11 results about "Transaldolase" patented technology

The present invention discloses a method for synthesizing hydroxytyrosol by multi-enzyme cascade, comprising: 1) preparing a hydroxytyrosol product by using 3,4-dihydroxybenzaldehyde, L-threonine, sodium formate, NAD + As raw material, L-threonine transaldolase, alcohol dehydrogenase, and formate dehydrogenase are used to catalyze the synthesis of L-threo-3-(3,4-dihydroxyphenyl)serine; 2) L-threo-3-(3,4-dihydroxyphenyl)serine is used as substrate, glucose, NAD + Hydroxytyrosol is synthesized through a cascade catalysis of phenylserine dehydratase, α-ketoacid decarboxylase, aldehyde reductase, and glucose dehydrogenase. The synthesis method provided by the present invention achieves a hydroxytyrosol yield of >99% and a space-time yield of 0.88 g / L / h, currently the highest, showing great potential for industrial application and suitable for further promotion and application.

The invention provides a one-step enzymatic synthesis technology of (2S, 3R)-p-methylsulfonyl phenyl serine ethyl ester. Specifically, the invention provides a method for preparing (2S, 3R)-p-methylsulfonyl phenyl serine ethyl ester by a one-step method, and the method comprises the step of obtaining (2S, 3R)-p-methylsulfonyl phenyl serine ethyl ester from p-methylsulfonyl benzaldehyde and L-threonine ethyl ester or a salt thereof under the action of transaldolase in the presence of phosphopyridoxal as a coenzyme.

A method to make tertiary β-hydroxy α-amino acids. The method includes reacting a ketone substrate and a primary or secondary β-hydroxy α-amino acid with an L-threonine aldolase and / or an L-threonine transaldolase for a time, at a temperature, and at a pH wherein the reaction yields a tertiary β-hydroxy α-amino acid product.

The present invention relates to a recombinant microorganism for producing 1,3-propanediol and a method for producing 1,3-propanediol using same. More specifically, the present invention provides a recombinant microorganism having an improved ability to produce 1,3-propanediol through overexpression of a transaldolase-encoding gene (tal), a succinyl-CoA synthetase-encoding gene (sucCD), a cystathionine γ-synthase-encoding gene (metB), an aspartate ammonia lyase-encoding gene(aspA), an aspartate aminotransferase-encoding gene (aspB), or a functional fragment thereof, and a method for producing 1,3-propanediol using same.

The present invention relates to a genetically engineered erythritol strain and a construction method thereof, as well as application of the strain in preparing erythritol by microbial fermentation. The present invention introduces xylose reductase, xylitol dehydrogenase and xylitol kinase into Yarrowia lipolytica to reshape the xylose metabolic pathway, strengthens the expression of transketolase TKL1, transaldolase TAL and erythrose reductase ER in the erythritol bioproduction pathway, reduces the production of byproducts mannitol and arabitol by knocking out mannitol dehydrogenase MDH and arabitol dehydrogenase ArDH, reduces the conversion of erythritol into other substances by knocking out erythritol dehydrogenase EYD, weakens the accumulation of erythritol, strengthens the expression of sugar uptake pathway genes hexokinase HK and transporters Stp1 and Stp2, and finally produces a high-yield erythritol bacterium that can utilize a mixed carbon source of glucose and xylose, with the yield increased from 50.17 g / L to 195.56 g / L. This provides an excellent strain source for the industrial production of erythritol synthesized using xylose as a substrate, and has great industrial application potential.

The present invention belongs to the field of biomedicine, and in particular to a kind of L-threonine transaldolase mutant and its application in the synthesis of chloramphenicol chiral intermediate.The present invention is with 4-nitrobenzaldehyde, L-threonine and sodium formate as substrates, using the co-expression cells of L-threonine transaldolase mutant PmLTTA-Mu4, alcohol dehydrogenase and formate dehydrogenase or its broken liquid as catalyst, under mild conditions (25-35 DEG C, pH6.5-7.5) asymmetric synthesis (2S, 3R)-4-nitrophenylserine.The method can completely convert 5% 4-nitrobenzaldehyde into (2S, 3R)-4-nitrophenylserine in 5h, and space-time yield is up to 15g / L / h, which is the highest level of current (2S, 3R)-4-nitrophenylserine biological synthesis. This synthesis method has mild conditions, simple operation, simple control, a single product configuration, no substrate residue, and a total yield of up to 85%. It has the advantages of high time-space yield, easy purification, and green environmental protection.

The invention relates to recombinant escherichia coli with high yield of gadusol and application of the recombinant escherichia coli, and belongs to the technical field of genetic engineering. The method comprises the following steps: firstly, expressing gadusol synthetic pathway related enzymes, namely EEVS and MT-OX, in escherichia coli, and secondly, systematically modifying a metabolic pathway, namely enhancing the expression of glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase and transketolase 1, and knocking out 6-phosphofructokinase, transaldolase genes and phosphoglycerate kinase genes at the same time. In addition, an efficient circulating system of cofactors SAM and NAD + is also constructed, and 4.2 g / L gadusol is synthesized by recombinant escherichia coli in a 5-L fermentation tank amplification system and is far higher than the highest yield in the prior art. According to the invention, efficient production of the gadusol is realized through engineering transformation of escherichia coli, and a foundation is laid for industrial preparation of the gadusol.

The invention discloses transaldolase and application thereof in preparation of a chloramphenicol intermediate. Compared with the amino acid sequence shown in SEQ ID NO: 1, the transaldolase contains amino acid residue difference at C57 and / or F59 sites, wherein the 57 and 59 positions refer to the amino acid residue number in SEQ ID NO: 1. The transaldolase disclosed by the invention is utilized to catalyze and generate a target product (2S, 3R)-p-nitrobenzene serine by taking p-nitrobenzaldehyde and L-threonine as substrates, the substrate conversion rate is relatively high, and the target product has relatively high stereoselectivity.

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 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.

The present invention relates to a recombinant cell. The recombinant cell may express a first enzyme, a second enzyme and a third enzyme and produce a nonstandard amino acid (nsAA). The first enzyme may be a L-threonine transaldolase (L-TTA) or a threonine aldolase (TAs). The second enzyme may be a phenylserine dehydratase or a threonine deaminase (TD). The third enzyme may be an aminotransferase (AT), a L-amino acid dehydrogenase (L-AADH) or a D-amino acid aminotransferase. At least one of the first enzyme, the second enzyme and the third enzyme may be heterologous to the recombinant cell. Also provided are a method for producing a nonstandard amino acid (nsAA) by the recombinant cell and a method for producing a nsAA in a container in the presence of the first enzyme, the second enzyme and the third enzyme.