18 results about "Aldehyde dehydrogenase" patented technology

Provided herein are recombinant microorganisms that express a subject polypeptide. Microorganisms can comprise an expression construct comprising a flagellin promoter operatively linked with a heterologous nucleotide sequence encoding the subject polypeptide. The flagellin promoter sequence can comprise a genetic modification that reduces CsrA inhibition of translation. Microorganisms also can comprise a genetic modification that reduces FlgM inhibition of SigD initiation of transcription. The target polypeptide can be an aldehyde dehydrogenase. Such microorganisms are useful in the treatment of alcohol hangover.

The present application provides a kind of kudzu vine cranberry composition for protecting liver from alcohol, which contains the following ingredients by weight: 30-50 parts of extract of Hovenia dulcis Thunb, 30-50 parts of mixed extract, 20-40 parts of extract of Pueraria lobata, 10-20 parts of extract of Poria cocos, 10-20 parts of extract of Glycyrrhiza uralensis, 0.05-0.1 parts of vitamin C; the raw materials of the mixed extract are mixed by cranberry and Fructus Lycii in a mass ratio of (1-2):(1-2). The present application further provides formulations and food containing the composition. The present application further protects the use of the composition or formulation in preparing health food or medicine with auxiliary protective effect on chemical liver injury. The composition provided by the present application can improve the activity of alcohol dehydrogenase / acetaldehyde dehydrogenase, reduce the content of MDA in tissues and increase the content of GSH, and reduce the content of triglyceride in liver cells, thereby comprehensively exerting the effect of protecting liver from alcohol, with high safety, small side effects, and wide sources of raw materials, and having important market value and development prospect.

The application discloses a genetically engineered bacterium for efficiently producing itaconic acid by using corn stalk hydrolysate and application thereof, and belongs to the technical field of gene recombination and metabolic engineering. The genetically engineered bacterium for efficiently producing itaconic acid by using corn stalk hydrolysate is characterized by the following aspects: taking a strain BW08 as a starting strain, heterologously expressing a homocentric acid decarboxylase gene CAD, deleting an isocitric acid dehydrogenase gene Icd, heterologously expressing a xylose acid dehydrase gene XD, a 2-keto-3-deoxy-xylose acid dehydrase gene KDXD and an alpha-ketoglutaric acid semialdehyde dehydrogenase gene KGSADH, and heterologously expressing a citric acid synthase gene gltA. In the fed-batch fermentation, the yield of itaconic acid of the genetically engineered bacterium reaches 68.6 g / L, and the conversion rate reaches 0.6 g / g (total sugar). The genetically engineered bacterium can efficiently metabolize corn stalk hydrolysate to produce itaconic acid.

The embodiment of the present application discloses a Clostridium ethanoligenes mutant with alcohol-aldehyde dehydrogenase knocked out and application thereof in reducing reverse absorption of ethanol product in one-carbon gas fermentation process, and belongs to the technical field of biotechnology. In the process of producing ethanol and microbial protein by Clostridium ethanoligenes using one-carbon gas fermentation, the reverse absorption phenomenon of product ethanol, the alcohol-aldehyde dehydrogenase (Adh, Alcohol dehydrogenase) on the chromosome of Clostridium ethanoligenes is knocked out by gene editing means, so as to reduce or completely block the reverse absorption pathway of ethanol, reduce the loss of ethanol in the fermentation process and in the wort storage tank, and help to improve the ethanol yield, reduce the waste of carbon source and improve the enterprise income.

Abstract Disclosed are biosynthetic methods and engineered microorganism that enhance or improve the biosynthesis of hexamethylenediamine, caproic acid or caprolactam. The engineered microorganisms include selected aldehyde dehydrogenase activity. Abstract 1 / 10 wo 2020 / 219863 PCT / US2020 / 029793 +HO2C 5CoA 5CoA SUCCINYL-CoA ACETYL-CoA A A HO2C 5CoA E,F,G HO2C 002H 3-OXOADIPL-CoA 3-OXOADIPATE B H OH OH HO2C 5CoA HO2C 002H 3-HYDROXYADIPYL-CoA 3-HYDROXYDIPATE C 000000 HO2C 5CoA HO2C OO2H 3-CARBOXY-2-PENTENOYL-CoA 5-CARBOXY-2-PENTENOATE D K,L,M HOC 5CoA HO2C OO2H ADIPYL-CoA ADIPATE X N Y H Z HO2C HO2C OPO3 ADIPATE SEMIALDEHYDE ADIPYLPHOSPATE O,P HO2C NH 6-AMINOCAPROATE S Q,R CoAS NH NH T 6-AMINOCAPROYL-CoA CAPROLACTAM U H V,WNH2 H2N NH2 6-AMINOCAPROATE SEMIALDEHYDE HEXAMETYLENEDIAMINE Fig. 1 SUBSTITUTE SHEET (RULE 26) 20 26 20 48 92 24 J un 2 02 6 1 / 1 0 w o 2 0 2 0 / 2 1 9 8 6 3 P C T / U S 2 0 2 0 / 0 2 9 7 9 3 2 0 2 6 2 0 4 8 9 2 2 4 J u n 2 0 2 6 A 5 C o A E , F , G H O 2 C O O 2 H 3 - O X O A D I P L - C o A 3 - O X O A D I P A T E B H O H O H 5 C o A H O 2 C 0 0 2 H 3 - H Y D R O X Y D I P A T E C 000000 H O 2 C 5 C o A O O 2 H 3 - C A R B O X Y - 2 - P E N T E N O Y L - C o A J O O 2 H 5 C o A H O 2 C A D I P Y L - C o A A D I P A T E X N Y H Z H O 2 C H O 2 C O P O 3 A D I P Y L P H O S P A T E H O 2 C N H 6 - A M I N O C A P R O A T E S Q , R C o A S N H N H 2 T 6 - A M I N O C A P R O Y L - C o A C A P R O L A C T A M U H V , W N H H 2 N N H 2 6 - A M I N O C A P R O A T E S E M I A L D E H Y D E H E X A M E T Y L E N E D I A M I N E F i g . 1 S U B S T I T U T E S H E E T ( R U L E 2 6 )

The present disclosure provides: a variant of a low-specific threonine aldolase; a microorganism comprising the variant; a microorganism comprising the variant and exhibiting enhanced aldehyde dehydrogenase activity; a method for producing at least one amino acid selected from the group consisting of glycine, alanine, and valine, the method comprising a step of culturing the microorganism; and a composition for producing the at least one amino acid, the composition comprising the microorganism. The microorganism exhibits an excellent ability to produce at least one amino acid selected from the group consisting of glycine, alanine, and valine.

The application discloses a method for fermenting 3-hydroxypropionic acid and acrylic acid. The application provides a recombinant Corynebacterium glutamicum, wherein the ald gene of the aldehyde dehydrogenase of the microorganism is up-regulated, the expression of the glycerolaldehyde-3-phosphate dehydrogenase gapA is down-regulated, the heterologous diol dehydratase gene pduCDEGH is expressed, the heterologous 3-phospho dehydrogenase gdp and glycerol 3-phosphatase gpp are expressed. The recombinant microorganism is fermented in a shake flask or a fermenter with glucose or other organic carbon sources as the substrate to obtain 3-hydroxypropionic acid. The 3-hydroxypropionic acid in the fermentation broth is acidified and heated to further obtain acrylic acid. The recombinant microorganism can efficiently produce 3-hydroxypropionic acid and acrylic acid by using cheap glucose, sucrose, molasses and the like as raw materials, the production process is green, safe and simple, and has a good market application prospect.

The application discloses a kind of for waste PET depolymerization system glycol directional efficient conversion of glycolic acid two enzyme level connection system and its application, belong to biological catalysis and resource recycling technical field.The system includes a kind of mutant alcohol dehydrogenase with high selectivity to glycol and a mutant aldehyde dehydrogenase ALDH-V7.Said mutant alcohol dehydrogenase is obtained in at least one combination mutation in 97 and 101 and / or 145 and 148 in the basis of ADH5 enzyme derived from acetic acid bacillus ( Gluconobacter oxydans ).The system can efficiently and directionally oxidize low-value glycol in waste PET chemical or biological depolymerization product to high-value-added product glycolic acid under mild conditions, effectively avoiding peroxidation and C-C bond rupture.The application provides an efficient and green biological catalysis solution for upgrading and recycling of waste PET, and realizes a circular economy path of "waste plastics-degradable plastic monomers".

This invention discloses a human-derived *Lactobacillus TG035* for sake brewing and its application in antioxidant and acetaldehyde dehydrogenase-producing products, belonging to the field of microbial technology. The strain TG035 has the preservation number CCTCC NO: M 20252662, and its 16S rDNA sequence is shown in SEQ ID NO.1. This strain possesses the dual function of producing acetaldehyde dehydrogenase and superoxide dismutase.

A method for preparing 5-hydroxymethyl-2-furanoic acid (HMFA), wherein NAD(P) is used... + Treatment with a β-dependent aldehyde dehydrogenase oxidized 5-hydroxymethylfurfural (HMF) present in aqueous solution to 5-hydroxymethyl-2-furanoic acid (HMFA) in vitro, forming NAD(P)H. The NAD(P)H produced during oxidation was then enzymatically regenerated back into NAD(P) using an oxidoreductase. + Furthermore, ketone compounds are used as cosubstrates for the oxidoreductase.

The present invention relates to an ALDH1A inhibitor compound isoform described in formula (I) and a pharmaceutical composition comprising the said compound. A medical compound for inhibiting the activity of subtype 1A aldehyde dehydrogenase protein is provided, comprising 2,6,8-trisubstituted imidazo[1,2-a]pyridine. Pathologies and diseases resulting from the upmodulation of one or more ALDH1A isoforms can thereby be prevented or treated. TIFF2026521872000027.tif51170

The application belongs to the technical field of nanomaterials, and provides a CaPhy-NAD nanoenzyme, a preparation method, application and an alcoholism treatment preparation thereof. The CaPhy-NAD nanoenzyme is prepared by using calcium phytate nanoparticles as a carrier and in-situ loading of ethanol oxidase, acetaldehyde dehydrogenase, horseradish peroxidase and coenzyme NAD. 2+ The CaPhy-NAD nanoenzyme can effectively activate the catalytic activity of acetaldehyde dehydrogenase, and the three enzymes can have a high-efficiency confined cascade reaction in the pore channel of the calcium phytate nanoparticles, so that the recycling of the coenzyme NAD is realized, and the three types of alcohol metabolism-related toxic substances, i.e., ethanol, acetaldehyde and hydrogen peroxide, can be simultaneously removed. The CaPhy-NAD nanoenzyme prepared by the application has excellent catalytic activity and good biological safety, and can be orally administered, thereby providing a new technical idea and solution for the prevention and treatment of alcoholism.

The invention relates to a method for producing 2,5-furandicarboxylic acid by oxidizing 5-formyl-2-furancarboxylic acid, which is present in an aqueous solution, by treatment with an aldehyde dehydrogenase in vitro to 2,5-furandicarboxylic acid, wherein the NAD(P)H formed during the oxidation is enzymatically oxidized back to NAD(P)+ by means of a dehydrogenase and D-fructose or acetone, after which the enzymes are removed.

Antibiotic-free systems for maintaining plasmids in host cells and methods of using same. The plasmids can comprise one or more plasmid-maintenance genes and a gene of interest configured to express in the host cell. The one or more plasmid-maintenance genes can comprise one or more of a prophage repressor gene, a sucrose phosphorylase gene, and an alcohol / aldehyde dehydrogenase gene. The methods can comprise growing the host cell with the plasmid comprised within the host cell, wherein the plasmid can be maintained during growth in the host cell without the use of antibiotics. In systems with a plasmid comprising a sucrose phosphorylase gene, the methods can comprise growing the host cell in the presence of sucrose as a sole carbon source. In systems with a plasmid comprising an alcohol / aldehyde dehydrogenase gene, the methods can comprise growing the host cell in the presence of glucose as a sole carbon source.

A method for preparing 5-hydroxymethyl-2-furanoic acid (HMFA), wherein NAD(P) is used... + Treatment with a β-dependent aldehyde dehydrogenase was used to oxidize 5-hydroxymethylfurfural (HMF) present in aqueous solution in vitro to 5-hydroxymethyl-2-furanoic acid (HMFA) to form NAD(P)H; subsequently, NAD(P)H oxidase was used to enzymatically regenerate the NAD(P)H formed during oxidation back into NAD(P). + The NAD(P)H oxidase is characterized by comprising an amino acid sequence selected from the group consisting of: i) an amino acid sequence having at least 80% identity with SEQ ID NO:14, SEQ ID NO:16 or SEQ ID NO:18; ii) an amino acid sequence encoded by a nucleic acid having at least 80% identity with SEQ ID NO:13, SEQ ID NO:15 or SEQ ID NO:17; and iii) an amino acid sequence encoded by a nucleic acid bound under stringent conditions to a nucleic acid molecule having a nucleic acid sequence having SEQ ID NO:13, SEQ ID NO:15 or SEQ ID NO:17.

The application discloses a method for biocatalyzing aromatic aldehyde into aromatic acid by using oxidized artificial nicotinamide cofactor. The method uses aromatic aldehyde compounds as substrates, uses aldehyde dehydrogenase and oxidized artificial nicotinamide cofactor as a catalytic system, and generates aromatic acid compounds through catalytic reaction in a solvent. The method is convenient to operate, has high product yield, and has a good industrial application prospect in the field of biocatalytic preparation of aromatic acid. In the method for biocatalyzing aromatic aldehyde into aromatic acid by using oxidized artificial nicotinamide cofactor, the cofactor used is artificially synthesized and is not a natural nicotinamide cofactor which is expensive, so that the production cost of aromatic acid from aromatic aldehyde is reduced.