71 results about "Formaldehyde dehydrogenase" patented technology

Patients needing NO donor therapy or inhibition of pathologically proliferating cells or increased NO bioactivity are treated with a therapeutically effective amount of an inhibitor of glutathione-dependent formaldehyde dehydrogenase.

The present invention provides novel glutathione-dependent formaldehyde dehydrogenase that makes possible quantitative measurement of formaldehyde by cycling reaction, and a determination method of formaldehyde and biological components, such as creatinine, creatine, homocysteine and the like, which produces formaldehyde as a reaction intermediate. In addition, the present invention provides a reagent kit for the above-mentioned determination method. The present invention provides a novel determination method of a homocysteine using transferase utilizing homocysteine and other compound as a pair of substrates. Particularly, the present invention provides a determination method of homocysteine which includes bringing betaine-homocysteine methyltransferase and dimethylglycine oxidase into contact with a sample and measuring produced hydrogen peroxide or formaldehyde. Moreover, the present invention provides novel dimethylglycine oxidase stable to thiol compound, which is suitably used for the measurement. The present invention provides a reagent kit used for any of the above-mentioned determination methods of homocysteines.

The invention discloses a formaldehyde biodegradation agent and a preparation method thereof, relates to the biodegradation agent and provides a pseudomonad, namely IOFA1, as well as the formaldehyde biodegradation agent and the preparation method thereof. The formaldehyde biodegradation agent is dry powder of pseudomonad IOFA1 thallus breaking solution. The formaldehyde biodegradation agent adopts formaldehyde dehydrogenase as a main component. The preparation method comprises the following steps: activating the pseudomonad IOFA1 by using a culture medium, inoculating the pseudomonad IOFA1 into the culture medium, and performing shaking culture; adding formaldehyde solution into the culture medium, and continuing performing the shaking culture; performing centrifugation on culture solution at the temperature of 4 DEG C, removing supernatant liquid and collecting thalli; adding 100ml of sterile water into the thalli to suspend the thalli, and collecting suspension; and performing the centrifugation after breaking the thalli in the suspension, removing precipitate, filtering the supernatant liquid for removing bacteria, performing freeze-drying to get the dry powder of the pseudomonad IOFA1 thallus breaking solution, and further performing purification to get the formaldehyde biodegradation agent.

Patients needing NO donor therapy or inhibition of pathologically proliferating cells or increased NO bioactivity are treated with a therapeutically effective amount of an inhibitor of glutathione-dependent formaldehyde dehydrogenase.

The present invention provides bioactive hollow nano-fibers and hollow microcapsules for efficiently catalyzing methanol synthesis through CO2. According to the present invention, a coaxial co-spinning technology is used to embed three enzymes for catalyzing methanol synthesis through CO2 and comprising formic dehydrogenase, formaldehyde dehydrogenase and ethanol dehydrogenase, and coenzyme NADH into the chamber of polyelectrolyte-doped hollow nano-fibers or hollow microcapsules; in order to achieve coenzyme regeneration, an oxidation reduction enzyme R adopting NAD<+> as coenzyme is embedded into the chamber; in order to accelerate a CO2 hydration reaction, carbonic anhydrase is immobilized on the outer surface of the hollow nano-fibers or hollow microcapsules through a layer-by-layer self-assembly technology; the small molecule NADH is bound on the inner wall of the hollow nano-fibers or hollow microcapsules through the electrostatic interaction between the NADH and the polyelectrolyte in the shell layer so as to achieve the recycling; and the polyelectrolyte-doped hollow nano-fiber or hollow microcapsule CO2 conversion catalyst has advantages of simple preparation, high conversion rate, and high stability, and provides wide application prospects in the field of the conversion of CO2 into methanol.

The invention discloses a method for producing L-2-aminobutyric acid by double immobilized multi-enzyme systems. The method provided by the invention comprises the following steps that 1, threonine dehydrogenase and leucine dehydrogenase are fixed on reversely-dissoluble pH-sensitive polymer carriers so that a co-immobilized multi-enzyme system is obtained; and 2, alcohol oxidase, formaldehyde dehydrogenase and formate dehydrogenlyase are fixed on reversely-dissoluble pH-sensitive polymer carriers so that a co-immobilized coenzyme regeneration system is obtained. The method for producing L-2-aminobutyric acid by the double immobilized multi-enzyme systems utilizes dissolution reversibility of co-immobilized enzymes, realizes effective separation of the co-immobilized enzymes and products, improves accessibility between the co-immobilized enzymes and reactants, improves recovery and utilization rates of threonine dehydrogenase, leucine dehydrogenase, alcohol oxidase, formaldehyde dehydrogenase and formate dehydrogenlyase, improves coenzyme regeneration efficiency, reduces follow-up separation purification processes, simplifies a process flow and reduces a production cost.

The invention discloses a method for detecting TMAO (trimethylamine oxide) by an enzyme method and application thereof. The detection method utilizes a multi-enzyme combination system containing TMAOTDM (demethylase), FADH (formaldehyde dehydrogenase), FDH (formate dehydrogenase) and diaphorase, so as to perform fluorescence determining on the TMAO; the method can be used for developing a TMAO detection kit. The method for detecting the TMAO by the enzyme method has the advantages that the defect of failure to directly determine based on dehydrogenase and diaphorase coupling because of no participation of NAD dependence dehydrogenase in the metabolism path of the TMAO is overcome; by adopting the multi-enzyme coupling of TDM-FADH-FDH-diaphorase, the system for fluorescence determining ofthe TMAO is constructed, and one TMAO molecule is decomposed into two fluorescence signals; the sensitivity is high, the detection is rapid and stable, the repeatability is good, the operation is simple and convenient, and the cost is lower.

The invention discloses a formaldehyde removing agent of biological enzyme. The formaldehyde removing agent of biological enzyme is prepared from the following components by weight percentage: 1 to 2% of biological enzyme composition, 1 to 3% of plant extract, 0.5 to 1% of protective agent, 1 to 2% of buffering agent, 0.1 to 0.3% of preservative, 0.1 to 0.3% of essence, the balance of water; thebiological enzyme is formaldehyde dehydrogenase, polyphenol oxidase and superoxide dismutase. The formaldehyde removing agent of biological enzyme is safe and non-toxic, harmless to humans and animals, and biodegradable and does not cause secondary pollution. The formaldehyde removing agent of biological enzyme is mainly used in indoor living environment and car to remove formaldehyde, can greatlyreduce the formaldehyde produced by furniture, leather, blankets and the like, and also has an effect of reducing benzene pollutants. The formaldehyde removing agent of biological enzyme has a long-lasting effect and has no corrosive effect on the surface of a treated object.

The invention relates to a reagent (kit) for measuring formaldehyde by using an enzyme colorimetric method as well as a method for measuring the concentration of the formaldehyde, and composition and ingredients of the reagent, belonging to the technical field of food / environmental test. The reagent (kit) comprises the main ingredients of buffer solution, coenzyme, formaldehyde dehydrogenase and stabilizing agent. The concentration of the formaldehyde is measured by mixing a sample and the reagent according a certain volume ratio to carry out a series of enzymatic reaction, placing the reactant under an ultraviolet / visible light analyzer and detecting the ascending degree of absorbance at a dominant wavelength of 340nm.

The invention provides a bio-enzyme catalytic and absorptive nutrient solution. The bio-enzyme catalytic and absorptive nutrient solution is characterized by comprising ammonium phosphate, ammonium ferrous sulfate, potassium dihydrogen phosphate, boric acid, potassium chloride, potassium permanganate, disodium hydrogen phosphate, plant extract solution and water, wherein the plant extract solution contains aloe extract solution, scindapsus aureus extract solution, chlorophytum comosum extract solution, peppermint extract solution and the water. The bio-enzyme catalytic and absorptive nutrient solution provided by the invention is non-toxic and odorless, a specific microorganism and formaldehyde dehydrogenase can be produced under the culture of the nutrient solution, and formaldehyde in the air and other indoor pollutants can be biologically and catalytically oxidized and converted into nutrient substance and energy of the microorganism itself, and secondary pollution is not brought to the environment, so the bio-enzyme catalytic and absorptive nutrient solution is an ideal indoor air purification material. In addition, the bio-enzyme catalytic and absorptive nutrient solution also can be used for promoting the growth of plant and fish. Therefore, the bio-enzyme catalytic and absorptive nutrient solution is wide in application range and low in cost, and is an environment-friendly product.

The invention belongs to biological technical field and relates to the improvement technology and the application of the expression system of existing pichia pastoris. Based on the metabolic pathway and the inherited characteristics of pichia pastoris carbon source and nitrogen source, and the clone and analysis to the formaldehyde dehydrogenase 1(FLD1) PFLD1 promoter gene which can be expressed under the induction of non-toxic nitrogen source nutrient such as choline, the invention provides a pichia pastoris expression vector whose promoter is a formaldehyde dehydrogenase promoter, the preparation method and the application as well as the corresponding expression system and the application of the expression system. The expression vector or expression system of the invention can take non-toxic choline nitrogen source as inducer when expressing foreign protein, with nearly the same foreign protein expression efficiency as taking toxic methanol as inducer. The green and safe expression system which does not use toxic inducer can be applied to produce genetic engineering food and pharmaceutical genetic engineering products.

The invention discloses a creatinine measurement reagent which comprises a reagent I and a reagent II, wherein the reagent I comprises 10-200mmol / L Good's buffering solution with the PH of 7.0-9.0, 5-120KU / L creatine amidine hydrolase, 2-50KU / L sarcosine oxidase, 1-10ml / L surfactant, 1-100mmol / L stabilizing agent and 0.1-50ml / l preservative; the reagent II comprises 10-200mmol / L Good's buffering solution with the PH of 7.0-9.0, 0.1-5mml / L NAD<+>, 3-200KU / L creatinine amidohydrolase, 1-50KU / L formaldehyde dehydrogenase, 1-10ml / L surfactant, 1-100mmol / L stabilizing agent and 0.1-50ml / l preservative. According to the creatinine measurement reagent disclosed by the invention, the problem of interference is solved; and the reagent components are stable.

The invention relates to a plant expression vector pH2-35S-PrbcS-adh of arabidopsis glutathione-dependent formaldehyde dehydrogenase gene, which is the plant expression vector of light-induced promoter (PrbcS) containing tomato Rubisco 3C small subunit gene and the arabidopsis glutathione-dependent formaldehyde dehydrogenase (FALDH) gene adh. The gene adh is amplified from arabidopsis, and the over expression of the gene adh in tobacco lamina cytoplasm is controlled by the light-induced promoter, so that the efficiency of decomposing formaldehyde by tobacco cell can be improved, thus enhancing the capability of absorbing and enduring exogenous formaldehyde by plant. The experiment proves that enzyme activity of adh transgenic tobacco FALDH is increased by about 3-5 times compared with that of wild type; after being cultured for 30 days on an MS solid culture medium containing 10mmol / L of formaldehyde, the growing situation of the adh transgenic tobacco is obviously superior to that of wild type. In addition, when 2mM formaldehyde liquid is used for treating the plant, the formaldehyde absorption rate of the adh transgenic tobacco is obviously higher than that of wild type.

The invention provides a bioenzyme formaldehyde remover and a preparation method and relates to the field of formaldehyde. The bioenzyme formaldehyde remover comprises, by weight, 5-10 parts of soybean protein, 0.5-2 parts of bioenzymes, 3-5 parts of bacillus subtilis, 1-3 parts of pseudomonas amygdala, 3-5 parts of citrobacter, 1-3 parts of alcaligenes faecalis, 3-5 parts of plant extracts, 1-3 parts of tea polyphenol, 0.5-2 parts of citric acid, 1-2 parts of protective agent and 0.2-1 part of active agent, the bioenzymes include formaldehyde dehydrogenase, polyphenol oxidase, protease and polysaccharide hydrolase, and the plant extracts include aloe extract, ivy extract, maguey extract and dayflower extract. Various microorganisms, the bioenzymes and the plant extracts are adopted to jointly act to remove formaldehyde, so that removal effect is improved; the bioenzyme formaldehyde remover is safe and nonhazardous.

The invention relates to a reagent (kit) for measuring formaldehyde by using an enzyme-multiplied method, an enzyme colorimetric method and an enzyme coupling method as well as a method for measuring the concentration of the formaldehyde, and composition and ingredients of the reagent, belonging to the technical field of food / environmental test. The reagent (kit) comprises the main ingredients of buffer solution, coenzyme, formaldehyde dehydrogenase, hydrogenlyase and stabilizing agent. The concentration of the formaldehyde is measured by mixing a sample and the reagent according to a certain volume ratio to carry out a series of enzymatic reaction, placing the reactant under an ultraviolet / visible light analyzer and detecting the ascending degree of absorbance at a dominant wavelength of 340nm.

The invention provides a formaldehyde removal coating and a preparation method thereof, and relates to the field of formaldehyde treatment. The formaldehyde removal coating comprises the following components in parts by weight: 5-10 parts of an activated carbon loaded nano TiO2 material, 3-5 parts of chitosan, 3-5 parts of rosin resin, 0.1-1 part of nano graphene, 5-10 parts of lignin, 1-5 parts of a plant extract, 1-5 parts of light calcium, 0.2-2 parts of biological enzyme, 30-50 parts of silicone acrylic emulsion, 0.05-1 part of a coalescing agent, 0.05-1 part of a defoaming agent, 0.05-1 part of a dispersing agent and 20-40 parts of water, the biological enzyme comprises peroxidase, formaldehyde dehydrogenase and polyphenol oxidase, wherein the plant extract is an aloe extract, a Chinese ivy extract, an Agave americana extract and a dayflower extract. Through use of the formaldehyde removal coating, formaldehyde is removed in a manner of combining physical adsorption, chemical catalysis, the biological enzyme and the plant extracts, the removal effect is improved, and the formaldehyde removal coating is safe, non-toxic and harmless.

The invention discloses a formaldehyde biodegradation agent and a preparation method thereof, relates to the biodegradation agent and provides a pseudomonad, namely IOFA1, as well as the formaldehyde biodegradation agent and the preparation method thereof. The formaldehyde biodegradation agent is dry powder of pseudomonad IOFA1 thallus breaking solution. The formaldehyde biodegradation agent adopts formaldehyde dehydrogenase as a main component. The preparation method comprises the following steps: activating the pseudomonad IOFA1 by using a culture medium, inoculating the pseudomonad IOFA1 into the culture medium, and performing shaking culture; adding formaldehyde solution into the culture medium, and continuing performing the shaking culture; performing centrifugation on culture solution at the temperature of 4 DEG C, removing supernatant liquid and collecting thalli; adding 100ml of sterile water into the thalli to suspend the thalli, and collecting suspension; and performing the centrifugation after breaking the thalli in the suspension, removing precipitate, filtering the supernatant liquid for removing bacteria, performing freeze-drying to get the dry powder of the pseudomonad IOFA1 thallus breaking solution, and further performing purification to get the formaldehyde biodegradation agent.

The invention discloses a method for preparing enzyme through coexpression of recombinant protease and molecular chaperone. In the method, recombinant plasmids for encoding formaldehyde dehydrogenase and formaldehyde superoxide dismutase are respectively converted into expression strains containing molecular chaperone coexpression plasmids, so that protease and the molecular chaperone are co-expressed and soluble recombinant expression of the protease (comprising histidine tag or not comprising the histidine tag) is achieved. The formaldehyde dehydrogenase, the formaldehyde superoxide dismutase and the histidine tag are subjected to fusion expression, soluble recombinant protein is subjected to affinity purification by the histidine tag to form the protein with the purity of over 90 percent, and about 1 milligram of protease can be obtained when 1 gram of thalli are obtained averagely. An enterokinase cutting sequence is introduced between the histidine tag and the protease, the tag can be removed through enzyme cutting, and amino acid carrier residue is absent. By the method, the soluble expression of the protease in an Escherichia coli expression system can be promoted, and massive recombinant protease can be efficiently prepared through purification.

The invention relates to the field of plant gene engineering and especially relates to a use of a bracketplant formaldehyde dehydrogenase gene and a plant expression vector in formaldehyde purifying plant cultivation. Through separation and function identification of the bracketplant gene FADLH, use of the gene CcFADLH in formaldehyde absorption and metabolism of plants is ensured. The invention discloses a formaldehyde dehydrogenase gene nucleotide sequence and a protein amino acid sequence coded by the formaldehyde dehydrogenase gene nucleotide sequence. The gene CcFADLH has full length of 1140bp and can code a protein comprising 379 amino acid residues. An experiment proves that the gene can improve a formaldehyde absorption rate of gloxinia. The gene has a wide application prospect and a large economic value in improvement of an indoor formaldehyde purification capability of ornamental plants based on gene engineering.

The invention relates to a reagent (kit) for measuring formaldehyde by using an enzyme-multiplied method, an enzyme colorimetric method and an enzyme coupling method as well as a method for measuring the concentration of the formaldehyde, and composition and ingredients of the reagent, belonging to the technical field of food / environmental test. The reagent (kit) comprises the main ingredients of buffer solution, coenzyme, ferricytochrome, catechol, magnesium chloride, formaldehyde dehydrogenase, hydrogenlyase, chlorobenzoic acid-1,2-dioxygenase and stabilizing agent. The concentration of the formaldehyde is measured by mixing a sample and the reagent according to a certain volume ratio to carry out a series of enzymatic reaction, placing the reactant under an ultraviolet / visible light analyzer and detecting the ascending degree of absorbance at a dominant wavelength of 340nm.

The invention relates to a method for guiding the expression of major capsid proteins L1 of HPV16 (human papilloma virus 16) in pichia pastoris by using a formaldehyde dehydrogenase promoter, wherein the expression of major capsid proteins L1 of HPV16 is controlled by a pichia pastoris formaldehyde dehydrogenase promoter. The method disclosed by the invention mainly comprises the following steps: i) building a pichia pastoris expression vector guided by a pichia pastoris formaldehyde dehydrogenase promoter; and ii) under the guidance of the formaldehyde dehydrogenase promoter, expressing the major capsid proteins L1 of HPV16 in different carbon / nitrogen source combined culture media. According to the invention, based on a pichia pastoris expression system, and starting with the regulating characteristics of the formaldehyde dehydrogenase promoter, the optimized expression of major capsid proteins L1 of HPV16 is implemented in the different carbon / nitrogen source combined culture media according to the characteristics of the promoter, so that the efficient expression of the major capsid proteins L1 of HPV16 is realized, thereby obtaining a low-cost virus-like particle preparation technology and implementing the low-cost preparation of human papilloma virus vaccines.

The invention relates to a reagent (kit) for measuring formaldehyde by using an enzyme triple multiplied method, an enzyme colorimetric method and an enzyme coupling method as well as a method for measuring the concentration of the formaldehyde, and composition and ingredients of the reagent, belonging to the technical field of food / environmental test. The reagent (kit) comprises the main ingredients of buffer solution, coenzyme, catechol, magnesium chloride, formaldehyde dehydrogenase, hydrogenlyase, chlorobenzoic acid-1,2-dioxygenase and stabilizing agent. The concentration of the formaldehyde is measured by mixing a sample and the reagent according to a certain volume ratio to carry out a series of enzymatic reaction, placing the reactant under an ultraviolet / visible light analyzer and detecting the ascending degree of absorbance at a dominant wavelength of 340nm.

The invention relates to a reagent (kit) for measuring formaldehyde by using an enzyme-multiplied method, an enzyme colorimetric method and an enzyme coupling method as well as a method for measuring the concentration of the formaldehyde, and composition and ingredients of the reagent, belonging to the technical field of food / environmental test. The reagent (kit) comprises the main ingredients of buffer solution, coenzyme, acetyl-coenzyme A, pyruvic acid, formaldehyde dehydrogenase, formic acid C-acetylase, pyruvate dehydrogenase and stabilizing agent. The concentration of the formaldehyde is measured by mixing a sample and the reagent according to a certain volume ratio to carry out a series of enzymatic reaction, placing the reactant under an ultraviolet / visible light analyzer and detecting the ascending degree of absorbance at a dominant wavelength of 340nm.

The invention relates to a reagent (kit) for measuring formaldehyde by using an enzyme-multiplied method, an enzyme colorimetric method and an enzyme coupling method as well as a method for measuring the concentration of the formaldehyde, and composition and ingredients of the reagent, belonging to the technical field of food / environmental test. The reagent (kit) comprises the main ingredients of buffer solution, coenzyme, acetyl-coenzyme A, 3-formyl acetic acid, formaldehyde dehydrogenase, formic acid C-acetylase, malonic acid-succinate semialdehyde dehydrogenase and stabilizing agent. The concentration of the formaldehyde is measured by mixing a sample and the reagent according to a certain volume ratio to carry out a series of enzymatic reaction, placing the reactant under an ultraviolet / visible light analyzer and detecting the ascending degree of absorbance at a dominant wavelength of 340nm.

The invention relates to a reagent (kit) for measuring formaldehyde by using an enzyme-multiplied method, an enzyme colorimetric method and an enzyme coupling method as well as a method for measuring the concentration of the formaldehyde, and composition and ingredients of the reagent, belonging to the technical field of food / environmental test. The reagent (kit) comprises the main ingredients of buffer solution, coenzyme, adenosine triphosphoric acid, tetrahydrofolic acid, glyceric aldehyde-3-phosphoric acid, formaldehyde dehydrogenase, formic acid-dihydrofolic acid ligase, glyceric aldehyde-3-glycerol phosphate dehydrogenase and stabilizing agent. The concentration of the formaldehyde is measured by mixing a sample and the reagent according to a certain volume ratio to carry out a series of enzymatic reaction, placing the reactant under an ultraviolet / visible light analyzer and detecting the ascending degree of absorbance at a dominant wavelength of 340nm.

The invention relates to an enzyme biosensor for detecting a formaldehyde gas. The enzyme biosensor which adopts the high catalytic activity and the high specificity of an enzyme and a microporous polytetrafluoroethylene membrane to acquire is used to detect and monitor the concentration of the trace formaldehyde gas. The formaldehyde gas which permeates the microporous membrane and foamed carbon to enter a sensor reaction chamber transmits electrons in the foamed carbon electrode through NAD<+> and benzoquinone under the catalysis of a formaldehyde dehydrogenase, so the concentration of the formaldehyde gas can be measured through the current detection. The sensor of the invention, which has the characteristics of simple structure, high sensitivity and difficult influence by other gases, is suitable for the medical examination and the continuous monitoring of indoor formaldehyde pollution.

The invention relates to a reagent (kit) for measuring formaldehyde by using an enzyme triple multiplied method, an enzyme colorimetric method and an enzyme coupling method as well as a method for measuring the concentration of the formaldehyde, and composition and ingredients of the reagent, belonging to the technical field of food / environmental test. The reagent (kit) comprises the main ingredients of buffer solution, coenzyme, acetaldehyde, coenzyme A, formaldehyde dehydrogenase, lactic acid aldolase, lactic dehydrogenase, pyruvate dehydrogenase and stabilizing agent. The concentration of the formaldehyde is measured by mixing a sample and the reagent according to a certain volume ratio to carry out a series of enzymatic reaction, placing the reactant under an ultraviolet / visible light analyzer and detecting the ascending degree of absorbance at a dominant wavelength of 340nm.

The invention relates to a reagent (kit) for measuring formaldehyde by using an enzyme-multiplied method, an enzyme colorimetric method and an enzyme coupling method as well as a method for measuring the concentration of the formaldehyde, and composition and ingredients of the reagent, belonging to the technical field of food / environmental test. The reagent (kit) comprises the main ingredients of buffer solution, coenzyme, acetyl-coenzyme A, formaldehyde dehydrogenase, formic acid C-acetylase, coenzyme A-disulfide reducase and stabilizing agent. The concentration of the formaldehyde is measured by mixing a sample and the reagent according to a certain volume ratio to carry out a series of enzymatic reaction, placing the reactant under an ultraviolet / visible light analyzer and detecting the ascending degree of absorbance at a dominant wavelength of 340nm.

The present invention provides formaldehyde dehydrogenase genes (FLD) from methylotrophic yeasts. The FLD structural genes confer resistance to formaldehyde and are therefore useful as a selectable marker in methylotrophic yeasts. The FLD promoter sequences are strongly and independently induced by either methanol as sole carbon source (with ammonium sulfate as nitrogen source) or methylamine as sole nitrogen source (with glucose as carbon source). Induction under either methanol, methylamine or both provides levels of heterologous gene expression comparable to those obtained with the commonly used alcohol oxidase I gene promoter (PAOX1). The FLD promoter of Pichia pastoris (PFLD1) is an attractive alternative to PAOX1 for expression of foreign genes in P. pastoris, allowing regulation by carbon (methanol) or nitrogen (methylamine) source within the same expression strain. Yeast strains, expression cassettes, expression vectors, and host cells comprising an FLD gene promoter and 3′ termination sequence are also provided.