18 results about "Aldehyde Reductase" patented technology

The invention relates to a method for increasing the yield of L-malic acid produced by fermentation by adding ethylene glycol, which comprises the following steps: constructing genetic engineering escherichia coli, and introducing ethylene glycol metabolism genes (overexpression) including glycerol dehydrogenase, lactaldehyde reductase, lactaldehyde dehydrogenase and the like; and overexpression of other genes involving malic acid production, such as malic acid synthase, phosphoenolpyruvate carboxylase and malic acid export protein. The gene engineering strain is an E.coli BW25113 strain of which ldhA, pta, poxB, adhE, pflB, mgsA, frdA, maeA, maeB, yqhD, ycdW and iclR genes are substantially inactivated, and the deleted genes are beneficial to reducing the generation of metabolic byproducts and increasing the accumulation of malic acid. The genetic engineering strain is subjected to fermentation culture by taking glucose and ethylene glycol as carbon sources, and L-malic acid is separated from a culture after culture is finished.

The invention discloses an aldehyde reductase mutant and application thereof in synthesis of a dexmethylphenidate hydrochloride intermediate, and belongs to the field of molecular biology and enzyme engineering. The aldehyde reductase mutant, polynucleotide for coding the mutant, and the recombinant expression vector can express the aldehyde reductase mutant and are used for constructing a recombinant cell or a recombinant strain for expressing the aldehyde reductase mutant. The provided aldehyde reductase mutant can catalyze 2-phenyl-2-((R)-piperidine-2)-acetaldehyde into (R)-2-phenyl-2-((R)-piperidine-2)-1-ethanol, especially improves the stereoselectivity of (R)-2-phenyl-2-((R)-piperidine-2)-1-ethanol, solves the problems of strict conditions, complex reaction and high cost in the existing synthesis method, and has a wide application prospect in the field of synthesis of (R)-2-phenyl-2-((R)-piperidine-2)-1-ethanol. Wide application prospects are realized.

To provide a method for producing 6-hydroxyhexanoic acid (6-HHA) with increased production efficiency through a bioprocess.SOLUTION: A method for producing 6-hydroxyhexanoic acid comprises culturing a bacterium belonging to the genus Shewanella in a medium containing adipic acid under metabolically controlled conditions, where the bacterium has a carboxylic acid reductase and an aldehyde reductase.SELECTED DRAWING: None

The present invention discloses a carboxyl-substituted quinoxalinone derivative and a preparation method and application thereof, and belongs to the technical field of synthetic drugs. The present invention provides a novel compound having a strong specific inhibitory ability against aldose reductase. By extracting aldose reductase from rat lens and conducting an activity assay experiment on the inhibitory activity of the compound, it is proved that the compound of the present invention has significant AKR1B1 inhibitory activity; by extracting aldehyde reductase from rat kidney and conducting an activity assay experiment on the inhibitory activity of the compound, the inhibitory selectivity of aldose reductase is evaluated, and it is proved that the compound of the present invention has high safety, can reduce toxic side effects, and achieve the effect of treating diabetic complications.

The present application relates to the technical field of genetic engineering, and discloses a recombinant Escherichia coli for high-yield O-acetyl-L-homoserine and application thereof. The recombinant Escherichia coli for high-yield O-acetyl-L-homoserine is obtained by the following combination of modification strategies: in Escherichia coli W3110, a gene encoding homoserine O-acetyltransferase is integrated into a gene site encoding L-arginine ABC transporter ATP binding subunit, then a gene encoding phosphoacetyltransferase is knocked out, then a gene encoding transcriptional anti-terminator and mRNA stability regulator is knocked out, then a gene encoding ATP-NAD kinase is integrated into a gene site encoding NADPH-dependent aldehyde reductase, and finally a gene promoter of acetyl-CoA synthetase is replaced by a Ptrc promoter to obtain the recombinant Escherichia coli. The recombinant Escherichia coli is used for fermentation to produce O-acetyl-L-homoserine, and has the advantage of high yield. metx artp patz cspc ppnk yahk acs ​​​​​​​

A method for biosynthesis of polymer precursors, including, adipic acid, 1,6-hexanediol, 6-hydroxyhexanoic and 6-aminocaproic acids from carboxylic acids is provided. A method for biosynthesis of adipic acid from six-carbon dicarboxylic acids having α, β-enoate reductase activity by treatment with an enzyme is provided. The biocatalytic conversion of aliphatic and hydroxycarboxylic acids to corresponding aldehydes, alcohols, and amines using novel carboxylate reductases, aldehyde reductases, and aminotransferases is described. Also provided are genetically engineered microorganisms for use in the biosynthetic processes.

The invention discloses a strain for preparing glycollic acid through whole-cell catalysis of ethylene glycol and a construction method and application of the strain, escherichia coli serves as host bacteria, propylene glycol oxidoreductase fucO mutant fucOI6L, L7V genes, acetaldehyde dehydrogenase aldA genes and glycollic aldehyde reductase ycdW genes are over-expressed in the host bacteria to obtain a recombinant strain E.coli GA-02, namely the strain, the E.coli GA-02 can catalyze 400 mM of ethylene glycol to prepare 367.73 mM of glycollic acid, and the E.coli GA-02 can catalyze 400 mM of ethylene glycol to prepare glycollic acid. The yield reaches 91.93%, efficient conversion from ethylene glycol to glycollic acid is realized, and conversion from glycollic acid to a downstream byproduct glyoxylic acid is avoided. The recombinant strain E.coli GA-02 constructed by the invention has important significance in the aspect of high-value conversion of waste carbon resources containing ethylene glycol, such as polyethylene glycol terephthalate (PET) plastic depolymers, and also provides a support technology for efficient preparation of glycollic acid.

The invention provides a recombinant algal strain for expressing glycollate oxidase, catalase, glyoxylate polyaldolase and hydroxymalonate semialdehyde reductase as well as a construction method and application of the recombinant algal strain, and belongs to the technical field of genetic engineering. The invention provides a recombinant microalgae strain, which is a microalgae strain for expressing glycollic acid oxidase, catalase, glyoxylic acid polyaldolase and hydroxymalonic semialdehyde reductase in chloroplast. The recombinant microalgae strain can decompose a light respiration by-product glycollic acid into carbon dioxide, the carbon dioxide concentration of chloroplast is improved, the carbon sequestration efficiency of microalgae is effectively improved, and fixed CO2 can be converted into biomass, pyruvic acid, starch, grease and other metabolites and bioactive substances. The recombinant microalgae strain disclosed by the invention has a wide application prospect in the aspects of biological carbon sequestration, synthesis of microalgae metabolites and preparation of microalgae bioactive substances.

The invention provides a novel reverse aldolase and reductase cascaded Bi-BDO independent synthesis pathway, and relates to the technical field of bioengineering, the pathway constructs a non-natural metabolism module composed of a modified reverse aldolase RA variant, 4-hydroxybutyraldehyde reductase AHR and a coenzyme cyclic regeneration enzyme, the RA variant performs hydrophobic modification on a Lys146 site, and the reverse aldolase and reductase cascaded Bi-BDO is obtained. Aldol condensation of a non-phosphorylated substrate hydroxyacetaldehyde is realized to generate a C4 intermediate, RA and AHR are physically anchored by utilizing an artificially synthesized scaffold protein, toxicity of the intermediate is avoided through a substrate channel effect, the intermediate is instantly reduced into 1, 4-butanediol, engineering bacteria of aldA and gapA genes are knocked out, a precursor is generated by utilizing a xylose way, and the 1, 4-butanediol is obtained. The method has the advantages that the method is simple in operation, the reduction reaction is driven by in-situ regeneration of NADPH by adding formate, finally, the high-purity product is obtained through macroporous adsorption resin enrichment and vacuum rectification, the TCA circulation decarboxylation step is omitted, the carbon conversion rate is close to the theoretical limit, effective decoupling of production and growth is achieved, and the yield and purity of Bi-BDO are remarkably improved.

The present invention discloses an application of a yellow eel aldehyde reductase protein and a preparation method thereof. The amino acid sequence of the yellow eel aldehyde reductase protein is shown in SEQ ID NO.1. The present invention shows for the first time that the yellow eel aldehyde reductase protein has reducing activity on S-nitrosoglutathione (GSNO), and is a new GSNO reductase. Intraperitoneal injection of the yellow eel aldehyde reductase protein into fish can significantly reduce inflammatory reactions and oxidative stress damage induced by pathogens, and therefore has very high application value in the prevention and treatment of fish pathogenic bacterial infections.

The present invention provides a microorganism capable of producing at least one C6-C26 free fatty alcohol or a mixture thereof from methanol, said microorganism comprising at least one gene enabling the expression of a thioesterase (TE), at least one gene enabling the expression of at least one carboxylic acid reductase (CAR) and at least one gene enabling the expression of an aldehyde reductase (ALDR). The present invention further provides methods for the manufacture of C6-C26 free fatty alcohols or mixtures thereof, as well as a free fatty alcohol composition obtained from these methods.

The application provides an engineering bacterium and a cell lysate thereof, and an application of the engineering bacterium in full-cell photocatalytic preparation of 1,3-propanediol, and belongs to the technical field of biotechnology. 12 The engineering bacterium comprises: a non-B 12 dependent glycerol dehydratase, a light-sensitive protein PSP2, a glycerol dehydratase activating enzyme, and an NADPH-dependent aldehyde reductase. The engineering bacterium provided in the application realizes catalysis of glycerol conversion under the condition of not depending on B 12 12, and drives the reductive activation of the glycerol dehydratase activating enzyme by using a light enzyme, so that the synthesis efficiency of 1,3-propanediol is finally improved, and the effect of coenzyme dependence and cost limitation of a traditional process is reduced.

The invention discloses a method for synthesizing raspberry ketone through chemical enzyme stage combination and application, and belongs to the technical field of organic synthesis and biological engineering. The raspberry ketone is obtained through whole-cell catalysis by taking recombinant engineering bacteria of co-expressed olefine aldehyde reductase and formate dehydrogenase genes as a biocatalyst. When the adding amount of a genetic engineering bacterium E.coli BL21 (DE3) pRSF-AtQOR (I56S / A69H / A118N)-LbFDH is 20 g / L, the substrate HBA is 100 g / L, the sodium formate is 125 g / L, the NADP < + > is 0.5 mM, the reaction temperature is 37 DEG C, the pH is 7.5, the reaction time is 12 h, and the rotating speed is 220 rpm, the raspberry ketone concentration can reach 82.23 g / L. The problems of serious environmental pollution of a chemical method and low yield of a biological method are solved.

The present invention belongs to the field of metabolic engineering, and specifically relates to a 1,2-pentanediol biosynthesis method and a recombinant microorganism for producing 1,2-pentanediol. The synthesis method of the present invention includes the following enzymes: threonine dehydratase, α-isopropylmalate synthase, α-isopropylmalate isomerase, β-isopropylmalate dehydrogenase, 2-oxidocarboxylic acid reductase, acyl CoA transferase, acyl CoA reductase, aldehyde reductase, cinnamic acid acylase, etc., and the above-mentioned enzyme gene encoding plasmid is used to obtain a recombinant microorganism, and the recombinant microorganism is fermented and cultured with an organic carbon source such as glucose to obtain high-yield 1,2-pentanediol. The present invention provides a biological method for synthesizing 1,2-pentanediol, and can significantly increase the yield of 1,2-pentanediol, and has broad application prospects.

The invention discloses a recombinant strain NT1003 ycjQ-LS01, a construction method of the recombinant strain NT1003 ycjQ-LS01 and application of the recombinant strain NT1003 ycjQ-LS01 to production of 1, 5-pentanediol. The method comprises the following steps: screening a key enzyme on a path for synthesizing 1, 5-pentanediol, forming a new path by using lysine decarboxylase CadA, transaminase PatA, amine oxidase ECAO and aldehyde reductase YahK, and finally introducing plasmids carrying the four enzymes into a strain NT1003 of which an alcohol degradation gene ycjQ is knocked out, so as to obtain a strain NT1003 ycjQ-LS01 with high yield of 1, 5-pentanediol. When the recombinant strain NT1003 ycjQ-LS01 takes Lys as a substrate, cofactors (only two NADPHs are needed) are reduced in a synthesis path, a production path (only four steps are needed) is simplified, and metabolic burden caused by introduction of excessive genes is avoided; in addition, an alcohol degradation gene ycjQ is knocked out of the strain, and degradation of pentanediol can be greatly reduced.

The invention relates to escherichia coli engineering bacteria co-utilizing glucose and ethylene glycol and a method for producing L-threonine through fermentation of the escherichia coli engineering bacteria, a genetic engineering method is adopted to obtain a genetic engineering strain, and the genetic engineering strain substantially expresses ethylene glycol metabolism genes including glycerol dehydrogenase, lactaldehyde reductase and lactaldehyde dehydrogenase; the amino acid sequence of the aspartic acid transferase, the aspartic acid kinase, the aspartic acid semialdehyde dehydrogenase, the homoserine dehydrogenase 1, the homoserine kinase, the threonine synthase, the threonine transport protein, the galactose synthase, the phosphoenolpyruvate decarboxylase and the phosphoenolpyruvate synthase are shown in the description; the gene engineering strain is an E.coli BW25113 strain which is characterized in that ldhA, pta, poxB, adhE, pflB, mgsA, frdA, ptsG, tdcB, tdh, ltaE, yiaY, yqhD and ycdW genes are substantially inactivated, or the gene engineering strain is an E.coli BW25113 strain which is obtained by substantially inactivating ldhA, pta, poxB, adhE, pflB, mgsA, frdA, ptsG, tdcB, tdh, ltaE, yiaY, yqhD and ycdW genes. And carrying out fermentation culture on the genetic engineering strain by taking glucose and ethylene glycol as carbon sources, and separating the L-threonine from the culture after the culture is finished.

The invention discloses a keto acid decarboxylase mutant and application thereof in synthesis of phenethyl alcohol derivatives, the keto acid decarboxylase mutant integrates and expresses an ipdC mutant derived from Klebsiellaapneumoniae and aldehyde reductase Cgl0331 through plasmid or genome, valine at the 467th site of the ipdC is mutated into tryptophan, valine at the 467th site of the aldehyde reductase Cgl0331 is mutated into tryptophan, valine at the 467th site of the aldehyde reductase Cgl0331 is mutated into tryptophan, valine at the 467th site of the aldehyde reductase Cgl0331, valine at the 467th site of the aldehyde reductase Cgl0331 the aldehyde reductase Cgl0331 is aldehyde reductase of a corynebacterium glutamicum endogenous source; according to the invention, the conversion rate of phenylpyruvic acid, hydroxyphenylpyruvic acid and 3, 4-dihydroxybenzophenone acid is improved; according to the invention, the aldehyde reductase coded by the Cgl0331 gene is overexpressed, so that the synthesis efficiency of 2-phenethyl alcohol, tyrosol and hydroxytyrosol is improved; the corynebacterium glutamicum whole-cell catalyst disclosed by the invention has higher tolerance to 2-phenethyl alcohol, tyrosol and hydroxytyrosol.

The present invention relates to a recombinant Corynebacterium glutamicum with high yield of 1,3-propylene glycol, wherein the recombinant Corynebacterium glutamicum can overexpress the following genes: deaminase gene AAD, decarboxylase gene KDC, and aldehyde reductase gene yqhD. The present invention enables Corynebacterium glutamicum to overexpress AAD gene, KDC gene and yqhD gene, and enhances the expression amount of homoserine synthesis pathway related enzyme genes, so that in the process of fermentation and production of 1,3-propylene glycol, the yield in the shake flask stage is as high as 6.7g / L, the yield in the fermentation tank is as high as 54.3g / L, the fermentation cost is low and the yield is high, the benefit of producing 1,3-propylene glycol is maximized, and it is suitable for practical promotion and application.