevated pressure, methane, oxygen, and cell lysates containing methane monooxygenase, methanol dehydrogenase, and enzymes that catalyze the conversion of formaldehyde to isobutanol, to form a cell-free reaction mixture, and incubating under suitable conditions the cell-free reaction to convert methane to isobutanol. 175-. (canceled)76. A composition comprising at least two cell lysates and the following enzymes: a methane monooxygenase , a methanol dehydrogenase , a hexulose-6-phosphate synthase , a 6-phospho-3-hexuloisomerase , a 6-phosphofructokinase , a fructose bisphosphate aldolase , a triose phosphate isomerase , a transketolase , a ribose-5-phosphate isomerase or a ribulose-5-phosphate 3-epimerase , a glyceraldehyde 3-phosphate dehydrogenase , a phosphoglycerate kinase , a phosphoglycerate mutase , an enolase , and a pyruvate kinase , wherein at least one of the cell lysates is obtained from recombinant cells that overexpress at least one of the foregoing enzymes.77. The composition of claim 76 , wherein(i) the methane monooxygenase has EC number 1.14.13.25 or 1.14.18.3,(ii) the methanol dehydrogenase has EC number 1.1.1.244, 1.1.2.7, or 1.1.99.37,(iii) the hexulose-6-phosphate synthase has EC number 4.1.2.43,(iv) the 6-phospho-3-hexuloisomerase has EC number 5.3.1.27,(v) the 6-phosphofructokinase has EC number 2.7.1.11,(vi) the fructose bisphosphate aldolase has EC number 4.1.2.13,(vii) the triose phosphate isomerase has EC number 5.3.1.1,(viii) the transketolase has EC number 2.2.1.1,(xi) the ribulose-5-phosphate 3-isomerase has EC number 5.3.1.6, or the ribulose-5-phosphate 3-epimerase has EC number 5.1.3.1,(xii) the glyceraldehyde 3-phosphate dehydrogenase has EC number 1.2.1.12,(xiii) the phosphoglycerate kinase has EC number 2.7.2.3,(xiv) the phosphoglycerate mutase has EC number ...

METHOD AND AGENTS FOR PRODUCING N-ACETYLNEURAMINIC ACID (NEUNAC)

The invention relates to an isolated nucleic acid molecule comprising at least one promoter that is active in fungal cells of the species, wherein a nucleic acid sequence encoding an N-acetylglucosamine-2-epimerase and/or an N-acetylneuraminic acid synthase is operatively bound to each promoter. The at least one promoter that is active in fungal cells is a constitutive promoter. 17-. (canceled)8. A method for producing N-acetylneuraminic acid (NeuNAc) ,comprising cultivating a fungal cell in the presence of an N-acetyl-D-glucosamine source,{'i': 'Trichoderma', 'claim-text': [{'i': 'Trichoderma', 'wherein the nucleic acid molecule comprises at least one constitutive promoter that is active in the genus , and'}, 'wherein the nucleic acid molecule further comprises a nucleic acid sequence encoding an N-acetylglucosamine 2-epimerase operatively linked to one or more of said at least one promoter and/or a nucleic acid sequence encoding an NeuNAc synthase operatively linked to one or more of said at least one promoter., 'wherein the fungal cell is of the genus and comprises a nucleic acid molecule,'}9. The method according to claim 8 , wherein the N-acetyl-D-glucosamine source is chitin.10Trichoderma reesei.. The method according to claim 8 , wherein the fungal cell is the of the species11. The method according to claim 8 , wherein said at least one promoter is selected from the group consisting of the promoters of the glycolytic genes claim 8 , and tef1a claim 8 , act claim 8 , cox4 claim 8 , neg1 and sar1.12. The method according to claim 11 , wherein said at least one promoter is a promoter of the glycolic genes and selected from pki claim 11 , gpd or zwf1.13. The method according to claim 9 , wherein the chitin is colloidal.14. The method according to claim 9 , wherein the chitin is crab-shell chitin.17. The method according to claim 8 , wherein said nucleic acid sequence encoding an N-acetylglucosamine 2-epimerase and/or said nucleic acid sequence encoding an NeuNAc ...

ALLULOSE EPIMERASE VARIANT, METHOD OF PRODUCING THE SAME, AND METHOD OF PRODUCING ALLULOSE USING THE SAME

The present invention provides a novel allulose epimerase variant and various uses thereof, in which glycine (Gly), an amino acid residue at position 216 of the amino acid sequence of wild-type D-allulose 3-epimerase derived from , is substituted with serine (Ser). The novel allulose epimerase variant according to the present invention has a higher conversion activity of fructose to allulose compared to the wild-type D-allulose 3-epimerase derived from , and in particular, it has excellent thermal stability under high temperature conditions of 60° C. or higher, so that the enzyme conversion reaction is performed at the industrial level for mass production of allulose to prevent contamination, to shorten production time, and to reduce production cost. 1. An allulose epimerase variant consisting of the amino acid sequence of SEQ ID NO: 5.2. A polynucleotide encoding the allulose epimerase variant of .3. The polynucleotide according to claim 2 , wherein the polynucleotide includes a nucleotide sequence of SEQ ID NO: 11.4. A recombinant vector including the polynucleotide of .5. A recombinant strain which is transformed by the polynucleotide of .6. A method for producing an allulose epimerase variant claim 2 , the method comprising:{'claim-ref': {'@idref': 'CLM-00005', 'claim 5'}, 'culturing the recombinant strain of to express the allulose epimerase variant; and'}separating the allulose epimerase variant from a lysate of the recombinant strain in which the allulose epimerase variant is expressed.7. A composition for producing allulose claim 1 , the composition comprising the allulose epimerase variant of .8. A composition for producing allulose claim 5 , the composition comprising the recombinant strain of claim 5 , a culture of the recombinant strain claim 5 , or a lysate of the recombinant strain.9. A method for producing allulose claim 5 , the method comprising:{'claim-ref': {'@idref': 'CLM-00001', 'claim 1'}, 'reacting fructose with the allulose epimerase variant ...

RECOMBINANT YEAST CELL

The present invention describes a recombinant yeast cell functionally expressing one or more heterologous nucleic acid sequences encoding for ribulose-1,5-phosphate carboxylase/oxygenase (EC4.1.1.39; Rubisco), and optionally one or more molecular chaperones for Rubisco, and one or more phosphoribulokinase (EC2.7.1.19; PRK), wherein one or more genes of the non-oxidative branch of the pentose phosphate pathway are overexpressed and/or wherein said yeast cell comprises a deletion or disruption of a glycerol-3-phosphate dehydrogenase (GPD) gene. 1. A recombinant yeast cell functionally expressing one or more heterologous nucleic acid sequences encoding for ribulose-1 ,5-phosphate carboxylase/oxygenase (EC4.1.1.39; Rubisco) and optionally one or more molecular chaperones for Rubisco , and further comprising one or more phosphoribulokinase (EC2.7.1.19; PRK) , wherein one or more genes of the non-oxidative branch of the pentose phosphate pathway are overexpressed.2. The recombinant yeast cell of further comprising a deletion or disruption of a glycerol-3-phosphate dehydrogenase (GPD) gene.3. The recombinant yeast cell of wherein one or more genes of the non-oxidative branch of the pentose phosphate pathway are overexpressed and wherein said yeast cell comprises a deletion or disruption of a glycerol-3-phosphate dehydrogenase (GPD) gene.4. The recombinant yeast cell according to wherein the GPD gene encodes for an enzyme having at least EC number 1.1.1.8.5. The recombinant yeast cell according to wherein the GDP is GPD1 and/or GPD2 claim 1 , optionally GPD2.6. The recombinant yeast cell according to claim 1 , wherein the one or more genes of the pentose phosphate pathway that is overexpressed encodes for an enzyme selected from the list of a transaldolase (EC 2.2.1.2) claim 1 , a transketolase (EC 2.2.1.1) claim 1 , a ribose-5-phosphate isomerase (EC 5.3.1.6) and a D-ribulose-5-phosphate 3-epimerase (EC 5.1.3.1).7. The recombinant yeast cell according to claim 1 , wherein ...

Novel cell wall deconstruction enzymes of scytalidium thermophilum, myriococcum thermophilum, and aureobasidium pullulans, and uses thereof

The present invention relates to novel polypeptides and enzymes (e.g., thermostable proteins and enzymes) having activities relating to biomass processing and/or degradation (e.g., cell wall deconstruction), as well as polynucleotides, vectors, cells, compositions and tools relating to same, or functional variants thereof. More particularly, the present invention relates to secreted enzymes that may be isolated from the fungi, Scytalidium thermophilum strain CBS 625.91, Myriococcum thermophilum strain CBS 389.93, and Aureobasidium pullulans strain ATCC 62921. Uses thereof in various industrial processes such as in biofuels, food preparation, animal feed, pulp and paper, textiles, detergents, waste treatment and others are also disclosed.

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

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. 1. 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).2. The co-culture of claim 1 , wherein the host cell is a yeast and the genetically distinct host cell is a yeast or bacterium.3. The recombinant microorganism of claim 1 , wherein said phosphoketolase is a single-specificity phosphoketolase with the Enzyme Commission Number 4.1.2.9.4. The recombinant microorganism of claim 1 , wherein said phosphoketolase is dual-specificity phosphoketolase with the Enzyme Commission Number 4.1.2.22.5Aspergillus, Neurospora, Lactobacillus, Bificlobacterium, Penicillium, Leuconostoc,Oenococcus.. The recombinant microorganism of claim 1 , wherein said phosphoketolase is from a genus selected from the group consisting of and6. The recombinant microorganism of claim 1 , wherein said phosphoketolase corresponds to a polypeptide selected from a group consisting of SEQ ID NOs: 9 claim 1 , 11 claim 1 , 12 claim 1 , 13 claim 1 , 14 ...

METHODS AND COMPOSITIONS FOR MODULATING SIALIC ACID PRODUCTION AND TREATING HEREDITARY INCLUSION BODY MYOPATHY

According to certain embodiments of the present invention, methods for modulating the production of sialic acid in a system are provided, which comprise providing the system with a wild-type GNE-encoding nucleic acid sequence. According to such embodiments, the system may comprise a cell, muscular tissue, or other desirable targets. Similarly, the present invention encompasses methods for producing wild-type GNE in a system that comprises a mutated endogenous GNE-encoding sequence. In other words, the present invention includes providing, for example, a cell or muscular tissue that harbors a mutated (defective) GNE-encoding sequence with a functional wild-type GNE encoding sequence. 1. A method for modulating the production of sialic acid in a system , which comprises providing the system with a wild-type GNE-encoding nucleic acid sequence.2. The method of claim 1 , wherein the wild-type GNE-encoding nucleic acid sequence comprises a promoter operably connected to the wild-type GNE-encoding nucleic acid sequence.3. The method of claim 2 , wherein the promoter is the CMV promoter.4. The method of claim 2 , wherein the wild-type GNE-encoding nucleic acid sequence is injected into the system claim 2 , wherein the system comprises muscle tissue of a mammal.5. The method of claim 2 , wherein the wild-type GNE-encoding nucleic acid sequence is disposed within or is connected to a lipid nanoparticle.6. The method of claim 5 , wherein the wild-type GNE-encoding nucleic acid sequence consists of SEQ ID NO: 9.7. The method of claim 5 , wherein the lipid nanoparticle comprises one or more agents capable of recognizing and binding to a muscle cell or a component thereof.8. A method for producing wild-type GNE in a system claim 5 , wherein the system comprises a mutated endogenous GNE-encoding sequence claim 5 , which comprises providing the system with a wild-type GNE-encoding nucleic acid sequence.9. The method of claim 8 , wherein the wild-type GNE-encoding nucleic acid ...

3-Epimerase

A protein comprising a polypeptide sequence having at least 70% sequence identity to SEQ ID NO: 6, SEQ ID NO: 2 or SEQ ID NO: 4. The protein has ketose 3-epimerase activity. 1. A method of manufacturing a product comprising the steps of:(a) producing allulose by contacting a protein having allulose 3-epimerase activity with a fructose substrate under conditions such that the fructose substrate is converted into allulose;wherein the protein having allulose 3-epimerase activity comprises an amino acid sequence having at least 90% sequence identity to the amino acid sequence of SEQ ID NO: 6; and(b) using the allulose produced in step (a) to manufacture the product.2. The method of claim 1 , wherein the product is a food product claim 1 , a beverage product claim 1 , a pharmaceutical product claim 1 , a nutritional product claim 1 , a sports product claim 1 , or a cosmetic product.3. The method of claim 2 , wherein the food product is a confectionery product claim 2 , a dessert product claim 2 , a cereal product claim 2 , a baked good claim 2 , a frozen dairy product claim 2 , a meat product claim 2 , a dairy product claim 2 , a condiment claim 2 , a snack bar claim 2 , a soup claim 2 , a dressing claim 2 , a mix claim 2 , a prepared food claim 2 , a baby food claim 2 , a diet preparation claim 2 , a syrup claim 2 , a food coating or frosting claim 2 , a dried fruit claim 2 , a sauce claim 2 , a gravy claim 2 , or a jam or jelly.4. The method of claim 2 , wherein the beverage product is a carbonated beverage claim 2 , a non-carbonated beverage claim 2 , a fruit-flavoured beverage claim 2 , a fruit juice claim 2 , a tea claim 2 , milk claim 2 , or coffee.5. The method of claim 1 , wherein the allulose produced in step (a) is at least partially purified.6. The method of claim 1 , wherein the protein having allulose 3-epimerase activity is present in an isolated host cell transformed with a vector comprising a nucleic acid molecule encoding the protein.7. The method of ...

Expression system for psicose epimerase and production for psicose using the same

A gene expression cassette capable of producing psicose at high yield with high stability, a GRAS (Generally recognized as safe) microorganism, a method of producing the enzyme by using the GRAS microorganism, and a method of producing the psicose by using the GRAS microorganism and enzyme are provided. 1Corynebacterium. A gene expression cassette , producing a psicose epimerase in sp. , and comprising:a nucleotide sequence encoding the psicose epimerase; and{'i': 'Corynebacterium', 'a regulating sequence being operably connected to the nucleotide sequence in the upstream regulating the expression of the nucleotide sequence in sp, and comprising a promoter, a ribosome binding site (RBS) sequence and a first spacer sequence in the direction of 5′ to 3′,'}wherein the promoter includes the nucleotide sequence of SEQ ID NO: 1,the ribosome binding site (RBS) sequence is a nucleotide sequence in a size of 7 to 20 bases including the nucleotide sequence of SEQ ID NO: 2, andthe first spacer sequence is selected from the group consisting of the nucleotide sequences of SEQ ID NO: 4 to SEQ ID NO: 6.2. The gene expression cassette according to claim 1 , wherein the regulating sequence further comprises a second RBS sequence which is connected to 3′-end of the first spacer directly or via a linker sequence in a length of 5 to 100 bases claim 1 , andwherein the second RBS sequence is a nucleotide sequence in a size of 7 to 20 bases including the nucleotide sequence of SEQ ID NO: 2.3. The gene expression cassette according to claim 2 , wherein the linker sequence is a nucleotide sequence in a size of 42 to 100 bp which includes the nucleotide sequence of SEQ ID NO: 12.4. The gene expression cassette according to claim 1 , wherein the regulating sequence further comprises a second spacer sequence selected from the group consisting of the nucleotide sequences of SEQ ID NO: 7 to SEQ ID NO: 11 claim 1 , wherein the second spacer is connected to 3′-end of the second RBS.5. The gene ...

Expression system for psicose epimerase and production for psicose using the same

A gene expression cassette capable of producing psicose at high yield with high stability, a GRAS (Generally recognized as safe) microorganism, a method of producing the enzyme by using the GRAS microorganism, and a method of producing the psicose by using the GRAS microorganism and enzyme are provided. 1. A method of producing a psicose epimerase , comprising:{'i': 'Corynebacterium', 'culturing a recombinant sp. cell transformed by a vector comprising a gene expression cassette, and'}{'i': 'Corynebacterium', 'reacting a fructose-containing substrate with at least one selected from the group consisting of an psicose epimerase obtained from the culture of the recombinant sp., a recombinant cell, a culture of the recombinant cell, a lysate of the recombinant cell and an extract of cell culture or the cell lysate,'}{'i': 'Corynebacterium', 'and wherein the gene expression cassette, producing a psicose epimerase in sp., and comprisinga nucleotide sequence encoding the psicose epimerase; and{'i': 'Corynebacterium', 'a regulating sequence being operably connected to the nucleotide sequence in the upstream regulating the expression of the nucleotide sequence in sp, and comprising a promoter, a ribosome binding site (RBS) sequence and a first spacer sequence in the direction of 5′ to 3′,'}wherein the promoter includes the nucleotide sequence of SEQ ID NO: 1,the ribosome binding site (RBS) sequence is a nucleotide sequence in a size of 7 to 20 bases including the nucleotide sequence of SEQ ID NO: 2, andthe first spacer sequence is selected from the group consisting of the nucleotide sequences of SEQ ID NO: 4 to SEQ ID NO: 6.2. The method according to claim 1 , wherein the reacting step is performed by contacting the fructose-containing substrate with a support immobilized by the psicose epimerase or the recombinant cell.3. The method according to claim 1 , wherein the method comprise further a step of adding at least a metal ion selected from the group consisting of a copper ...

NOVEL ARABINOSE-FERMENTING EUKARYOTIC CELLS

Eukaryotic cells, preferably a yeast or a filamentous fungus, with the ability to convert L-arabinose into D-xylulose 5-phosphate are provided, said ability acquired by transformation with nucleotide sequences coding for an arabinose isomerase, a ribulokinase, and a ribulose-5-P-4-epimerase from a bacterium of genus or . Preferably the can produce a fermentation product such as ethanol, lactic acid, 3-hydroxy-propionic acid, acrylic acid, acetic acid, succinic acid, citric acid, amino acids, 1,3-propane-diol, ethylene, glycerol, -lactam antibiotics and cephalosporins. The invention further relates to processes for producing these fermentation products wherein a cell of the invention is used to ferment arabinose into the fermentation products. 1. A eukaryotic cell comprising a first , a second , and a third nucleotide sequence , the expression of which confers on the cell , or increases in the cell , the ability to convert L-arabinose to D-xylulose 5-phosphate , wherein:(a) the first nucleotide sequence encodes an arabinose isomerase protein that comprises an amino acid sequence that is at least 90% identical to SEQ ID NO: 2;(b) the second nucleotide sequence encodes a ribulokinase protein that comprises an amino acid sequence that is at least 90% identical to SEQ ID NO: 6; and(c) the third nucleotide sequence encodes a ribulose-5-P-4-epimerase protein that comprises an amino acid sequence that is at least 90% identical to SEQ ID NO: 7.2Arthrobacter, ClavibacterGramella.. The cell according to claim 1 , wherein at least one of the first claim 1 , second and third nucleotide sequences encodes an amino acid sequence that originates from a bacterial genus selected from the group consisting of claim 1 , and3Arthrobacter aurescens, Clavibacter michiganensisGramella forsetii.. The cell according to claim 1 , wherein the first claim 1 , second claim 1 , and third nucleotide sequence encodes an amino acid sequence that originates from a bacterial species selected from the ...

MICROORGANISMS AND METHODS FOR THE CO-PRODUCTION OF ETHYLENE GLYCOL AND THREE CARBON COMPOUNDS

The present application relates to recombinant microorganisms useful in the biosynthesis of monoethylene glycol (MEG) and one or more three-carbon compounds such as acetone, isopropanol or propene. The MEG and one or more three-carbon compounds described herein are useful as starting material for production of other compounds or as end products for industrial and household use. The application further relates to recombinant microorganisms co-expressing a C2 branch pathway and a C3 branch pathway for the production of MEG and one or more three-carbon compounds. Also provided are methods of producing MEG and one or more three-carbon compounds using the recombinant microorganisms, as well as compositions comprising the recombinant microorganisms and/or optionally the products MEG and one or more three-carbon compounds. 2. The recombinant microorganism of claim 1 , wherein the feedstock comprises exogenous glucose.3. The recombinant microorganism of claim 1 , wherein an endogenous or exogenous D-xylose isomerase catalyzes the conversion of D-xylose to D-xylulose.4. The recombinant microorganism of claim 1 , wherein the recombinant microorganism further expresses at least one exogenous nucleic acid molecule encoding a xylose reductase or aldose reductase that catalyzes the conversion of D-xylose to xylitol and at least one exogenous nucleic acid molecule encoding a xylitol dehydrogenase that catalyzes the conversion of xylitol to D-xylulose.5. The recombinant microorganism of claim 1 , wherein the recombinant microorganism further comprises at least one endogenous or exogenous nucleic acid molecule encoding a secondary alcohol dehydrogenase that catalyzes the conversion of acetone to isopropanol.6. The recombinant microorganism of claim 1 , wherein the recombinant microorganism further comprises: at least one endogenous or exogenous nucleic acid molecule encoding a secondary alcohol dehydrogenase that catalyzes the conversion of acetone to isopropanol; and at least one ...

CELLS PRODUCING GLYCOPROTEINS HAVING ALTERED N- AND O-GLYCOSYLATION PATTERNS AND METHODS AND USE THEREOF

The present application relates to the field of glyco-engineering and, more specifically, to eukaryotic cells wherein both an endoglucosaminidase is present and made deficient in UDP-galactose 4-epimerase (GalE). Typically, a glycoprotein is also present in the cells. These cells can be used to deglycosylate or partly deglycosylate the (exogenous) glycoprotein, in particular, without the need for adding an extra enzyme. Methods are also provided for the application of these cells in protein production. 1. A eukaryotic cell comprising an exogenous nucleic acid sequence encoding an endoglucosaminidase enzyme and deficient in expression and/or activity of an endogenous UDP-galactose 4-epimerase (GalE).2. The eukaryotic cell according to claim 1 , further comprising a second exogenous nucleic acid sequence encoding a glycoprotein.3. The eukaryotic cell according to claim 1 , which does not express an endogenous endoglucosaminidase enzyme.4. The eukaryotic cell according to claim 1 , which is a mammalian cell.5. The eukaryotic cell according to claim 1 , wherein the endoglucosaminidase is a mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase (E.C. 3.2.1.96).6. The eukaryotic cell according to claim 1 , wherein the glycoprotein is secreted by the eukaryotic cell.7. The eukaryotic cell according to claim 1 , wherein the endoglucosaminidase is operably linked to an endoplasmic reticulum or Golgi localization signal.8. A method for producing single GlcNAc modified proteins also lacking O-glycosylation in a eukaryotic cell claim 1 , the method comprising the steps of:providing a eukaryotic cell comprising a first exogenous nucleic acid sequence encoding an endoglucosaminidase enzyme, deficient in expression and/or activity of an endogenous UDP-galactose 4-epimerase (GalE) and comprising a second exogenous nucleic acid sequence encoding a glycoprotein, in conditions suitable for expressing the endoglucosaminidase enzyme and the glycoprotein; andrecovering the glycoprotein ...

3-EPIMERASE

A protein comprising a polypeptide sequence having at least 70% sequence identity to SEQ ID NO:6, SEQ ID NO:2 or SEQ ID NO:4. The protein has ketose 3-epimerase activity. 1. A protein comprising a polypeptide sequence having at least 70% sequence identity to SEQ ID NO: 6 , SEQ ID NO: 2 or SEQ ID NO: 4 , wherein the protein has ketose 3-epimerase activity.2. A protein according to claim 1 , wherein the polypeptide sequence has at least 90% sequence identity to SEQ ID NO: 6 claim 1 , SEQ ID NO: 2 or SEQ ID NO: 4.3. A protein according to claim 1 , wherein the polypeptide sequence comprises the sequence of SEQ ID NO: 13.4. A protein according to claim 1 , wherein the protein is immobilized on a solid substrate.5. (canceled)6. A nucleic acid molecule comprising a polynucleotide sequence encoding a protein according to .7. A nucleic acid molecule according to claim 6 , comprising a polynucleotide sequence which:i) has at least 70% sequence identity to SEQ ID NO: 5, SEQ ID NO: 1 or SEQ ID NO: 3; orii) hybridizes under highly stringent conditions to a polynucleotide having a sequence complementary to the sequence set forth in SEQ ID NO: 5, SEQ ID NO: 1 or SEQ ID NO: 3.8. A vector comprising a nucleic acid molecule according to .9. A host cell comprising a recombinant nucleic acid molecule according to .10. A host cell according to claim 9 , wherein the host cell is a yeast claim 9 , bacterium or other microorganism claim 9 , or is a mammalian claim 9 , plant or other cell culture.11E. coli.. A host cell according to claim 10 , wherein the host cell is12. Allulose produced by a protein according to .13. A method of producing allulose comprising contacting a protein according to with a fructose substrate under conditions such that the fructose substrate is converted into allulose.14. A method according to claim 13 , wherein the protein is present in a host cell.15. A method according to claim 13 , wherein the protein is in isolated form.16. A method according to claim 13 , ...

Biotechnological production of lnt, lnnt and the fucosylated derivatives thereof

The present invention relates to primarily genetically modified microorganisms for in vivo synthesis of lacto-N-tetrose (LNT) and lacto-N-neotetrose (LNnT), and their fucosylated derivatives, and to uses of such microorganisms in methods of producing lacto-N-tetrose and lacto-N-neotetrose, and their fucosylated derivatives.

GLUCOSE METABOLISM WITH MOLECULAR PURGE VALVE

Provided is an engineered pathway that can function in a cell-free system, cellular system or a combination thereof to convert a sugar to a chemical or biofuel. 1. A recombinant , artificial or engineered metabolic pathway comprising a plurality of enzymatic steps that converts a substrate to acetyl-phosphate , pyruvate , glyceraldehyde-3-phosphate , or acetyl-CoA , wherein the pathway includes an unbalanced production and utilization of a co-factor , the pathway comprising a non-naturally occurring purge valve pathway that recycles the co-factor , wherein the purge valve pathway comprises an enzyme that uses the co-factor to convert a metabolite to an intermediate or product in one or more of the plurality of enzymatic steps.2. The recombinant claim 1 , artificial or engineered pathway of claim 1 , wherein the co-factors are oxidizing/reducing co-factors.3. The recombinant claim 2 , artificial or engineered pathway of claim 2 , wherein the oxidizing/reducing co-factors are NAD/NADH claim 2 , NADP/NADPH or FAD/FADH.4. The recombinant claim 3 , artificial or engineered pathway of claim 3 , wherein a first cofactor comprises NAD/NADH and a second cofactor comprises NADP/NADPH.5. The recombinant claim 1 , artificial or engineered pathway of claim 1 , wherein the purge valve pathway comprises an NADH oxidase.6. The recombinant claim 5 , artificial or engineered pathway of claim 5 , wherein the NADH oxidase is a NoxE or homolog thereof.7. The recombinant claim 6 , artificial or engineered pathway of claim 6 , wherein the NADH oxidase comprises a sequence that is at least 50% identical to SEQ ID NO:18.8. The recombinant claim 1 , artificial or engineered pathway of claim 1 , wherein the pathway carries out the following:(i) converts glucose to glucose-6-phosphate;(ii) converts glucose-6-phosphate to 6-phospho-D-glucono-1,5-lactone;(iii) converts 6-phospho-D-glucono-1,5-lactone to 6-phospho-D-gluconate;(iv) converts 6-phospho-D-gluconate to ribulose-5-phosphate;(v) ...

Antitumor agent and evaluation method thereof

Provided is a novel cancer treatment method that exhibits a significantly excellent antitumor effect and causes less adverse reactions. The present invention provides an antitumor agent wherein a peptide having 4 linked epitopes and an immune checkpoint modulator are administered in combination. An antitumor effect in humans can be evaluated by providing a cell coexpressing an epitope peptide of a human tumor antigen derived from SART2 and human HLA-A24.

Cells with improved pentose conversion

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.

ENZYMATIC PRODUCTION OF D-ALLULOSE

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 ...

Method for establishing a non-human mammalian animal model suffering from obesity or related disease and use thereof

A method for preparing a model of an animal suffering from non-human mammal obesity or a related disease, comprising the following steps: (a) providing a cell of a non-human mammal, and inactivating Glce gene in the cell, thereby obtaining a non-human mammal cell with an inactivated Glce gene; and (b) using the cell having an inactivated Glce gene obtained in step (a) to prepare and obtain a model of an animal suffering from Glce gene-inactivated obesity or a related disease. The animal model is an effective model for an animal suffering from obesity or a related disease, which may be used for researching diseases such as obesity, hyperlipidemia, hypertension, and diabetes, and may also be used for screening and testing experiments of specific drugs.

3-EPIMERASE

A protein comprising a polypeptide sequence having at least 70% sequence identity to SEQ ID NO: 6, SEQ ID NO: 2 or SEQ ID NO: 4. The protein has ketose 3-epimerase activity. 1. A protein comprising a polypeptide sequence having at least 70% sequence identity to SEQ ID NO: 6 , SEQ ID NO: 2 or SEQ ID NO: 4 , wherein the protein has ketose 3-epimerase activity.2. A protein according to claim 1 , wherein the polypeptide sequence has at least 90% sequence identity to SEQ ID NO: 6 claim 1 , SEQ ID NO: 2 or SEQ ID NO: 4.3. A protein according to claim 1 , wherein the polypeptide sequence comprises the sequence of SEQ ID NO: 13.4. A protein according to claim 1 , wherein the protein is immobilized on a solid substrate.5. A nucleic acid molecule comprising a polynucleotide sequence encoding a protein according to .6. A nucleic acid molecule according to claim 5 , comprising a polynucleotide sequence which:i) has at least 70% sequence identity to SEQ ID NO: 5, SEQ ID NO: 1 or SEQ ID NO: 3; orii) hybridizes under highly stringent conditions to a polynucleotide having a sequence complementary to the sequence set forth in SEQ ID NO: 5, SEQ ID NO: 1 or SEQ ID NO: 3.7. A vector comprising a nucleic acid molecule according to .8. A host cell comprising a recombinant nucleic acid molecule according to .9. A host cell according to claim 8 , wherein the host cell is a yeast claim 8 , bacterium or other microorganism claim 8 , or is a mammalian claim 8 , plant or other cell culture.10E. coli.. A host cell according to claim 9 , wherein the host cell is11. Allulose produced by a protein according to .12. A method of producing allulose comprising contacting a protein according to with a fructose substrate under conditions such that the fructose substrate is converted into allulose.13. A method according to claim 12 , wherein the protein is present in a host cell.14. A method according to claim 12 , wherein the protein is in isolated form.15. A method according to claim 12 , wherein the ...

Composition for Epimerization of Non-Phosphorylated Hexose Comprising Sugar Epimerases Derived from Thermophiles

The present invention relates to a composition for epimerization of a non-phosphorylated hexose, comprising sugar epimerases derived from thermophiles, and a method for preparing a non-phosphorylated hexose epimer using the composition. The sugar epimerases derived from thermophiles according to the present invention can effectively catalyze an epimerization reaction of a non-phosphorylated hexose and can easily produce an epimer form of the non-phosphorylated hexose, in particular a rare sugar hexose, and thus can be usefully utilized in the pharmaceutical and food industry. 112-. (canceled)13Thermotoga.. A method for preparing a non-phosphorylated hexose epimer , the method comprising treating a non-phosphorylated hexose with UDP-glucose-4-epimerase derived from the genus of14Thermotoga maritima.. The method of claim 13 , wherein the UDP-glucose-4-epimerase is from15. The method of claim 13 , wherein the non-phosphorylated hexose is an aldohexose or a ketohexose.16. The method of claim 15 , wherein the aldohexose is at least one selected from the group consisting of allose claim 15 , altrose claim 15 , glucose claim 15 , mannose claim 15 , gulose claim 15 , idose claim 15 , talose claim 15 , and galactose.17. The method of claim 15 , wherein the ketohexose is at least one selected from the group consisting of fructose claim 15 , psicose claim 15 , sorbose claim 15 , and tagatose.18. The method of claim 13 , wherein the non-phosphorylated hexose epimer is a C2 or C4 epimer.19. The method of claim 13 , wherein the non-phosphorylated hexose is tagatose and epimer of the non-phosphorylated hexose is fructose.20. The method of claim 13 , wherein the non-phosphorylated hexose is fructose and epimer of the non-phosphorylated hexose is tagatose.21. The method of claim 13 , wherein the non-phosphorylated hexose is glucose and epimer of the non-phosphorylated hexose is mannose.22. The method of claim 13 , wherein the non-phosphorylated hexose is galactose and epimer of the ...

A novel thermostable fructose-6-phosphate-3-epimerase and a method for producing allulose using the same

The present disclosure relates to fructose-6-phosphate-3-epimerase consisting of an amino acid sequence of SEQ ID NO: 1, a nucleic acid encoding the fructose-6-phosphate-3-epimerase, and a transformant comprising the nucleic acid. Additionally, the present disclosure relates to a composition for producing allulose, which comprises the fructose-6-phosphate-3-epimerase of the present disclosure, and a method for producing allulose using the fructose-6-phosphate-3-epimerase of the present disclosure.

A Novel D-Psicose 3-Epimerase and Method for Producing D-Psicose Using the Same

The present disclosure relates to novel D-psicose 3-epimerase and a method for producing psicose using the same. 110- (canceled)11. A method for producing D-psicose , comprising reacting D-fructose with D-psicose 3-epimerase consisting of an amino acid sequence of SEQ ID NO: 1 , a microorganism expressing the D-psicose 3-epimerase , or a culture of the microorganism.12. The method of claim 11 , wherein the D-psicose 3-epimerase is encoded by a polynucleotide sequence of SEQ ID NO: 2.13. The method of claim 11 , wherein the reaction is carried out at a pH of 5.0 to 9.0.14. The method of claim 11 , wherein the reaction is carried out at a temperature of 40° C. to 90° C.15. The method of claim 11 , wherein the reaction is carried out for 0.5 hours to 48 hours.16. The method of claim 11 , wherein the method further comprises reacting a metal with the D-psicose 3-epimerase claim 11 , the microorganism expressing the D-psicose 3-epimerase claim 11 , or the culture of the microorganism claim 11 , before reacting the D-fructose.17. The method of claim 11 , wherein the method further comprises reacting a metal with the D-psicose 3-epimerase claim 11 , the microorganism expressing the D-psicose 3-epimerase claim 11 , or the culture of the microorganism claim 11 , after reacting the D-fructose.18. The method of claim 11 , wherein the method further comprises reacting a metal with the D-psicose 3-epimerase claim 11 , the microorganism expressing the D-psicose 3-epimerase claim 11 , or the culture of the microorganism claim 11 , simultaneously with reacting the D-fructose.19. A method for producing D-psicose claim 11 , the D-fructose is reacted with the D-psicose 3-epimerase consisting of an amino acid sequence of SEQ ID NO: 1. The present disclosure relates to D-psicose 3-epimerase and a method for producing D-psicose using the same.D-Psicose (hereinafter referred to as “psicose”) is a monosaccharide known as a rare sugar present in nature. Psicose has a sweetness degree of ...

MOUSE MODEL AND TREATMENT OF HEREDITARY INCLUSION BODY MYOPATHY

Disclosed herein are methods of treating HIBM in a subject comprising identifying subject in need thereof; and administering to the subject a compound, or a pharmaceutically acceptable salt, ester, amide, glycol, peptidyl, or prodrug thereof, wherein the compound is a compound that is biosynthesized in a wild type individual along a biochemical pathway between glucose and sialic acid, inclusive. Also disclosed herein are vectors comprising a nucleic acid sequence that encodes a polypeptide having at least 80% sequence identity to the sequence set forth in SEQ ID NO:2, recombinant cells comprising these vectors, and recombinant animals comprising the cells. In addition, methods of identifying a compound having therapeutic effect for HIBM are disclosed. 1. A vector comprising a nucleic acid sequence that encodes a polypeptide having at least 80% sequence identity to the sequence set forth in SEQ ID NO:2.2. The vector of claim 1 , wherein the polypeptide has a sequence selected from the group consisting of set forth in SEQ ID NO:2 through SEQ ID NO:19.3. A recombinant cell comprising the vector wherein the vector comprises a nucleic acid sequence that encodes a polypeptide having at least 80% sequence identity to the sequence set forth in SEQ ID NO:2.4. The cell of claim 3 , wherein the polypeptide has a sequence selected from the group consisting of set forth in SEQ ID NO:2 through SEQ ID NO:19.5. The cell of claim 3 , wherein the cell is a stem cell.6. The cell of claim 5 , wherein the cell is an embryonic stem cell.7. The cell of claim 5 , wherein the cell is murine.8. A recombinant animal wherein the animal has a cell that expresses a polypeptide having at least 80% sequence identity to the sequence set forth in SEQ ID NO:2.9. The animal of claim 8 , wherein the animal is made by the process of:producing a vector comprising a nucleic acid sequence that encodes a polypeptide having at least 80% sequence identity to the sequence set forth in SEQ ID NO:2;producing a ...

Fructose to Allulose Conversion

The present disclosure describes a method of producing allulose from fructose with a novel psicose-3-epimerase enzyme from a species. Once identified and isolated, the psicose-3-epimerase gene was cloned into a novel production strain and evaluated in both benchtop and pilot scale production environments. Evaluation of the in vivo enzyme activity and downstream processing involves immobilization of the enzyme on solid matrix resins, which is discloses herein. 1. A method of producing allulose comprising:{'i': 'Burkholderia', 'contacting a solution containing fructose with a psicose-3-epimerase enzyme from a species having at least 84% sequence identity to SEQ ID NO:1 for a time and under conditions suitable to convert at least a portion of the fructose to allulose.'}2. The method of claim 1 , wherein said psicose-3-epimerase is immobilized on a solid matrix resin.3. The method of claim 2 , wherein said solid matrix resin is a weak base anion exchange resin.4. The method of claim 2 , wherein said solid matrix resin is a phenol formaldehyde based condensate resin functionalized to contain tertiary amine free base groups.5. The method of wherein said solid matrix resin is DUOLITE™ A568.6. The method of claim 2 , wherein said solid matrix is a methacrylic acid based resin functionalized to contain C2-C6 amine linkages.7. The method of wherein said solid matrix resin from the group consisting of Lifetech™ ECR8315 claim 6 , Lifetech™ ECR 8415 claim 6 , and SEPABEADS™ EC-HA.8. The method wherein said resin is Lifetech™ ECR 8415.9BulkholderiaBurkholderia, Candidatus Burkholderia verschuerenii, Burkholderia jiangsuensis, BurkholderiaBurkholderia grimmiaeCandidatus Burkholderia brachyanthoides.. The method of wherein said sp. is selected from the group consisting of RP64sp. MR1 claim 1 , claim 1 , and10BulkholderiaBurkholderia. The method of wherein said sp. is RP64.11. The method of wherein said enzyme has a polypeptide sequence selected from the group consisting of SEQ ID ...

FERMENTATIVE PRODUCTION OF OLIGOSACCHARIDES BY TOTAL FERMENTATION UTILIZING A MIXED FEEDSTOCK

Disclosed are genetically engineered microbial cells for the production of oligosaccharides comprising a galactose-β1,4-glucose moiety at their reducing end, wherein said microbial cells are able to produce said oligosaccharides in the absence of exogenously added lactose, and a method of producing said oligosaccharides using said microbial cells. 1. A genetically engineered microbial cell for the production of lactose or an oligosaccharide of interest which comprises a galactose-β1 ,4-glucose moiety at its reducing end , wherein said microbial cell possesses:at least one glucose transporter for translocating glucose from the culture medium into the microbial cell's cytoplasm;an UDP-galactose biosynthesis pathway; andat least one β-1,4-galactosyltransferase being able to galactosylate free glucose to intracellularly produce lactose.2. The genetically engineered microbial cell according to claim 1 , wherein the at least one glucose transporter is selected from the group consisting of glucose facilitated diffusion proteins and glucose translocating permeases.3. The genetically engineered microbial cell according to claim 1 , wherein said microbial cell expresses or overexpresses at least one gene encoding the glucose transporter claim 1 , preferably at least one gene selected from the group consisting of glf claim 1 , galP and functional variants thereof.4. The genetically engineered microbial cell according to claim 1 , wherein said microbial cell possesses a phosphoglucomutase claim 1 , a UTP-glucose-1-phosphate-uridyltransferase claim 1 , and a UDP-glucose 4-epimerase.5Neisseria meningitidisAggregatibacter aphrophilusPasteurella multocida. The genetically engineered microbial cell according to wherein the β-1 claim 1 ,4-galactosyltransferase is encoded by a gene selected from the group consisting of IgtB claim 1 , lex-1 claim 1 , galTpm1141 and functional variants thereof.6. The genetically engineered microbial cell according to claim 1 , wherein said microbial ...

MICROORGANISMS AND METHODS FOR THE CO-PRODUCTION OF ETHYLENE GLYCOL AND THREE CARBON COMPOUNDS

The present application relates to recombinant microorganisms useful in the biosynthesis of monoethylene glycol (MEG) and one or more three-carbon compounds such as acetone, isopropanol or propene. The MEG and one or more three-carbon compounds described herein are useful as starting material for production of other compounds or as end products for industrial and household use. The application further relates to recombinant microorganisms co-expressing a C2 branch pathway and a C3 branch pathway for the production of MEG and one or more three-carbon compounds. Also provided are methods of producing MEG and one or more three-carbon compounds using the recombinant microorganisms, as well as compositions comprising the recombinant microorganisms and/or optionally the products MEG and one or more three-carbon compounds. 14.-. (canceled)5. A recombinant microorganism capable of co-producing monoethylene glycol (MEG) and acetone from a feedstock comprising exogenous D-xylose , wherein the recombinant microorganism expresses one or more of the following:(a) at least one endogenous or exogenous nucleic acid molecule encoding a D-tagatose 3-epimerase that catalyzes the conversion of D-xylulose to D-ribulose;(b) at least one endogenous or exogenous nucleic acid molecule encoding a D-ribulokinase that catalyzes the conversion of D-ribulose from (a) to D-ribulose-1-phosphate;(c) at least one endogenous or exogenous nucleic acid molecule encoding a D-ribulose-1-phosphate aldolase that catalyzes the conversion of D-ribulose-1-phosphate from (b) to glycolaldehyde and dihydroxyacetonephosphate (DHAP);(d) at least one endogenous or exogenous nucleic acid molecule encoding a glycolaldehyde reductase that catalyzes the conversion of glycolaldehyde from (c) to MEG;(e) at least one exogenous nucleic acid molecule encoding a thiolase that catalyzes the conversion of acetyl-CoA to acetoacetyl-CoA;(f) at least one endogenous or exogenous nucleic acid molecule encoding an acetate: ...

CELLS WITH IMPROVED PENTOSE CONVERSION

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 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 ...

NOVEL PSICOSE-6-PHOSPHATE PHOSPHATASE, COMPOSITION FOR PRODUCING PSICOSE INCLUDING SAID ENZYME, METHOD FOR PRODUCING PSICOSE USING SAID ENZYME

The present application relates to a psicose-6-phosphate phosphatase comprising motif A and motif B, a composition for producing D-psicose comprising the enzyme, and a method for producing D-psicose using the enzyme. 1. A psicose-6-phosphate phosphatase comprising motif A represented by Xa1-Xa2-Xa3-DPLDG-Xa4 wherein Xa1 is W , F , V , I or A , Xa2 is I , F , V , A or absent , Xa3 is V , I or L , and Xa4 is T or S and motif B represented by Ya1-D-Ya2-Wa1-Ya3-Wa2-Ya4-Wa3 wherein Ya1 is W , Y , T , L or V , Ya2 is V , I , C , F or A , Wa1 is AAG , AAS , SAG , APG , APF , AGG , APL or AGA , Ya3 is W , I , P , M , V , Y , F , R , L , T or S , Wa2 is LLV , LIV , LLI , LII , ILI , FIA , ALV , IIA , VLV , VIL , TIG , NFC or PIF , Ya4 is E , R , S , T , L , K or P , and Wa3 is EAGG , EGGG , EAKG , KAGG , AAGG , YVDG , EAGA or RLGV.2. The psicose-6-phosphate phosphatase according to claim 1 , wherein claim 1 , in motif A claim 1 , Xa1 is W or F claim 1 , Xa2 is I or V claim 1 , Xa3 is V or I claim 1 , and Xa4 is T; and in motif B claim 1 , Ya1 is W claim 1 , Ya2 is V or I claim 1 , Wa1 is AAG claim 1 , Ya3 is W claim 1 , I or V claim 1 , Wa2 is LLV claim 1 , LIV claim 1 , LII or LLI claim 1 , Ya4 is E claim 1 , R or S claim 1 , and Wa3 is EAGG or EGGG.3. The psicose-6-phosphate phosphatase according to claim 1 , wherein the psicose-6-phosphate phosphatase comprises any one of the amino acid sequences set forth in SEQ ID NOS: 1 claim 1 , 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 , and 20 or a sequence having a identity of at least 85% to an amino acid sequence other than motif A and motif B in the sequences set forth in SEQ ID NOS: 1 claim 1 , 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 ...

CELL SUITABLE FOR FERMENTATION OF A MIXED SUGAR COMPOSITION

The present invention relates to a cell suitable for production of one or more fermentation product from a sugar composition comprising glucose, galactose, arabinose and xylose, wherein the cell comprises two to fifteen copies of one or more xylose isomerase gene or two to fifteen copies of one or more xylose reductase and xylitol dehydrogenase, and two to ten copies of araA, araB and araD, genes, wherein these genes are integrated into the cell genome. 1Saccharomyces cerevisiae. A transformed cell suitable for producing at least one fermentation product from a sugar composition comprising glucose , galactose , xylose , arabinose and mannose , wherein said cell comprises:(a) two to fifteen copies of at least one xylose isomerase gene or two to fifteen copies of at least one xylose reductase and xylitol dehydrogenase, and(b) from two to ten copies of L-arabinose isomerase (araA), L-ribulokinase (arae), and L-ribulose-5-phosphate 4-epimerase (araD) genes,wherein said genes are integrated into the cell genome,and wherein said cell comprises a disruption or deletion of the GAL80 (transcriptional repressor) gene.2. The yeast cell according to claim 1 , wherein said cell is capable of converting at least 90% of glucose claim 1 , xylose arabinose claim 1 , galactose and mannose available claim 1 , into a fermentation product.3. The yeast cell according to claim 1 , wherein said cell comprises overexpressed PPP-genes TAL1 (transaldolase) claim 1 , TKL1 (transketolase) claim 1 , RPE1 (ribulose-phosphate 3-epimerase) claim 1 , and RKI1 (ribulose-5-phosphate isomerase).4. The yeast cell according to claim 1 , wherein said cell comprises a XKS1 (xylulose kinase) gene.5. The yeast cell according to claim 1 , wherein an aldose reductase gene is deleted.6. The yeast cell according to claim 1 , wherein all genes exogenous to said cell are integrated into the genome of said cell.7. A yeast cell according to claim 1 , wherein genes have been introduced in said cell by introduction ...

VARIANTS OF GAL2 TRANSPORTER AND THEIR USES

The present invention relates to polypeptides which are Gal2 variants comprising at least one amino acid substitution at a position corresponding to T354, and optionally further amino acid substitution(s). The present invention further relates to nucleic acid molecules encoding the polypeptides and to host cells containing said nucleic acid molecules. The present invention further relates to a method for the production of bioethanol and/or other bio-based compounds, comprising the expression of said nucleic acid molecules, preferably in said host cells. The present invention also relates to the use of the polypeptides, nucleic acids molecule or host cells for the production of bioethanol and/or other bio-based compounds, and/or for the recombinant fermentation of biomaterial containing pentose(s), preferably D-xylose and/or L-arabinose. 1. A polypeptide , comprising at least one amino acid substitution at a position corresponding to T354 of the amino acid sequence of SEQ ID NO: 1 ,wherein the polypeptide has at least 80% sequence identity with the amino acid sequence of SEQ ID NO: 1, and wherein the polypeptide has an in vitro and/or in vivo pentose transport function.2Saccharomyces cerevisiae.. The polypeptide according to claim 1 , wherein the polypeptide is Gal2 of3. The polypeptide according to claim 1 , wherein the amino acid substitution at a position corresponding to T354 of the amino acid sequence of SEQ ID NO: 1 is T354A.4. The polypeptide according to claim 1 , comprising a further amino acid substitution at a position corresponding to V71 of the amino acid sequence of SEQ ID NO: 1.5. The polypeptide according to claim 1 , wherein the amino acid substitution at a position corresponding to T354 increases the activity of the in vitro and/or in vivo pentose transport function compared to a polypeptide without such amino acid substitution.6. The polypeptide according to claim 1 , wherein the amino acid substitution at a position corresponding to T354 increases ...

Composition for Epimerization of Non-Phosphorylated Hexose Comprising Sugar Epimerases Derived from Thermophiles

The present invention relates to a composition for epimerization of a non-phosphorylated hexose, comprising sugar epimerases derived from thermophiles, and a method for preparing a non-phosphorylated hexose epimer using the composition. The sugar epimerases derived from thermophiles according to the present invention can effectively catalyze an epimerization reaction of a non-phosphorylated hexose and can easily produce an epimer form of the non-phosphorylated hexose, in particular a rare sugar hexose, and thus can be usefully utilized in the pharmaceutical and food industry. 1. A composition for epimerization of a non-phosphorylated hexose , comprising sugar epimerases derived from thermophiles.2Thermotogales.. The composition of claim 1 , wherein the thermophile is from the order3. The composition of claim 1 , wherein the sugar epimerase is at least one selected from the group consisting of aldose-1-epimerase claim 1 , D-tagatose 3-epimerase claim 1 , L-ribulose-5-phosphate 4-epimerase claim 1 , UDP-N-acetylglucosamine 2-epimerase claim 1 , ribulose phosphate 3-epimerase claim 1 , nucleotide sugar epimerase claim 1 , UDP-glucose-4-epimerase claim 1 , and D-tagaturonate epimerase.4. The composition of claim 1 , wherein the non-phosphorylated hexose is an aldohexose or a ketohexose.5. The composition of claim 4 , wherein the aldohexose is at least one selected from the group consisting of allose claim 4 , altrose claim 4 , glucose claim 4 , mannose claim 4 , gulose claim 4 , idose claim 4 , talose claim 4 , and galactose.6. The composition of claim 4 , wherein the ketohexose is at least one selected from the group consisting of fructose claim 4 , psicose claim 4 , sorbose claim 4 , and tagatose.7. The composition of claim 1 , wherein the epimerization is C-2 claim 1 , C-3 claim 1 , or C-4 epimerization of the non-phosphorylated hexose.8Thermotogales.. The composition of claim 1 , wherein the epimer of the non-phosphorylated hexose is tagatose or fructose when the ...

A bacillus subtilis strain, culture method and use thereof

A Bacillus subtilis strain or a progeny thereof, a method of culturing the same and uses thereof. The invention also relates to a culture and lysate of the Bacillus subtilis strain or its progeny, and a method for producing D-psicose epimerase and producing D-psicose using the Bacillus subtilis strain or its progeny.

POLYNUCLEOTIDE ENCODING PSICOSE EPIMERASE AND METHOD OF PRODUCING PSICOSE USING THE SAME

A psicose 3-epimerase, a polynucleotide encoding the enzyme, a recombinant vector carrying the polynucleotide, a recombinant cell harboring the recombinant vector, and use thereof are provided. 1. A psicose epimerase , comprising the amino acid sequence of SEQ ID NO: 1.2. A polynucleotide encoding the psicose epimerase of .3. The polynucleotide of claim 2 , which comprises the nucleotide sequence of SEQ ID NO: 2.4. A recombinant vector carrying the polynucleotide of .5. A recombinant cell harboring the recombinant vector of .6. A composition for production of psicose claim 4 , comprising at least one selected from the group consisting of a protein comprising the amino acid sequence of SEQ ID NO: 1 claim 4 , a polynucleotide encoding the protein claim 4 , a recombinant vector carrying the polynucleotide claim 4 , a recombinant cell harboring the recombinant vector claim 4 , a culture of the recombinant cell claim 4 , and a lysate of the recombinant cell.7. The composition of claim 6 , which further comprises at least one selected from the group consisting of a copper ion claim 6 , a manganese ion claim 6 , a magnesium ion claim 6 , a zinc ion claim 6 , a nickel ion claim 6 , a cobalt ion claim 6 , an iron ion claim 6 , an aluminum ion claim 6 , and a calcium ion.8. A method for producing psicose claim 6 , comprising reacting at least one selected from the group consisting of a protein comprising the amino acid sequence of SEQ ID NO: 1 claim 6 , a polynucleotide encoding the protein claim 6 , a recombinant vector carrying the polynucleotide claim 6 , a recombinant cell harboring the recombinant vector claim 6 , a culture of the recombinant cell claim 6 , and a lysate of the recombinant cell claim 6 , with D-fructose.9. The method of claim 8 , wherein the D-fructose is used at a concentration of 55 to 75% (w/w).10. The method of claim 8 , wherein the reacting is carried out at a pH of 7 to 10.11. The method of claim 8 , wherein the reacting is carried out at a ...

Process For Producing Ethanol And Fermenting Organisms

Processes for producing ethanol comprise saccharifying cellulosic material with a cellulolytic enzyme composition and fermenting the saccharified cellulosic material with a fermenting microorganism to produce ethanol. The fermenting organism is CIBTS1260 (deposited under Accession No. NRRL Y-50973 at the Agricultural Research Service Culture Collection (NRRL), Illinois 61604 U.S.A.) or a fermenting organism that has properties that the same or about the same as that of CIBTS1260). 1. A process for producing ethanol , comprising:(a) saccharifying a cellulosic material with a cellulolytic enzyme composition;{'i': Saccharomyces cerevisiae', 'Saccharomyces cerevisiae, '(b) fermenting the saccharified cellulosic material with a fermenting microorganism to produce the fermentation product; wherein the fermenting organism is CIBTS1260 (deposited under Accession No. NRRL Y-50973 at the Agricultural Research Service Culture Collection (NRRL), Illinois 61604 U.S.A.) or a fermenting organism having properties that are about the same as that of CIBTS1260.'}2. The process of claim 1 , comprising recovering the fermentation product from the fermentation.3. The process of claim 1 , wherein the cellulosic material is pretreated.4. The process of claim 1 , wherein the cellulolytic enzyme composition comprises one or more enzymes selected from the group consisting of a cellulase claim 1 , an AA9 polypeptide claim 1 , a hemicellulase claim 1 , a CIP claim 1 , an esterase claim 1 , an expansin claim 1 , a ligninolytic enzyme claim 1 , an oxidoreductase claim 1 , a pectinase claim 1 , a protease claim 1 , and a swollenin.56-. (canceled)7. The process of claim 1 , wherein steps (a) and (b) are performed simultaneously in a simultaneous saccharification and fermentation (SSF).8. The process of claim 1 , wherein steps (a) and (b) are performed sequentially (SHF).910.-. (canceled)11Saccharomyces cerevisiae. The process of claim 1 , wherein fermenting organism having properties that are ...

METHOD FOR PRODUCING PSICOSE

A method of preparing D-psicose includes a step of reacting D-fructose as a substrate and an epimerase thereof in microorganisms at a temperature of 40° C. or higher. The method may further includes inducing the microorganisms to have resting cells by culturing the microorganisms in a medium not containing the D-fructose before the reaction. The method of preparing D-psicose may significantly improve the production amount of D-psicose and production rate of D-psicose. 1. A method of preparing D-psicose , comprising a step of reacting D-fructose as a substrate and an epimerase thereof in microorganisms at a temperature of 40° C. or higher.2. The method according to claim 1 , wherein the microorganisms express the epimerase endogenously or by transformation.3. The method according to claim 1 , further comprising a step of inducing the microorganisms to have resting cells by culturing the microorganisms in a medium not containing the D-fructose before the reaction.4. The method according to claim 1 , further comprising a step of recovering and reusing the microorganisms to convert D-fructose into D-psicose after the reaction.5. The method according to claim 4 , wherein the microorganisms are gram-positive bacteria.6. The method according to claim 1 , wherein the D-fructose is provided from a medium containing only inorganic salts and D-fructose.7. The method according to claim 6 , wherein the inorganic salts are manganese salts or cobalt salts.8. The method according to claim 1 , wherein the reaction temperature is 40 to 90° C.9Escherichia, Bacillus, Corynebacterium, Actinomyces,Kluyveromyces. The method according to claim 1 , wherein the microorganisms are yeasts claim 1 , or combinations thereof.10Agrobacterium tumefaciensAnaerostipes caccae. The method according to claim 1 , wherein the microorganisms are transformed with a gene encoding -derived D-psicose 3-epimerase corresponding to SEQ ID NO: 1 or a gene encoding -derived D-psicose 3-epimerase corresponding to ...

DEGRADATION PATHWAY FOR PENTOSE AND HEXOSE SUGARS

The present application relates to recombinant microorganisms useful in the biosynthesis of monoethylene glycol (MEG) or glycolic acid (GA), or MEG and one or more co-product, from one or more pentose and/or hexose sugars. Also provided are methods of producing MEG (or GA), or MEG (or GA) and one or more co-product, from one or more pentose and/or hexose sugars using the recombinant microorganisms, as well as compositions comprising the recombinant microorganisms and/or the products MEG (or GA), or MEG and one or more co-product. 1. A recombinant microorganism expressing at least one enzyme having pentose-phosphate aldolase activity wherein said microorganism produces one or more products derived from glyceraldehyde-3-phosphate (G3P) and glycolaldehyde from one or more pentose and/or hexose sugars via a pentose-phosphate intermediate; wherein the one or more product is selected from monoethylene glycol (MEG) and glycolic acid (GA) wherein the pentose-phosphate intermediate is D-ribose-5-phosphate , D-ribulose-5-phosphate or D-xylulose-5-phosphate and wherein the enzyme have D-ribose-5-phosphate , D-ribulose-5-phosphate or D-xylulose-5-phosphate aldolase activity.23.-. (canceled)4. The recombinant microorganism of claim 1 , wherein the recombinant microorganism co-produces monoethylene glycol (MEG) or glycolic acid (GA) and one or more co-products claim 1 , wherein the one or more co-products are selected from acetone claim 1 , isopropanol claim 1 , propene claim 1 , L-serine claim 1 , glycine claim 1 , monoethanolamine (MEA) claim 1 , ethylenediamine claim 1 , or a combination thereof.5. (canceled)6E. coli;. The recombinant microorganism of claim 1 , wherein the microorganism comprises expression of at least one enzyme having transketolase activity claim 1 , wherein the at least one enzyme having transketolase activity is encoded by an amino acid sequence having at least 70% sequence identity claim 1 , at least 80% sequence identity claim 1 , or at least 90% ...

3-EPIMERASE

A protein comprising a polypeptide sequence having at least 70% sequence identity to SEQ ID NO: 6, SEQ ID NO: 2 or SEQ ID NO: 4. The protein has ketose 3-epimerase activity. 1. A protein comprising a polypeptide sequence having at least 70% sequence identity to SEQ ID NO: 6 , SEQ ID NO: 2 or SEQ ID NO: 4 , wherein the protein has ketose 3-epimerase activity.2. A protein according to claim 1 , wherein the polypeptide sequence has at least 80% claim 1 , 90% claim 1 , 95% or 99% sequence identity claim 1 , or 100% sequence identity claim 1 , to SEQ ID NO: 6 claim 1 , SEQ ID NO: 2 or SEQ ID NO: 4.3. A protein according to or claim 1 , wherein the polypeptide sequence comprises the sequence of SEQ ID NO: 13.4. A protein according to any one of to claim 1 , wherein the protein is immobilized on a solid substrate.5. Use of a protein according to any one of the preceding claims for synthesizing allulose.6. A nucleic acid molecule comprising a polynucleotide sequence encoding a protein according to any one of to .7. A nucleic acid molecule according to claim 6 , comprising a polynucleotide sequence which:i) has at least 70%, 80%, 90%, 95% or 99% sequence identity, or 100% sequence identity, to SEQ ID NO: 5, SEQ ID NO: 1 or SEQ ID NO: 3; orii) hybridizes under highly stringent conditions to a polynucleotide having a sequence complementary to the sequence set forth in SEQ ID NO: 5, SEQ ID NO: 1 or SEQ ID NO: 3.8. A vector comprising a nucleic acid molecule according to or .9. A host cell comprising a recombinant nucleic acid molecule according to or .10. A host cell according to claim 9 , wherein the host cell is a yeast claim 9 , bacterium or other microorganism claim 9 , or is a mammalian claim 9 , plant or other cell culture.11E. coli.. A host cell according to claim 10 , wherein the host cell is12. Allulose produced by a protein according to any one of to .13. A method of producing allulose comprising contacting a protein according to any one of to with a fructose ...

Composition for preparing tagatose and method for preparing tagatose from fructose

The present invention relates to a composition for preparing tagatose, wherein the composition is used for preparing tagatose from fructose and contains a protein including any one amino acid sequence of SEQ ID NOS: 1 to 7 or a microorganism expressing the protein. In addition, the present invention relates to a method for preparing tagatose from fructose, the method comprising a step of allowing the composition to react with fructose.

SYNTHESIS OF D-ALLULOSE

The invention relates to a process for the synthesis of a product saccharide, preferably of D-allulose from an educt saccharide, preferably from D-fructose under heterogeneous or homogeneous catalysis which includes chemical and/or enzymatic catalysis. The synthesis is performed in at least two reactors that are arranged in series and the reaction product exiting the first reactor is subjected to chromatographic separation before it enters the second reactor. Preferably, the chromatographic separation is integrated in a simulated moving bed. 1: A process for the synthesis of product saccharide in at least two reactors Rand R , the method comprising the steps of{'sub': '1', '(i) supplying a liquid comprising educt saccharide to the reactor Rand converting a portion of the educt saccharide to product saccharide under enzymatic catalysis thereby providing a liquid comprising product saccharide and residual educt saccharide;'} a first chromatographic fraction comprising residual educt saccharide and optionally product saccharide; and', 'a second chromatographic fraction comprising product saccharide and optionally residual educt saccharide; and, '(ii) separating at least a portion of the product saccharide from the residual educt saccharide of step (i) by liquid chromatography thereby providing'}{'sub': '2', '(iii) supplying the first chromatographic fraction of step (ii) to the reactor Rand converting at least a portion of the residual educt saccharide to product saccharide under enzymatic catalysis.'}24-. (canceled)5: The process according to claim 1 , wherein(i) the educt saccharide is glucose, the product saccharide is fructose, and the conversions according to step (i) and/or step (iii) are performed under enzymatic catalysis by glucose-fructose-epimerase; or(ii) the educt saccharide is fructose, the product saccharide is tagatose, and the conversions according to step (i) and/or step (iii) are performed under enzymatic catalysis by tagatose-3-epimerase; or(iii) ...

Genetically Modified Yeast Species, and Fermentation Processes Using Genetically Modified Yeast

Yeast cells are transformed with an exogenous xylose isomerase gene. Additional genetic modifications enhance the ability of the transformed cells to ferment xylose to ethanol or other desired fermentation products. Those modifications include deletion of non-specific or specific aldose reductase gene(s), deletion of xylitol dehydrogenase gene(s) and/or overexpression of xylulokinase. 145-. (canceled)46. A fermentation process in which a genetically modified yeast cell having a genome and a functional , exogenous xylose isomerase gene which encodes a xylose isomerase enzyme that is at least 90% homologous to SEQ. ID. NO. 59 , wherein the exogenous xylose isomerase gene is operatively linked to promoter and terminator sequences that are functional in the yeast cell , and the modified yeast cell further has a deletion or disruption of a native gene that produces an enzyme that catalyzes the conversion of xylose to xylitol is cultured under fermentation conditions in a fermentation broth that includes a pentose sugar , wherein the fermentation process includes a growth phase and a production phase , and during the production phase the concentration of cells in the fermentation broth is in the range of 3 to 10 g dry cells/liter of fermentation broth.47. A fermentation process of wherein ethanol is produced as a major fermentation product.48. A fermentation process of wherein lactate is produced as a major fermentation product.49. The fermentation process of in which the pentose sugar includes xylose.50. The fermentation process of in which the fermentation broth further includes a hexose sugar.51. The fermentation process of which is an anaerobic fermentation.52108-. (canceled)109. The fermentation process of wherein the final concentration of the fermentation product is at least 14 g/L. This application claims benefit of U.S. Provisional Application No. 60/467,727, filed May 2, 2003.This invention was made under contract no. DE-FC07-021D14349 with the United States ...

Method of Production of Monosaccharides

The present invention is directed towards genetic modification of native gene encoding for D-tagatose 3-epimerase and rhamnose isomerase to substantially increase the expression level of these enzymes and use of said enzymes in a process to produce rare monosaccharides such as psicose and allose. Also disclosed in the present invention is expression constructs comprising the modified genes and a host cells to express the same.

Method for Producing Heparosan Compound Having Isomerized Hexuronic Acid Residue

The present invention provides a method for producing a heparosan compound having an isomerized hexuronic acid residue and a method for producing a heparan sulfate with improved C5-epimerization efficiency. Specifically, the present invention provides a method for producing a heparosan compound having an isomerized hexuronic acid residue, said method comprising producing the heparosan compound having the isomerized hexuronic acid residue from a heparosan compound in the presence of a protein selected from the group of consisting of the following (A) to (F): (A) a protein comprising the amino acid sequence of SEQ ID No:2; (B) a protein which comprises an amino acid sequence having 90% or more homology to the amino acid sequence of SEQ ID No:2 and has a D-glucuronyl C5-epimerase substituted, added or inserted amino acid residues in the amino acid sequence of SEQ ID No:2 and has a D-glucuronyl C5-epimerase activity; (D) a protein comprising the amino acid sequence of SEQ ID NO:5; (E) a protein which comprises an amino acid sequence having 90% or more homology to the amino acid sequence of SEQ ID No:5 and has a D-glucuronyl C5-epimerase activity; and (F) a protein which comprises an amino acid sequence having one or several deleted, substituted, added or inserted amino acid residues in the amino acid sequence of SEQ ID No:5 and has a D-glucuronyl C5-epimerase activity. 1. A method for producing a heparosan compound having an isomerized hexuronic acid residue , said method comprising producing the heparosan compound having the isomerized hexuronic acid residue from a heparosan compound in the presence of a protein selected from the group of consisting of:(A) a protein comprising the amino acid sequence of SEQ ID No:2;(B) a protein which comprises an amino acid sequence having 80% or more homology to the amino acid sequence of SEQ ID No:2 and has a D-glucuronyl C5-epimerase activity;(C) a protein which comprises an amino acid sequence having one or several deleted, ...

KETOSE 3-EPIMERASE WITH IMPROVED THERMAL STABILITY

It is found that a variant enzyme with an improved thermal stability can be obtained by substituting a specific amino acid in the amino acid sequence of a ketose 3-epimerase originated from and that D-psicose can be efficiently produced. 110-. (canceled)12. The variant of ketose 3-epimerase according to claim 11 , which is immobilized on an immobilization carrier.13. A method for preparing a D-ketose comprising:{'claim-ref': {'@idref': 'CLM-00011', 'claim 11'}, 'treating D-fructose with the variant of ketose 3-epimerase according to .'} This application is a National Stage of International Application No. PCT/JP2019/002340 filed Jan. 24, 2019, claiming priority based on Japanese Patent Application No. 2018-009389 filed Jan. 24, 2018.The present invention relates to a novel ketose 3-epimerase with an improved thermal stability and a method for producing the same.D-psicose is known as one of rare sugars, which exist only in very small quantities in the nature. Since the sweetness of D-psicose is about 70% of that of sugar, D-psicose is utilized as a sweetener. D-psicose has a caloric value almost close to zero, is also known to have various physiological functions, such as suppression of an increase in the blood sugar level, and thus is attracting attention as a food ingredient having functionality. For these reasons, the need for an efficient and safe method for producing D-psicose is increasing in the food industry.On the other hand, since D-psicose is an epimer of D-fructose, production methods that react D-psicose 3-epimerase with D-fructose have been established. For example, ketose 3-epimerase originated from M30 (Patent Literature 1) and D-psicose 3-epimerase originated from (Patent Literature 2) are disclosed. In addition, a psicose epimerase variant originated from (Patent Literature 3) and D-psicose 3-epimerase variant originated from (Patent Literature 4) with improved thermal stability, by which denaturation of enzymes due to a temperature is suppressed to ...

Polypeptides having D-Psicose 3 Epimerase Activity and Polynucleotides Encoding Same

The present invention relates to isolated polypeptides having D-psicose 3-epimerase activity and polynucleotides encoding the polypeptides. The invention also relates to nucleic acid constructs, vectors, and host cells comprising the polynucleotides as well as methods of producing and using the polypeptides. 1. An isolated polypeptide having D-psicose 3-epimerase activity , selected from the group consisting of:(a) a polypeptide having at least 70% sequence identity to the polypeptide of SEQ ID NO: 2 or SEQ ID NO: 4;(b) a polypeptide encoded by a polynucleotide that hybridizes under very high stringency conditions with (i) the polypeptide coding sequence of SEQ ID NO: 1 or SEQ ID NO: 3, or (ii) the full-length complement thereof;(c) a polypeptide encoded by a polynucleotide having at least 70% sequence identity to the polypeptide coding sequence of SEQ ID NO: 1 or SEQ ID NO: 3;(d) a variant of the polypeptide of SEQ ID NO: 2 or SEQ ID NO: 4 comprising a substitution, deletion, and/or insertion at one or more positions; and(e) a fragment of the polypeptide of (a), (b), (c), or (d) that has D-psicose 3-epimerase activity.29-. (canceled)10. An isolated polynucleotide encoding the polypeptide of .11. A nucleic acid construct or expression vector comprising the polynucleotide of operably linked to one or more control sequences that direct the production of the polypeptide in an expression host.12. A recombinant host cell comprising the polynucleotide of operably linked to one or more control sequences that direct the production of the polypeptide.1314-. (canceled)15. A method of producing a polypeptide having D-psicose 3-epimerase activity claim 12 , comprising cultivating the recombinant host cell of under conditions conducive for production of the polypeptide.16. The method of claim 15 , further comprising recovering the polypeptide.1719-. (canceled)20. A method for producing D-psicose claim 15 , the method comprising:{'claim-ref': {'@idref': 'CLM-00001', 'claim 1'}, ...

YEAST CELL CAPABLE OF SIMULTANEOUSLY FERMENTING HEXOSE AND PENTOSE SUGARS

A method for preparing a yeast capable of simultaneously fermenting a pentose and a hexose sugar, comprising: (a) providing a yeast comprising: one or more heterologous genes encoding an enzyme of a pentose metabolic pathway; disruptions of a gene encoding a ribulose-phosphate 3-epimerase and of a gene encoding a glucose-6-phosphate isomerase; one or more overexpressed endogenous genes encoding an enzyme of the pentose phosphate pathway; and a disruption of one or more genes encoding an NADPH dependent 6-phosphogluconate dehydrogenase, (b) subjecting said yeast to evolutionary engineering on a medium comprising a hexose sugar and at least one pentose sugar, selecting for a yeast with improved growth rate obtain an evolved yeast; (d) restoring, in the evolved yeast, one or more of the disrupted genes, or: (d′) identifying genetic permutations in at least part of the genome of the evolved yeast by genome sequencing; (e) constructing an improved pentose and hexose-fermenting yeast comprising one or more said genetic permutations. Also described is a recombinant yeast comprising one or more heterologous genes of a pentose metabolic pathway, and a gene encoding a variant of a parent polypeptide, the variant comprising an amino acid sequence comprising at least one mutation, when aligned with the amino acid sequence in SEQ ID NO: 6. 1. A method for preparing a yeast which is capable of simultaneously fermenting a pentose and a hexose sugar , said method comprising: one or more heterologous genes encoding an enzyme of a pentose metabolic pathway;', 'a disruption of a gene encoding a ribulose-phosphate 3-epimerase and a disruption of a gene encoding a glucose-6-phosphate isomerase; and', 'one or more overexpressed endogenous genes encoding an enzyme of the pentose phosphate pathway; and optionally:', 'a heterologous gene encoding an NADH-dependent 6-phosphogluconate dehydrogenase; and', 'a disruption of one or more genes encoding an NADPH dependent 6-phosphogluconate ...

ENZYMATIC PRODUCTION OF D-ALLULOSE

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 ...

Microbial fermentation method for production of n-acetyl-d-glucosamine and/or d-glucosamine salt

This Invention discloses a method for production of N-Acetyl-D-Glucosamine and/or D-Glucosamine Salt by microbial fermentation. The method is intended to manufacture N-Acetyl-D-Glucosamine and/or D-Glucosamine Salt in higher efficiency and higher yield, by expression of vitreoscilla hemoglobin in microorganism.

METHOD FOR PRODUCING N-ACETYL-D-GLUCOSAMINE AND/OR D-GLUCOSAMINE SALT BY MICROBIAL FERMENTATION

The present invention discloses a process for producing N-acetyl-D-glucosamine and D-glucosamine salts by microbial fermentation. The invention includes a method to produce N-acetyl-D-glucosamine and/or D-glucosamine salts with higher efficiency and higher yield by increasing the effect of N-acetyl-D-aminomannose-6-phosphate epimerase in microorganisms. 1. A method for producing N-Acetyl-D-Glucosamine and/or D-Glucosamine salt by microbial fermentation , comprising:A) culturing a microorganism in a fermentation medium, wherein said microorganism comprises at least one genetic modification that increases the activity of N-acetyl-D-aminomannose-6-phosphate epimerase (NanE) in said microorganism; andB) collecting N-Acetyl-D-Glucosamine produced in the culturing step A).2. The method of claim 1 , wherein said genetic modification that increases the activity of N-acetyl-D-aminomannose-6-phosphate epimerase (NanE) is selected from: a) increased enzymatic activity of N-acetyl-D-aminomannose-6-phosphate epimerase (NanE) in said microorganism; and/or b) N-acetyl-D-aminomannose-6-phosphate epimerase (NanE) is overexpressed in said microorganism.3. The method of claim 2 , wherein said microorganism is transformed with at least one recombinant nucleic acid molecule comprising a nucleic acid sequence encoding N-acetyl-D-aminomannose-6-phosphate epimerase (NanE); said nucleic acid sequence encoding N-acetyl-D-aminomannose-6-phosphate epimerase (NanE) comprises at least one genetic modification that increases the activity of N-acetyl-D-aminomannose-6-phosphate epimerase (NanE).4. The method of claim 2 , said genetic modification comprises one or two of substitutions at positions corresponding to the amino acid sequence of SEQ ID NO.: 17: the 133th cysteine is substituted with arginine and the 187th tyrosine is substituted with histidine.5. The method of claim 3 , said nucleic acid sequence encoding N-acetyl-D-aminomannose-6-phosphate epimerase (NanE) is SEQ ID NO.: 26.6. The ...

Genetically modified yeast species and fermenation processes using genetically modified yeast

Yeast cells are transformed with an exogenous xylose isomerase gene. Additional genetic modifications enhance the ability of the transformed cells to ferment xylose to ethanol or other desired fermentation products. Those modifications', include deletion of non-specific or specific aldose reductase gene(s), deletion of xylitol dehydrogenase gene(s) and/or overexpression of xylulokinase.

制备2-表-5-表有效醇酮的方法

一种制备2‑表‑5‑表有效醇酮的方法，设计并实现了一种新的2‑表‑5‑表有效醇酮合成途径、即在体外利用重组表达纯化得到的转醛酶、转酮酶、5‑磷酸核酮糖‑3‑差向异构酶、5‑磷酸核糖异构酶及2‑表‑5‑表有效醇酮合成酶，将底物6‑磷酸果糖与β‑羟基丙酮酸催化合成2‑表‑5‑表有效醇酮。本发明为构建以生物质为原料的体外合成途径产氨基环醇类物质的前体提供了新的思路。

사이코스 에피머화 효소 및 이를 이용한 사이코스로 전환용 조성물

본 발명에 따른 D-사이코스 3-에피머화 효소는 과당의 3번째 탄소 위치를 에피머화하여 사이코스를 생산하는 탁월한 활성을 보유한 효소로써, 이 효소의 산업적으로 유용한 넓은 범위의 pH, 높은 온도에서의 안정성을 특징으로 산업화에 적용한다면 경제성이 높은 사이코스의 대량생산이 가능하며, 기능성 당산업뿐만 아니라 이를 이용한 건강식품소재, 의약용, 화장품용 소재 등 유용하게 사용될 수 있다.

알룰로스 에피머화 효소 변이체, 이의 제조방법 및 이를 이용한 알룰로스의 제조방법

본 발명은 플라보니프랙터 플라우티( Flavonifractor plautii )에서 유래한 야생형 D-알룰로스 3-에피머화 효소의 아미노산 서열 중 특정 위치에 존재하는 아미노산 잔기가 다른 아미노산 잔기로 치환된 신규 알룰로스 에피머화 효소 변이체 및 이의 다양한 용도를 제공한다. 본 발명에 따른 신규 알룰로스 에피머화 효소 변이체는 플라보니프랙터 플라우티( Flavonifractor plautii )에서 유래한 야생형 D-알룰로스 3-에피머화 효소에 비해 과당의 알룰로스로의 전환 활성이 높고, 특히 60℃ 이상의 고온 조건에서 열 안정성이 매우 우수하기 때문에 알룰로스의 대량 생산을 위한 산업화 수준의 효소 전환 반응시 오염을 방지할 수 있고 생산 시간을 단축시킬 수 있으며 생산 비용을 절감시킬 수 있다.

Production for functional sweetener

본 발명은 기능성 감미료 생산용 효소 및 이를 이용한 기능성 감미료를 생산하는 방법에 관한 것이다. The present invention relates to an enzyme for producing a functional sweetener and a method for producing a functional sweetener using the same.

一株枯草芽孢杆菌及其培养方法与应用

本发明涉及一株枯草芽孢杆菌及其培养方法与应用。枯草芽孢杆菌(Bacillus subtilis)BLCY‑005，2016年10月26日保存于中国微生物菌种保藏管理委员会普通微生物中心，保藏号CGMCC No.13152。本发明还涉及该枯草芽孢杆菌的培养方法与应用。本发明首次获得的高产D‑阿洛酮糖差向异构酶的枯草芽孢杆菌BLCY‑005，其发酵液中的D‑阿洛酮糖差向异构酶酶活可达到143U/ml，较传统D‑阿洛酮糖差向异构酶活提高50％以上，显著降低生产成本，最适pH值为5.5～6.5，与传统菌株产D‑阿洛酮糖差向异构酶最适pH偏中性相比，有利于生产中对污染的控制。

Expression system for psicose epimerase and production for psicose using the same

본 발명은 사이코스 에퍼머화 효소를 높은 안정성과 발현율로 생산할 수 있는 유전자 발현 시스템, 이를 이용한 GRAS(Generally recognized as safe) 미생물, 상기 GRAS 미생물 또는 상기 미생물로부터 얻어진 효소를 이용한 사이코스 생산방법에 관한 것이다. The present invention relates to a gene expression system capable of producing a perming enzyme at high stability and expression rate in psicose, a generically recognized as safe microorganism using the same, and a method for producing psicos using an enzyme obtained from the microorganism or the GRAS will be.

D-psicose 3-epimerase variants and production method of D-psicose using them

본 발명은 열 안정성이 향상된 아그로박테리움 투메파시엔스 ( Agrobacterium tumefaciens ) 유래의 사이코스 에피머화 효소 변이체, 상기 변이체를 코딩하는 유전자를 포함하는 재조합 벡터 및 상기 변이체를 포함하는 미생물에 관한 것이다. 또한 상기 효소 변이체, 또는 상기 미생물을 이용하여 사이코스를 제조하는 방법에 관한 것이다.

Genetically modified yeast species and fermentation processes using genetically modified yeast

Yeast cells are transformed with an exogenous xylose isomerase gene. Additional genetic modifications enhance the ability of the transformed cells to ferment xylose to ethanol or other desired fermentation products. Those modifications', include deletion of non-specific or specific aldose reductase gene(s), deletion of xylitol dehydrogenase gene(s) and/or overexpression of xylulokinase.