57 results about "Aldehyde dehydrogenase (NAD+)" patented technology

Using the methods of the present invention, intermediate (int) levels of aldehyde dehydrogenase (ALDH) activity reliably distinguished leukemic CD34+CD38− cells capable of engrafting immunodeficient mice, from residual normal hematopoietic stem cells that exhibited relatively higher ALDH activity. Minimal residual disease (MRD) detected during complete remission was enriched for the CD34+CD38−ALDHint leukemic cells, and the presence of these cells after therapy highly correlated with subsequent clinical relapse. The methods of the present invention can distinguish normal from leukemic CD34+CD38− cells, and identifies those AML cells associated with relapse. Methods of prediction of relapse of AML patients and methods of treatment are also provided.

Populations of stem cells and methods for their isolation and use are provided. These stem cell populations comprise aldehyde dehydrogenase positive (ALDHbr) cells isolated from bone marrow, and ALDHbr CD105+ cells derived from any stem cell source. These populations may also comprise cells expressing such surface markers as CD34, CD38, CD41, CD45, CD105, CD133, CD135, CD117, and HLA-DR, and / or are substantially free from such cell surface markers as CD3, CD7, CD 10, CD 13, CD 14, C1319, CD33, CD35, CD56, CD 127, CD 138, and glycophorin A. The population may also comprise cells expressing CD90. The stem cell populations of the invention are isolated from a stem cell source such as bone marrow, peripheral blood, umbilical cord blood, and fetal liver. Methods of the invention comprise isolating and purifying stem cell populations from stem cell sources, and methods of using these cells to reconstitute, repair, and regenerate tissues.

A non-naturally occurring microbial organism has at least one exogenous nucleic acid encoding a MEK pathway enzyme expressed in a sufficient amount to produce MEK. The MEK pathway includes an enzyme selected from an acetoacetyl-CoA dehydrogenase (bifunctional), an acetoacetyl-CoA aldehyde dehydrogenase, a 3-oxobutyraldehyde reductase, a 3-oxobutanol dehydratase, an MEK oxidoreductase, a 3-oxobutyraldehyde aminotransferase, a 4-aminobutan-2-one deaminase, a 2-amino-4-ketopentanoate (AKP) thiolase, an AKP aminotransferase, a 2,4-dioxopentanoate decarboxylase, an AKP deaminase, an acetylacrylate decarboxylase, an AKP decarboxylase, a glutamate dehydrogenase, a 3-oxobutyraldehyde oxidoreductase (aminating) and an AKP oxidoreductase (aminating). A 2-butanol pathway further includes an MEK reductase. A method for producing MEK or 2-butanol includes culturing these organisms under conditions and for a sufficient period of time to produce MEK or 2-butanol.

Disclosed is a strain of Escherichia sp., capable of producing O-acetyl homoserine in high yield, with the introduction and enhancement therein of the activity of: homoserine acetyl transferase, aspartokinase and homoserine dehydrogenase; and at least one enzyme selected from a group consisting of phosphoenolpyruvate carboxylase, aspartate aminotransferase and aspartate semi-aldehyde dehydrogenase. Also, a method of producing O-acetyl homoserine using the strain is provided.

A non-naturally occurring microbial organism has at least one exogenous nucleic acid encoding a MEK pathway enzyme expressed in a sufficient amount to produce MEK. The MEK pathway includes an enzyme selected from an acetoacetyl-CoA dehydrogenase (bifunctional), an acetoacetyl-CoA aldehyde dehydrogenase, a 3-oxobutyraldehyde reductase, a 3-oxobutanol dehydratase, an MEK oxidoreductase, a 3-oxobutyraldehyde aminotransferase, a 4-aminobutan-2-one deaminase, a 2-amino-4-ketopentanoate (AKP) thiolase, an AKP aminotransferase, a 2,4-dioxopentanoate decarboxylase, an AKP deaminase, an acetylacrylate decarboxylase, an AKP decarboxylase, a glutamate dehydrogenase, a 3-oxobutyraldehyde oxidoreductase (aminating) and an AKP oxidoreductase (aminating). A 2-butanol pathway further includes an MEK reductase. A method for producing MEK or 2-butanol includes culturing these organisms under conditions and for a sufficient period of time to produce MEK or 2-butanol.

The invention discloses a recombinant strain for producing a 3-hydracrylic acid homopolymer and / or a 3-hydracrylic acid copolymer and an application thereof. The construction method of the recombinant strain comprises the following steps: leading 1,3-Propanediol dehydrogenase coded genes, aldehyde dehydrogenase coded genes, 3-hydracrylic acid coenzyme A ligase coded genes and PHA (Polyhydroxyalkanoates) polymerase coded genes into a starting strain to obtain the recombinant strain. The experiments in the invention prove that the engineering bacteria can efficiently express 3-hydracrylic acid coenzyme A ligase coded genes and PHA polymerase coded genes and enable the 3-hydracrylic acid to be finally polymerized into 3-hydracrylic acid homopolymer (P(3HP)) from the 3-hydracrylic acid coenzyme A. Minitype fermentation tank experiments show that the engineering bacteria provided by the invention can have a maximum P (3HP) output of 8.9g / L after being fermented in a 6L fermentation tank and the P (3HP) can account for a maximum 91.5% of cell dry weight. In addition, the recombinant strain provided by the invention has the advantages of simple production process, low costs and broad application prospects.

The invention discloses a genetically engineered bacterium for expressing a human derived acetaldehyde dehydrogenase gene and application thereof, and belongs to the technical field of gene engineering and enzyme. The ALDH2 gene efficient expression component Trp1L-URA3-TPIp-ALDH2-TPIt-Trp1R is integrated into the genome of Saccharomyces cerevisiae W303-1A, the stability of gene expression is improved compared with free plasmid expression, a constitutive promoter is used, no induction agent is added during fermentation, and the product is relatively safe. When fermentation is performed for 96hours, the specific activity of producing acetaldehyde dehydrogenase reaches 0.97 U / mg. The specific activity of the producing acetaldehyde dehydrogenase reaches 6.256 U / mg in ethanol with the concentration of 250 mg / 100 mL, and the specific activity of the producing aldehyde dehydrogenase in a buffer with pH of 3 reaches 0.301 U / mg. The Saccharomyces cerevisiae is selected as a host strain, on the one hand, the activity of the enzyme is kept, on the other hand, product safety is improved, and a new approach and a theoretical basis are provided for the research and development of antialcoholicdrugs.

A 3-hydroxypropionic acid(3HP) degradation way of halophilic bacteria is analyzed for the first time by a transcriptomics method, the inventor finds that the 3-hydroxypropionic acid can degrade genesdddA and dddC, and recombination halophilic bacteria TD delta dddA which cannot degrade 3HP is obtained. Based on this, an alcohol dehydrogenase gene AdhP and an aldehyde dehydrogenase gene AldDTD, which are from the halophilic bacteria endogenous and responsible for production and metabolism of the 3HP are further utilized, and a synthetizing biology means is taken for adjusting and controlling the expression level of the metabolic way. Through screening, the recombination halophilic bacteria high in yield of the 3HP is obtained, and the yield and the productivity are respectively 0.93g / g ofthe 1,3-propylene glycol(PDO) and 2.4g / L / h, which are the highest 3HP yield and productivity reported so far.

The present disclosure provides optimized recombinant cells for the production of n-butanol. Methods for the use of these cells are also provided. Specifically, the utility of acylating aldehyde dehydrogenases and pyruvate:flavodoxin / ferredoxin-oxidoreductase for the improvement of n-butanol yields from recombinant cells is disclosed.

The invention discloses an ALDH2 (aldehyde dehydrogenase 2) Gene polymorphism detection kit, having the advantages that detection sensitivity is high, the lowest detection limit is 7.8 pg DNA; the kitis simple to operate and allows point-of-care test without professional knowledge; the detection time is short, down to 45 min; the detection specificity is high, and the detection accuracy is very high since a specific fluorescent probe is used; nucleic acid extraction is not required, low-melting-point agarose is added, and PCR (polymerase chain reaction) is greatly avoided. When used with ParaDNA gene amplification detectors to carry out POCT (point-of-care test), the kit can be used to clinically provide guidance on the administration of nitroglycerin and the notification on the risk of alcohol drinking.

The present invention provides compositions comprising therapeutic nucleic acids such as interfering RNA (e.g., dsRNA such as siRNA) that target aldehyde dehydrogenase (ALDH) gene expression, lipid particles comprising one or more (e.g., a cocktail) of the therapeutic nucleic acids, methods of making the lipid particles, and methods of delivering and / or administering the lipid particles (e.g., for treating alcoholism in humans).

The invention discloses a method for preparing glucaric acid from inositol by adopting a ''one pot-two step'' enzyme catalysis means, and comprises the following steps: catalyzing inositol by utilizing inositol oxidase so as to produce an intermediate glucuronic acid; and then, converting the intermediate glucuronic acid into the glucaric acid by utilizing aldehyde dehydrogenase. Compared with existing gluconic acid production methods, the method disclosed by the invention has the advantages of being simple in production process, green, friendly, high in yield, conducive to large-scale preparation and the like.

Provided herein are methods, compositions and formulations to prevent or ameliorate ethanol intolerance, reduce or ameliorate symptoms associated with acetaldehyde accumulation accompanying ethanol consumption, or reduce the risk of diseases or disorders caused by acetaldehyde accumulation, comprising administering 4-MP, or physiologically acceptable salts thereof, to subjects with reduced or absent aldehyde dehydrogenase subtype 2 (ALDH2) activity.

The invention discloses an inositol oxygenase mutant and application thereof, and belongs to the technical field of bioengineering. The method comprises the steps that an inositol oxygenase mutant with improved enzyme activity is obtained through site-specific mutagenesis and co-expressed with aldehyde dehydrogenase (udh) in yeast, and the glucaric acid synthetic route is enhanced. Through comparisons, the yield of recombinant Pichia pastoris GS115-udh-mioxK59V / R171S is the highest, and glucaric acid 1.20g / L is produced in a YPD-MI culture medium during flask shaking fermentation culture. A metabolic engineering strategy is adopted, microbiological strains are improved to synthesize the target product glucaric acid, and a certain foundation is laid for efficient production of glucaric acid through a biological method.

The invention discloses an indole acetaldehyde dehydrogenase gene ald2 and an overexpression method and application thereof. An IAA biosynthesis key gene ald2 of Trichoderma harzianum NJAU4742 is disclosed, and the nucleotide sequence is shown in SEQ ID NO: 1. The gene ald2 of IAA biosynthesis key gene ald2 of Trichoderma harzianum NJAU4742 is provided. A method for overexpression of an indoleacetaldehyde dehydrogenase gene ald2. The application of indole aldehyde dehydrogenase gene ald2 and its overexpressed fragment in the construction of Trichoderma harzianum NJAU4742 with significantly increased IAA production. The ald2 gene of the newly discovered Trichoderma harzianum NJAU4742 plays an important role in the IAA synthesis process, and the IAA content at the columnar sheath position inthe root hair region of the plant main root system can be significantly increased after the gene is overexpressed. The present invention provides theoretical basis and technical guarantee for the development of novel Trichoderma bio-organic fertilizer and ecological agriculture.

This invention relates to the bioproduction of substituted or unsubstituted phenylacetaldehyde, 2-phenylethanol, phenylacetic acid or phenylethylamine by subjecting a starting material comprising glucose, L-phenylalanine, substituted L-phenylalanine, styrene or substituted styrene to a plurality of enzyme catalyzed chemical transformations in a one-pot reaction system, using recombinant microbial cells overexpressing the enzymes. To produce phenylacetaldehyde from styrene, the cells are modified to overexpress styrene monooxygenase (SMO) and styrene oxide isomerase (SOI). To produce phenylacetic acid from styrene, SMO, SOI and aldehyde dehydrogenase are overexpressed. Alternatively, to produce 2-phenylethanol, SMO, SOI and aldehyde reductase or alcohol dehydrogenase are overexpressed, while to produce phenylethylamine, SMO, SOI and transaminase are overexpressed.

High aldehyde dehydrogenase 1A1 (ALDH1A1) activity has emerged as a reliable marker for the identification of both normal and cancer stem cells. Herein, is presented AlDeSense, a turn-on green fluorescent probe for aldehyde dehydrogenase 1A1 (ALDH1A1) and Ctrl-AlDeSense, a matching non-responsive reagent. AlDeSense exhibits a 20-fold fluorescent enhancement when treated with ALDH1A1. Through the application of surface marker antibody staining, tumorsphere assays, and assessment of tumorigenicity, the disclosed results show that cells exhibiting high AlDeSense signal intensity have properties of cancer stem cells. Herein, is also reported the development of a red congener, red-AlDeSense. Importantly, red-AlDeSense represents one of only a few examples of a turn-on sensor in the red region using the d-PeT quenching mechanism.

The invention discloses a method for rapidly detecting activity of acetaldehyde dehydrogenase by using a fluorescence spectrophotometer. The method comprises the steps of firstly preparing coenzyme I solutions of different concentration gradients from a Tris-HCl buffer solution and a coenzyme I, detecting fluorescence values of the coenzyme I solutions of different concentrations, establishing a coenzyme I concentration-fluorescence value corresponding standard curve, controlling the temperature of a reaction system, prepared from crude aldehyde dehydrogenase enzyme liquid, a 0.1mol / L Tris-HCl buffer solution with the pH value of 7.0-9.0 and the like, to be 25-40 DEG C, maintaining for 10-30 minutes, then, determining the minutely fluorescence change value of the crude aldehyde dehydrogenase enzyme liquid in the reaction system under the conditions that the excitation wavelength is 320-380nm and the emission wavelength is 440-480nm, and finally, calculating the activity unit of acetaldehyde dehydrogenase according to an equation, namely the enzyme activity unit=delta fluorescence value / 3. The determination method is simple and convenient in operation and high in sensitivity.

The invention discloses a recombinant strain for producing a 3-hydracrylic acid homopolymer and / or a 3-hydracrylic acid copolymer and an application thereof. The construction method of the recombinant strain comprises the following steps: leading 1,3-Propanediol dehydrogenase coded genes, aldehyde dehydrogenase coded genes, 3-hydracrylic acid coenzyme A ligase coded genes and PHA (Polyhydroxyalkanoates) polymerase coded genes into a starting strain to obtain the recombinant strain. The experiments in the invention prove that the engineering bacteria can efficiently express 3-hydracrylic acid coenzyme A ligase coded genes and PHA polymerase coded genes and enable the 3-hydracrylic acid to be finally polymerized into 3-hydracrylic acid homopolymer (P(3HP)) from the 3-hydracrylic acid coenzyme A. Minitype fermentation tank experiments show that the engineering bacteria provided by the invention can have a maximum P (3HP) output of 8.9g / L after being fermented in a 6L fermentation tank and the P (3HP) can account for a maximum 91.5% of cell dry weight. In addition, the recombinant strain provided by the invention has the advantages of simple production process, low costs and broad application prospects.

The present invention relates to a yeast cell that is genetically modified comprising:a) a disruption of one or more aldehyde dehydrogenase (E.C:1.2.1.4) native to the yeast;b) one or more nucleotide sequence encoding a heterologous NAD+-dependent acetylating acetaldehyde dehydrogenase (E.C. 1.2.1.10);c) one or more nucleotide sequence encoding a homologous or heterologous acetyl-CoA synthetase (E.C. 6.2.1.1); andd) a modification that leads to reduction of glycerol 3-phosphate phosphohydrolase (E.C. 3.1.3.21) and / or glycerol 3-phosphate dehydrogenase (E.C. 1.1.1.8 or E.C. 1.1.5.3) activity, native to the yeast.

A microorganism capable of producing acrylic acid, comprising a genetic modification that increases activity of CoA acylating aldehyde dehydrogenase (ALDH) catalyzing conversion of 3-hydroxypropionaldehyde (3-HPA) to 3-hydroxy propionyl-CoA (3-HP-CoA) and a genetic modification that increases activity of 3-HP-CoA dehydratase catalyzing conversion of 3-HP-CoA to acrylyl-CoA in the microorganism in comparison with a cell that is not genetically engineered; as well as a method of producing the microorganism, and a method of producing acrylic acid using the same.

The present invention relates to a yeast cell that is genetically modified comprising:a) a disruption of one or more aldehyde dehydrogenase (E.C:1.2.1.4) native to the yeast;b) one or more nucleotide sequence encoding a heterologous NAD+-dependent acetylating acetaldehyde dehydrogenase (E.C. 1.2.1.10);c) one or more nucleotide sequence encoding a homologous or heterologous acetyl-CoA synthetase (E.C. 6.2.1.1); andd) a modification that leads to reduction of glycerol 3-phosphate phosphohydrolase (E.C. 3.1.3.21) and / or glycerol 3-phosphate dehydrogenase (E.C. 1.1.1.8 or E.C. 1.1.5.3) activity, native to the yeast.

The present invention relates to a biomarker composition for diagnosing the toxicity of nanoparticles, which shows a change in expression by exposure to the nanoparticles, the biomarker composition comprising at least one gene selected from the group consisting of aldehyde dehydrogenase, glutamic-pyruvate transaminase, glutamate dehydrogenase, glutamicoxaloacetic transaminase, glutamic acid decarboxylase and glutamate-ammonia ligase, and to a method for evaluating the toxicity of nanoparticles using the same. The biomarker is a gene marker having a high correlation with the toxicity of nanoparticles, and the use of the biomarker can determine whether nanoparticles have toxicity, with high detection sensitivity. Also, the method is useful in monitoring or evaluating the toxicity of nanoparticles by analyzing factors having a high correlation with toxicity of nanoparticles. Furthermore, the method can be effectively used as a tool for studying various diseases caused by exposure to nanoparticles or evaluating the effects of nanoparticles on health.

The present invention relates to a hangover alleviating composition containing a conjugate of sesamol and a peptide as an active ingredient. Specifically, the conjugate of sesamol and a peptide according to the present invention significantly increases the activity of alcohol dehydrogenase (ADH) or aldehyde dehydrogenase (ALDH) involved in the alcohol metabolising process, quickly breaks down the concentration of alcohol in the body, and improves alcohol-induced motor impairment, thus having the advantage of being able to be usefully used as an active ingredient in a hangover alleviating composition.

The invention relates to a method for determining the activity of creatinine, and also the reagent kit for creatinine diagnosis. The reagent kit comprises cushioning solution, coenzyme, creatinine enzyme, creatinase, creatine oxidase, peroxydase, aldehyde dehydrogenase, deacidized chromogen combination, and stabilizer. By mixing sample and reagent of a predetermiend volumetric ratio, generating coupling reaction between them, subjecting the final reactant to biochemiscal analyser, the main wavelength absorbancy variance ratio (speed) can be detected, and the creatinine content can thus be measured. The method of the invention can be used to obtain the needed measurement result purely through biochemical analytic instruments, and advantages of the method include higher sensibility, better accuracy, less susceptibility to contamination of internal or external materials, and easy application.

The invention provides a construction method of a synthetic strain for generating fengycin by transforming xylose through regulating and controlling a Dahms pathway. The construction method comprises the following steps of: connecting a promoter gene P43, xylose dehydrogenase xylB, xylC, a xylosic acid lactonase gene yjhG and a 2-ketone-3-deoxyxylosic acid dehydratase gene yjhH in series to prepare a Dahms xylose pathway module into a shuttle vector pHY300PLK; meanwhile, starting from metabolite glycolaldehyde of the Dahms pathway, connecting an aldehyde dehydrogenase gene aldA, malic acid synthetase aceB, malic acid dehydrogenase mdh and the promoter P43 in series to prepare an glycolaldehyde back-complement TCA regulating and controlling module into a shuttle vector pHP13; co-expressing the two shuttle vectors in a chassis strain to construct a fengycin high-quality strain BSU02 which is synthesized by co-expressing and transforming the xylose through the Dahms module and the glycolaldehyde back-complement TCA regulating and controlling module.