140 results about "Aldehyde dehydrogenase" 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 provides a lysine artificial operon and application thereof. The gene sequence of the artificial operon comprises a promoter, a lysC gene for coding aspartate kinase, an asd gene for coding aspartate semialdehyde dehydrogenase, a dapA gene for coding dihydropicolinic acid synthetase and a dapB gene for coding dihydropicolinic acid reductase, the ddh gene is used for coding diaminopimelate dehydrogenase; the lysA gene is used for coding diaminopimelate decarboxylase; except for the first lysC gene, sequences of RBS ribose binding sites of other genes are RBS ribose binding sites translated after gene transcription by intercepting 20-26nt DNA sequences at the upstream of a coding region ATG (adenosine triphosphate); the RBS ribose binding site is connected in front of the corresponding gene.

The invention discloses a Lactobacillus paracasei grx06 and an application thereof in the aspects of dispelling the effects of alcohol and protecting the liver, the strain number of the Lactobacillus paracasei is grx06, the Lactobacillus paracasei is preserved in the China General Microbiological Culture Collection Center on February 18, 2025, and the preservation number is CGMCC No: 33560. The lactobacillus paracasei obtained by screening in the invention has the capability of producing ethanol dehydrogenase and acetaldehyde dehydrogenase at high yield, and is high in ethanol tolerance. In addition, the traditional Chinese medicine composition has the effects of promoting ethanol metabolism in rats and recovering liver injury. Wide application prospects are realized in the field of anti-alcohol and liver-protecting products.

The invention provides geranial dehydrogenase as well as a preparation method and application thereof, and relates to the technical field of biology, and the amino acid sequence of the geranial dehydrogenase is as shown in SEQ ID NO.1. Citral can be used as a substrate to catalytically synthesize the aromatic folic acid, and the conversion rate reaches 90%. The geranial dehydrogenase can be used for efficiently synthesizing the aromatic folic acid and can be used for biocatalytically converting the aromatic folic acid. Meanwhile, NAD < + > is used as a coenzyme to improve the enzymatic reaction efficiency, so that efficient catalytic synthesis of the aromatic folic acid is realized.

The invention relates to a method for producing vanillin from natural lignocellulose biomass through co-culture of pichia pastoris, which comprises the following steps: respectively constructing a xylan hydrolysis recombinant strain (for releasing ferulic acid) and a vanillin synthesis recombinant strain (for converting ferulic acid) to realize conversion production from a natural xylan substrate to vanillin. In order to reduce the generation of by-products, 15 genes for coding aldehyde dehydrogenase (ALDRs), alcohol dehydrogenase (ADHs) and aldehyde ketoreductase (AKRs) are further knocked out from the vanillin synthesis recombinant strain, so that the vanillin can be further converted into the by-product vanillic acid, thereby improving the yield and purity of the vanillin.

The invention discloses a genetically engineered probiotic composition for expressing ADH (adenosine dihydrogenase) and ALDH (aldehyde dehydrogenase) and application of the genetically engineered probiotic composition in hangover alleviating and liver protection. The genetically engineered probiotic composition (such as EcN.1917-ADH and EcN.1917-ALDH) is constructed by introducing genes of alcohol dehydrogenase (ADH, NCBI (National Center for Biotechnology Information) Gene ID: 855349) and acetaldehyde dehydrogenase (ALDH, NCBI Gene ID: 855206) of saccharomyces cerevisiae into probiotics (such as escherichia coli). The engineering bacterium shows remarkable ethanol, acetaldehyde and endurance capacity in an in-vitro experiment, and the ethanol degradation rate is remarkably higher than that of a wild type strain; a mouse drunkenness model verifies that drunkenness and death caused by drinking can be reduced through pretreatment, drunkenness tolerance time is remarkably prolonged, and movement coordination disorder caused by alcohol can be improved. The strain can effectively promote alcohol metabolism and relieve alcoholic liver injury, and a new candidate strain is provided for development of a hangover-alleviating and liver-protecting viable bacterial preparation.

The invention provides polypeptides and encoding nucleic acids of aldehyde dehydrogenase variants. The invention also provides cells expressing aldehyde dehydrogenase variants. The invention further provides methods for producing 3-hydroxybutyraldehyde (3-HBal) and / or 1,3-butanediol (1,3-BDO), or an ester or amide thereof, comprising culturing cells expressing an aldehyde dehydrogenase variant or using lysates of such cells. The invention additional provides methods for producing 4-hydroxybutyraldehyde (4-HBal) and / or 1,4-butanediol (1,4-BDO), or an ester or amide thereof, comprising culturing cells expressing an aldehyde dehydrogenase variant or using lysates of such cells.

Methods of producing a consumable alcoholic product involve utilizing one or more enzymes to reduce or remove an oral pain response otherwise experienced upon consumption of the product. Methods involve admixing at least one oxidase with a fermentate and optionally distilling the fermentate to produce a consumable alcoholic product, such as a distilled alcohol. Methods involve admixing at least one oxidase comprising an aldehyde dehydrogenase.

A method for preparing glycine by using threonine relates to a fermentation process in which threonine is decomposed into glycine and acetaldehyde by aldolase. Glycine and acetyl coenzyme A can be produced in a fermentation process, in which acetaldehyde is reduced into acetyl coenzyme A or an acetyl coenzyme A derivative by acetylating acetaldehyde dehydrogenase; or threonine is dehydrogenated by threonine dehydrogenase to obtain 2-amino-3-ketobutyric acid, which is then ligated by 2-amino-3-ketobutyrate CoAligase to obtain acetyl coenzyme A. Coenzyme A can be converted into an acetyl coenzyme A derivative under different fermentation conditions.

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 invention provides a compound with which a molecular probe capable of distinguishing NSCs from CSCs can be produced, and a method for detecting cancer stem cells using the compound. The present invention relates to a compound having a formyl group, a substrate moiety, a quenching moiety, and a luminescent moiety that is non-luminous due to the quenching moiety, wherein the luminescent moiety may be rendered luminous by detaching the substrate moiety by a substrate-degrading enzyme and also converting the formyl group to a carboxy group by an aldehyde dehydrogenase to allow the quenching moiety to dissociate.

This invention relates to a hangover relief composition containing a dried powder, lysate, or extract of enzymes that produce glutathione and aldehyde dehydrogenase. Specifically, this invention relates to a hangover relief composition containing dried powder, lysate, or extract of *Saccharomyces cerevisiae* Kwon P-1 KCTC 13925BP, *Saccharomyces cerevisiae* Kwon P-2 KCTC14122BP, and *Saccharomyces cerevisiae* Kwon P-3 KCTC14123BP, which simultaneously produce glutathione and aldehyde dehydrogenase.

The present invention relates to a yeast cell, in particular a recombinant yeast cell, the cell lacking enzymatic activity needed for the NADH-dependent glycerol synthesis or the cell having a reduced enzymatic activity with respect to the NADH-dependent glycerol synthesis compared to its corresponding wild-type yeast cell, the cell comprising one or more heterologous nucleic acid sequences encoding an NAD+-dependent acetylating acetaldehyde dehydrogenase (EC 1.2.1.10) activity. The invention further relates to the use of a cell according to the invention in the preparation of ethanol.

The invention provides polypeptides and encoding nucleic acids of aldehyde dehydrogenase variants. The invention also provides cells expressing aldehyde dehydrogenase variants. The invention further provides methods for producing 3-hydroxybutyraldehyde (3-HBal) and / or 1,3-butanediol (1,3-BDO), or an ester or amide thereof, comprising culturing cells expressing an aldehyde dehydrogenase variant or using lysates of such cells. The invention additional provides methods for producing 4-hydroxybutyraldehyde (4-HBal) and / or 1,4-butanediol (1,4-BDO), or an ester or amide thereof, comprising culturing cells expressing an aldehyde dehydrogenase variant or using lysates of such cells.

The application discloses a method for preparing and removing odor of Hirudo nipponia freeze-dried powder, and the method comprises the following steps: inducing clean treatment in an empty stomach, low-temperature stress pretreatment, in-situ quick freezing under the protection of inert gas, segmented vacuum freeze-drying and low-temperature airflow crushing. The application induces the expression up-regulation of aldehyde dehydrogenase and alcohol dehydrogenase in the body of Hirudo nipponia through low-temperature stress, and utilizes ice crystals to destroy cell compartmentalization in in-situ quick freezing, so that the enzymes and their substrates are contacted, in-situ enzymatic conversion occurs under the protection of inert gas, and fishy components are degraded into low-smell metabolites. The application does not need exogenous odor-removing substances and post-processing procedures, has high antithrombin activity retention rate, greatly reduces the total amount of fishy substances, and realizes in-situ synergistic odor removal in the whole freeze-drying process.

Alcohol dehydrogenases and aldehyde dehydrogenases having kinetic properties advantageous for the industrial production of glycolic acid or other hydroxycarboxylic acids, from ethylene glycol or other aliphatic polyhydric alcohols having a terminal hydroxyl group, are described herein. Microorganisms expressing one or both dehydrogenases, as well as their use in fermentative processes are also described.

The present invention discloses the construction and application of a recombinant Gluconobacter oxydans, belonging to the fields of genetic engineering and whole-cell catalysis. The present invention heterologously expresses an epoxide hydrolase from Sphingomonas in Gluconobacter oxydans, and simultaneously utilizes the alcohol and aldehyde dehydrogenases bound to the membrane of Gluconobacter oxydans itself to synthesize R-mandelic acid in a one-step process using styrene oxide as a substrate. The present invention combines the transcriptome data of Gluconobacter oxydans, screens 7 strong promoters using green fluorescent protein as a reporter gene, and determines the strongest promoter P for expressing the epoxide hydrolase gene. 12780 , ultimately significantly increasing the yield of R-mandelic acid.

Process for the production of 5-hydroxymethyl-2-furancarboxylic acid (HMFA), wherein 5-hydroxymethylfurfural (HMF), which is present in an aqueous solution, is oxidized to obtain 5-hydroxymethyl-2-furancarboxylic acid (HMFA) by treatment with an NAD(P)+-dependent aldehyde dehydrogenase in vitro with NAD(P)H being formed; after said oxidation step the NAD(P)H formed during the oxidation is enzymatically regenerated with an oxidoreductase back to NAD(P)+, and a keto compound is used as a cosubstrate of the oxidoreductase.

This invention relates to the field of functional food technology, and more particularly to the application of safflower honey, or safflower honey extract, in enhancing the activity of alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH). The invention has found that safflower honey, or safflower honey extract, can effectively enhance ADH and ALDH activity, thereby promoting alcohol metabolism and achieving a hangover-relieving effect. Further research on the extract revealed that a mixture of syringaldehyde, riboflavin, lutein, luciferin, and three p-coumaroyl spermidine plays a key role in enhancing ADH and ALDH activity, thus providing an application of this mixture in hangover relief. The application of safflower honey and its extract provided by this invention has high application value for developing foods and health products with hangover-relieving effects.

The present invention relates to a yeast cell, in particular a recombinant yeast cell, the cell lacking enzymatic activity needed for the NADH-dependent glycerol synthesis or the cell having a reduced enzymatic activity with respect to the NADH-dependent glycerol synthesis compared to its corresponding wild-type yeast cell, the cell comprising one or more heterologous nucleic acid sequences encoding an NAD+-dependent acetylating acetaldehyde dehydrogenase (EC 1.2.1.10) activity. The invention further relates to the use of a cell according to the invention in the preparation of ethanol.

Provided is a genetically engineered strain of Saccharomyces cerevisiae ST100-Suc3 for producing succinic acid. The Saccharomyces cerevisiae ST100-Suc3 is obtained by overexpressing malate dehydrogenase (ScMDH3R), fumarase (RoFUM) and fumarate reductase (TbFRD) in Saccharomyces cerevisiae PY-EDS8 while knocking out a glycerol-3-phosphate dehydrogenase (GPD1) gene, an alcohol dehydrogenase (ADH1) gene and an aldehyde dehydrogenase (ALD6) gene. The Saccharomyces cerevisiae strain is Saccharomyces cerevisiae PY-EDS8, with the deposit number GDMCC No: 63815. The strain exhibits tolerance to high-concentration succinic acid and can grow in a liquid medium supplemented with 100 g / L of succinic acid (pH=2.68), but produces almost no succinic acid.

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.

A production method according to one embodiment is a method for producing 4-(aminomethyl)cyclohexane-1-carboxylic acid from 1,4-bis(aminomethyl)cyclohexane using a protein consisting of an amino acid sequence having 60% or more identity to an amino acid sequence shown in any one of SEQ ID NOs. 1 to 4 and 103 to 105 and having transamination activity, and a protein consisting of an amino acid sequence having 50% or more identity to an amino acid sequence shown in any one of SEQ ID NOs. 19 to 22, 35 to 46 and 127 to 139 and having aldehyde dehydrogenase activity.

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 application discloses an aldolase bioelement screening method and related application of a series of aldolases in catalyzing a condensation reaction of formaldehyde and pyruvic acid to synthesize 4-hydroxy-2-ketobutyric acid. The aldolase provided by the application is a protein shown in SEQ ID NO. 1-NO. 10, or a functionally identical protein obtained through substitution and / or deletion / addition of one or more amino acid residues. The aldolase has the following characteristics: 1) belonging to the HpcH functional domain family protein; 2) the sequence length is 240-320 amino acids; 3) the existing database function annotation is 4-hydroxy-2-oxovalerate aldolase (can catalyze the condensation reaction of acetaldehyde and pyruvic acid); the aldolase can take formaldehyde and pyruvic acid as substrates, and can carry out enzyme catalysis reaction in appropriate conditions and medium, and can efficiently biosynthesize 4-hydroxy-2-ketobutyric acid, and has the remarkable characteristics of mild reaction condition, good stereoselectivity and no pollution.

The invention relates to the technical field of biology, and discloses a genetically engineered bacterium for high yield of 1, 4-butanediol and application of the genetically engineered bacterium. Escherichia coli is used as a chassis bacterium, a gene ldhA for coding lactic dehydrogenase, a gene adhE for coding ethanol dehydrogenase, a gene pflB for coding formate lyase, and a gene gabD and a gene yneI for coding succinate semialdehyde dehydrogenase are knocked out from a chassis bacterium genome, expression of a succinate semialdehyde dehydrogenase gene sucD and a 4-hydroxybutyrate dehydrogenase gene 4hbD is strengthened, a pdhR gene is knocked out, and a recombinant plasmid is obtained. The expression of the gene gltAR164L is enhanced, the gene mdh, the gene arcA, the gene poxB, the gene sdhAB and the gene ptsG are knocked out, and the expression of the glf gene and the ppc gene is enhanced; the method comprises the following steps of: transferring plasmids carrying a gene ald for coding aldehyde dehydrogenase, a gene cat2 for coding acyltransferase and a gene yqhD for coding alcohol dehydrogenase into a chassis bacterium, and carrying out metabolic transformation to obtain a genetically engineered bacterium which carries exogenous plasmids and has the capabilities of high yield and extracellular accumulation of 1, 4-BDO, so that the yield of 1, 4-BDO can be increased to 4.71 g / L.

The invention discloses a dry chemical reaction reagent for measuring potassium ions in urine. The dry chemical reaction reagent is prepared by drying a dry chemical reaction solution within a first temperature range for a first time period, the dry chemical reaction solution consists of acetaldehyde dehydrogenase, coenzyme, a protective agent, a stabilizer, a film-forming agent, a surfactant and diaphorase; the coenzyme is one of NAD < + > or NADP < + >; the protective agent is a mixed solution of one or more of BSA (Bovine Serum Albumin) and sericin; the stabilizer is a mixed solution of one or more of cane sugar and trehalose; the film-forming agent is any one of gelatin, polyethylene glycol and carboxymethyl cellulose; and the surfactant is a triton series or Tween series surfactant. The determination method for determining the potassium ions in the urine comprises the following steps: adding a dry chemical reaction reagent into a corresponding reaction hole of a reaction device, drying, and directly forming a film as a carrier of a potassium ion reaction; a to-be-detected sample is diluted with a sample diluent and then added into a reaction hole of the reaction device for reaction, and the concentration of potassium ions is determined according to the color depth of a reaction solution.

The present invention relates to food and pharmaceutical compositions for inhibiting tremor or dyskinesia comprising a novel aldehyde dehydrogenase encoded by a gene having more than 98% homology with the gene of SEQ ID NO: 1. Furthermore, the present invention relates to a food composition and a pharmaceutical composition for inhibiting tremor or dyskinesia, said composition comprising a lysate of any one selected from the group consisting of KCTC 13925BP, KCTC 14122BP, KCTC 14123BP, KCTC 14983BP, KCTC 14984BP and KCTC 14985BP, or a mixture thereof.

The invention provides an engineering bacterium for producing spermidine and a preparation method of the engineering bacterium, and relates to the field of genetic engineering. According to the invention, arginine decarboxylase, aspartate kinase, aspartate-semialdehyde dehydrogenase, spermidine efflux protein (MdtI / MdtJ), carboxylaminopropyl agmatine dehydrogenase (CAPADH), carboxylaminopropyl agmatine decarboxylase (CAPADC) and aminopropyl agmatine urea hydrolase (APAUH) are subjected to overexpression in escherichia coli by using a gene engineering technology, and then the escherichia coli is subjected to enzyme deactivation, so that the escherichia coli is obtained. The genetically engineered bacterium capable of producing the spermidine can be obtained by simultaneously knocking out a spermidine transport system (PotBCAD), a spermidine-N-acetyltransferase (spermidine-N-acetyltransferase) and a homoserine dehydrogenase (homoserine dehydrogenase), so that the genetically engineered bacterium capable of producing the spermidine can be obtained. The engineering bacterium greatly reduces the production cost of spermidine, has a wide application prospect, and lays a foundation for green production of spermidine.

The invention relates to a method for producing 5-hydroxymethyl-2-furancarboxylic acid (HMFA), wherein 5-hydroxymethylfurfural (HMF), which is present in an aqueous solution, is oxidized in order to form 5-hydroxymethyl-2-furancarboxylic acid (HMFA) by means of a treatment using an NAD(P)+-dependent aldehyde dehydrogenase in vitro, thereby forming NAD(P)H, after which the NAD(P)H formed during the oxidation process is enzymatically regenerated using an NAD(P)H oxidase in order to form NAD(P)+. The method is characterized in that the NAD(P)H oxidase comprises an amino acid sequence selected from the group consisting of: i) an amino acid sequence which has an identity of at least 80% to SEQ ID No. 14, SEQ ID No. 16, or SEQ ID No. 18, ii) an amino acid sequence encoded by a nucleic acid which has an identity of at least 80% to SEQ ID No. 13, SEQ ID No. 15, or SEQ ID No. 17, and iii) an amino acid sequence encoded by a nucleic acid which, under stringent conditions, binds to a nucleic acid molecule having the nucleic acid sequence SEQ ID No. 13, SEQ ID No. 15, or SEQ ID No. 17.