13 results about "Transketolase" patented technology

The invention discloses saccharomyces cerevisiae with high yield of salidroside as well as a construction method and application of the saccharomyces cerevisiae. According to the recombinant saccharomyces cerevisiae, ribulose-5-phosphate isomerase RKI1 and transketolase TKL1 are expressed in host bacteria, so that precursor supply is increased; reverse methyltransferase ARO2 and phenylalanine decarboxylase ARO10 are expressed at the same time, and a tyrosine branch pathway is adjusted; then, UDP-glycosyl transferase of different sources is expressed, and iterative site-specific mutagenesis is carried out on the UDP-glycosyl transferase to enhance conversion of hydroxytyrosol to salidroside; the salidroside production performance of the recombinant strain is verified on the basis of a precursor supply pathway, a tyrosine regulation pathway and key enzyme screening, and the salidroside production capacity of the saccharomyces cerevisiae is further improved.

Disclosed herein are genetically engineered yeast cells capable of producing xylitol and characterized by a deletion or disruption of a native gene encoding a glycerol-3-phosphate dehydrogenase 2a enzyme at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99%, or 100% identical to SEQ ID NO:107. The genetically engineered yeast cell may additionally overexpress a native glycerol kinase enzyme, express a transketolase enzyme, have a deletion or disruption of a native gene encoding an erythrose reductase, be engineered to overexpress a native RPE enzyme, express an exogenous XPDH enzyme, express an exogenous XKS enzyme, express an exogenous XDH enzyme, overexpress a native X5PP enzyme, and / or express an exogenous X5PP enzyme.

The present invention relates to the technical fields of biocatalysis and biopharmaceuticals. Disclosed is an aldehyde / ketone-initiated enzymatic synthesis method for (1R,2R)-p-methylsulfonylphenylserinol. In the method provided in the present invention, using transaminase and transketolase as catalysts, in the presence of an amino donor and an aldehyde compound or a ketone compound, a substrate p-methylsulfonylbenzaldehyde is catalyzed to produce (1R,2R)-p-methylsulfonylphenylserinol. The method provided in the present invention reduces operation steps and can realize the replacement and recycling of expensive non-industrial starting material hydroxypyruvic acid, thereby reducing production costs and thus being suitable for industrial production.

The invention discloses transketolase, transaminase and a method for preparing (1R, 2R)-1, 3-dihydroxy-2-amino-1-p-methylsulfonyl phenylpropane.The amino acid sequence of the transketolase is shown as SEQ ID NO: 6, the amino acid sequence of the transaminase is shown as SEQ ID NO: 10, the conversion rate of the transketolase used for preparing the (1R, 2R)-1, 3-dihydroxy-2-amino-1-p-methylsulfonyl phenylpropane is 99.9%, and the conversion rate of the transaminase used for preparing the (1R, 2R)-1, 3-dihydroxy-2-amino-1-p-methylsulfonyl phenylpropane is 99.9%. The method has the advantages that the de value is 97.0%, the ee value is 99.5%, the reaction cost is low, the product has high optical purity, the mode of sequentially adding enzymes along with the reaction process in a one-pot method system is adopted, the reaction system does not need to be prepared repeatedly, the operation steps are simplified, and therefore the method is beneficial to reduction of by-products and suitable for industrial production.

Disclosed herein are genetically engineered yeast cells capable of producing xylitol and characterized by overexpression of a native glycerol kinase enzyme and overexpression of a native transketolase enzyme. The genetically engineered yeast cell may additionally have a deletion or disruption of a native gene encoding an erythrose reductase and may be engineered to overexpress a native RPE enzyme, express an exogenous XPDH enzyme, express an exogenous XKS enzyme, express an exogenous XDH enzyme, overexpress a native X5PP enzyme, and / or express an exogenous X5PP enzyme.

The invention discloses recombinant escherichia coli, a construction method thereof and application of the recombinant escherichia coli in production of 3-dehydroshikimic acid, and belongs to the technical field of bioengineering. According to the recombinant escherichia coli, escherichia coli FMME-DHS03 is used as an original strain, pyruvate kinase gene pykA is knocked out, excessive 3-dehydroquinic acid synthase gene aroB, transketolase gene tktA and galactose permease gene galP are added, the finally obtained recombinant strain is fermented for 40 h, the yield of 3-dehydroshikimic acid reaches 130.9 g / L, and the yield of glucose reaches 0.55 g / g. The process for producing the 3-dehydroshikimic acid through fermentation is simple and easy to operate, free of additional antibiotics, short in period, high in yield, low in culture medium cost and suitable for industrial production.

Provided are a Corynebacterium glutamicum variant with improved L-lysine producing ability and a method of producing L-lysine using the same. The variant increases or enhances the expression of a gene encoding transketolase, thereby improving a production yield of L-lysine, as compared to a parent strain.

The present invention relates to a biocatalytic process for the production of aroma chemicals by carboligation using a transketolase (EC 2.2.1.1) as shown for transketolase from Geobacillus stearothermophilus and several sequence variants to catalyse the conversion of a donor molecule selected from 2-oxobutanoic acid and 3-methyl-2-oxopentanoic acid and an acceptor molecule selected from propanal and 2-methylbutanal, two identical or different donor molecules, or two identical or different acceptor molecules, thereby obtaining a coupling product in the presence of coenzyme thiamine diphosphate, the products being 3-hydroxy-5-methyl-heptan-4-one, 4-hydroxy-5-methyl-heptan-3-one, 5-hydroxy-3,6-dimethyl-octan-4-one and 4-hydroxy-hexan-3-one as precursor for filbertone.

This invention discloses a self-initiated one-pot enzymatic synthesis method for (1R,2R)-p-methylsulfonylbenzylserine, specifically a D-serine-driven self-initiated one-pot enzymatic synthesis method for (1R,2R)-p-methylsulfonylbenzylserine, belonging to the fields of biocatalysis and biopharmaceutical technology. The method provided by this invention utilizes engineered transaminases and transketolases as catalysts, using D-serine as an amino donor to catalyze the reaction with p-methylsulfonylbenzaldehyde to produce hydroxypyruvate as an initiator, achieving efficient conversion of p-methylsulfonylbenzaldehyde to (1R,2R)-p-methylsulfonylbenzylserine. The method provided by this invention utilizes D-serine to generate hydroxypyruvate in situ and achieves the recycling of hydroxypyruvate, eliminating the need for the additional addition of expensive hydroxypyruvate (HPA) and the exogenous cofactor thiamine pyrophosphate (TPP), saving production costs and making it suitable for industrial production.

The application discloses a Yarrowia lipolytica gene engineering bacterium for producing erythritol by glycerol, and the Yarrowia lipolytica gene engineering bacterium is obtained by random insertion mutation mediated by non-homologous end connection, and strains with high cell growth and high erythritol yield are screened. Further, the gene engineering bacterium overexpresses glycerol dehydrogenase gene GCY3 or ARA1 and dihydroxyacetone kinase gene DAK2 of a glycerol metabolism dihydroxyacetone pathway. Further, the gene engineering bacterium overexpresses transketolase gene TKL1 and transaldolase gene TAL1 of a non-oxidative pentose phosphate pathway. The application further discloses a construction method and application of the gene engineering bacterium. The superior gene engineering bacterium obtained by constructing a mutant library has the characteristics of tolerating high-concentration glycerol, and the substrate conversion rate and glycerol utilization rate are significantly higher than those of a starting strain.

The invention relates to a construction method, a production method and application of a genetically engineered bacterium for synthesizing Gadusol, the genetically engineered bacterium for synthesizing Gadusol is obtained by taking escherichia coli MG1655 as an initial strain, knocking out a ketoaldolase gene on an escherichia coli MG1655 genome and cooperatively expressing an exogenous EEVS gene and an exogenous MT-Ox gene. According to the invention, an EEVS gene and a DrMT-Ox gene are integrated to a specific gene locus of an escherichia coli chromosome in a multi-copy form, and a key enzyme gene of a phosphate pentose pathway (PPP) is integrated and overexpressed on the chromosome, so that efficient biosynthesis of Gadusol is realized in escherichia coli for the first time; the method does not need exogenous plasmids, does not depend on inducers and antibiotics, can efficiently utilize a cheap carbon source, and realizes high-yield, stable and green production of Gadusol.

The present invention relates to a biocatalytic process for the production of aroma chemicals. More particularly, the process comprises a transaldolase or transketolase catalyzed conversion of a donor molecule and an acceptor molecule, two identical or different donor molecules, or two identical or different acceptor molecules, thereby obtaining a coupling product. The present invention also provides an aroma composition comprising said coupling product. The present invention further relates to a product supplemented with said coupling product. The present invention further relates to the use of said coupling product as an aroma chemical.

Disclosed herein are genetically engineered yeast cells capable of producing xylitol and characterized by a deletion or disruption of a native gene encoding an erythritol reductase that is at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99%, or 100% identical to at least one of SEQ ID NO: 292 and 295. The genetically engineered yeast cell may additionally be engineered to overexpress a native RPE enzyme, express an exogenous XPDH enzyme, express an exogenous XKS enzyme, express an exogenous XDH enzyme, overexpress a native X5PP enzyme, and / or express an exogenous X5PP enzyme.