263 results about "Enzyme catalyzed" patented technology

The invention relates to the technical field of biological catalysis, and discloses an L379A mutant enzyme for preparing rebaudioside I. The enzyme is obtained by the following mutations generated by UGT76G1: leucine of the 379th amino acid sequence is mutated into alanine; the enzyme can be applied to RA in-vitro conversion preparation of RI with higher utilization value, the conversion rate is higher than 50%, and the enzyme activity is remarkably improved by 7 times compared with the original enzyme catalytic conversion enzyme activity. The UGT76G1 mutant disclosed by the invention has the advantages that (1) the blank is filled, and a special enzyme catalyst capable of realizing efficient in-vitro synthesis of rebaudioside I (RI) is provided for the first time; 2) efficiency jump: the catalytic conversion rate is greatly increased from original about 7% to more than 50% (increase gt; and 3) stability and reliability: in the cross-scale reaction of 10mL to 5L, the catalyst has stable catalytic performance, shows excellent industrial application potential, and is suitable for popularization and application.

The invention provides an application of inositol monophosphate in an enzyme catalysis reaction system for preparing inositol. The invention also provides a preparation method of the inositol, the starch is used as a substrate, glucan phosphorylase, glucose phosphate mutase, inositol-3-phosphate synthase and inositol monophosphate are added as enzyme catalysts to catalyze the substrate to generate the inositol, the inositol monophosphate is derived from Archaeoglobus fulgidus, the amino acid sequence is shown as SEQ ID NO: 12, or the amino acid sequence is shown as SEQ ID NO: 1, or the amino acid sequence is shown as SEQ ID NO: 2, or the amino acid sequence is shown as SEQ ID NO: 3, or the amino acid sequence is shown as SEQ ID NO: 4, or the amino acid sequence is shown as SEQ ID NO: 5, or the amino acid sequence is shown as SEQ ID NO: 6. The inositol monophosphate is derived from Thermococcus kodakarensis, and the amino acid sequence of the inositol monophosphate is as shown in SEQ ID NO: 13; or the inositol monophosphate is derived from Pseudothermotoga lettinae, and the amino acid sequence of the inositol monophosphate is as shown in SEQ ID NO: 14. Inositol-3-phosphate synthetase and inositol monophosphate with good performance are screened, high-concentration starch is efficiently catalyzed to be converted into inositol by a one-pot method in a whole-cell feeding mode, and NAD < + > and other coenzymes do not need to be used. Under a 60L reaction system, 200g / L of corn starch is catalyzed, the unit yield of the prepared inositol reaches 161g / L, and the method has a good industrial application prospect.

The invention discloses a 7alpha-hydroxysteroid dehydrogenase mutant with improved catalytic activity as well as a coding gene and application thereof, and the amino acid sequence of the 7alpha-hydroxysteroid dehydrogenase mutant is obtained by mutation at one or more sites of the 120th site, the 195th site and the 207th site on the basis of the amino acid sequence shown in SEQ ID NO: 1. According to the 7alpha-HSDH mutant disclosed by the invention, the key site of the 7alpha-HSDH enzyme is modified, so that the mutant with higher activity than that of a wild enzyme is obtained, the efficiency bottleneck in UDCA biosynthesis is effectively broken through, and an efficient and green enzyme catalyst is provided for industrial application.

The invention discloses application of laccase as a catalyst in catalytic synthesis of allantoin. According to the invention, laccase from thermophilus is used as an enzyme catalyst, uric acid is oxidized, hydrolyzed and decarboxylated to synthesize allantoin, and efficient biosynthesis of allantoin is realized under mild conditions; wherein the amino acid sequence of the laccase derived from the thermophilic fungi is as shown in SEQ ID NO. 1. The invention provides an efficient, environment-friendly and low-cost biosynthesis approach for biosynthesis of allantoin, and has industrial application prospects in biosynthesis of allantoin.

The invention discloses a method for producing p-coumaric acid through double-enzyme cascade catalysis, which comprises the following steps: taking phenol, pyruvic acid and ammonium chloride as substrates, and carrying out cascade enzyme catalytic reaction on a tyrosine phenol lyase product and a tyrosine ammonia lyase product to synthesize p-coumaric acid. According to the method, phenol, pyruvic acid and ammonium chloride are used as substrates, a tyrosine phenol lyase product and a tyrosine ammonia lyase product are used as catalysts, the tyrosine phenol lyase product can convert the substrates into L-tyrosine, and the tyrosine ammonia lyase product can directly use the L-tyrosine as the substrate to convert the L-tyrosine into p-coumaric acid. Therefore, the tyrosine phenol lyase product and the tyrosine ammonia lyase product can realize cascade enzyme catalytic reaction in the same reactor, phenol with lower cost can be adopted as a conversion substrate, separation and purification of an intermediate product L-tyrosine are avoided, and the whole process flow is simple and efficient.

The invention relates to the technical field of biology, in particular to a purification method of ergothioneine. The invention provides a method for purifying high-purity ergothioneine from an enzyme catalytic reaction. According to the method, high-purity ergothioneine is purified from the enzyme catalysis reaction liquid, so that the purification steps are greatly simplified, and the total purification yield is increased; and only a single organic solvent ethanol is used for crystallization, so that the ergothioneine product with high purity and uniform and thick particles is obtained, and the method is suitable for large-scale production of ergothioneine.

The present invention belongs to the technical field of synthesizing and preparing organic polymer optical materials, and specifically relates to a method for preparing a pentaerythritol tetramercaptocarboxylate composition. The method comprises the following two steps: first, an addition reaction of thiourea with acrylic acid under photocatalysis to generate mercaptopropionic acid in situ; and second, a lipase-catalyzed esterification reaction of mercaptopropionic acid with pentaerythritol to obtain colorless, transparent, high-purity pentaerythritol tetramercaptocarboxylate. Simultaneously, a polymerizable modified polyurethane optical material containing the pentaerythritol tetramercaptocarboxylate is prepared, characterized by low cost, high light transmittance, and adjustable refractive index.

The invention provides a glutaminase mutant and application of the glutaminase mutant. Wherein the glutaminase mutant comprises (a) a protein which is subjected to amino acid mutation and has a glutaminase activity function on at least one of the following sites of S467, Y334, K400, N521, R337, E402 or D447 of an amino acid sequence as shown in SEQ ID NO: 2, and (b) a protein which is subjected to amino acid mutation on at least one of the following sites of S334, Y334, K400, N521, R337, E402 or D447 of the amino acid sequence as shown in SEQ ID NO: 2; and (b) a protein which has 80% or more homology with the amino acid sequence limited by (a) and has a glutaminase function. The glutaminase mutant with the amino acid sequence disclosed by the invention has relatively high specific enzyme activity during enzyme catalytic reaction, and is low in cost and strong in market competitiveness when being used for commercial food processing.

The invention relates to the technical field of catalysis, and particularly discloses a method for preparing pure biodiesel from kitchen waste oil through enzyme catalytic desulfurization. The method comprises the following steps: adding a Sm2O3 / ZrO2 solid acid catalyst into the kitchen waste oil for pretreatment to obtain pretreated waste oil, and then adding lipase into the pretreated waste oil for catalyzing transesterification to obtain the biodiesel. According to the method for preparing the pure biodiesel from the kitchen waste oil through enzyme catalytic desulfurization, in-situ esterification and synchronous desulfurization of free fatty acid can be completed in a single-step reaction, the stability of a conversion reaction is effectively improved, the production process is simplified, and the conversion efficiency of preparing the biodiesel from the kitchen waste oil is improved.

The present application relates to a kind of sulfide monooxygenase mutant and its application in esomeprazole synthesis.The sulfide monooxygenase mutant, its encoding gene, the preparation method of the recombinant expression vector containing the gene sequence, co-expression recombinant vector and recombinant expression transformant, and the application of the recombinant sulfide monooxygenase mutant catalyst in esomeprazole synthesis are specifically disclosed.Compared with other sulfide monooxygenases, the sulfide monooxygenase mutant obtained by the present application can efficiently utilize the coenzyme NADH with lower cost and higher stability to catalyze the asymmetric oxidation reaction of omeprazole sulfide, prepare esomeprazole, has the advantages of high substrate concentration, mild reaction condition, environment-friendly, simple operation, high yield, low production cost and good industrial application prospect.

The invention belongs to the technical field of organic synthesis, and particularly relates to a process for catalytically synthesizing ascorbyl tetraisopalmitate by a biological enzyme. The synthesis process comprises the following steps: attaching a biological enzyme to a metal organic framework compound material (MOFs material) to prepare biological enzyme catalyst powder, and adding a small amount of biological enzyme catalyst powder into methyl n-hexylcaprate and ascorbic acid which are used as raw materials for transesterification to prepare ascorbyl tetraisopalmitate. The process route is simple, few three wastes are generated, compared with a traditional preparation process of tetra-isopalm ascorbate, the yield and purity of the product are greatly improved, and experimental results show that the highest yield of the product is 89%, and the purity of the product reaches 99.0%.

The invention discloses a resourceful treatment process for phenol-ammonia wastewater. The process comprises the following steps: pretreating to remove oil, acid and ammonia, and recovering ammonia water; preparing a silicon-based supported phenol oxidase catalyst; carrying out enzyme catalysis polycondensation on the pretreated wastewater to generate polyphenols; residual phenol is deeply removed through electrochemical feeding of the three-dimensional electrode; after polyphenol substances are separated, supernate is subjected to biochemical treatment and is discharged after reaching the standard; and finally, carrying out dehydration, granulation, segmented pyrolysis graphitization and post-treatment on the collected polyphenol sludge to prepare the carbon negative electrode material. According to the method, deep purification of the phenol-ammonia wastewater and collaborative recycling of pollutants are achieved, toxic phenols are converted into carbon material precursors with high additional value, the recycled ammonia water can be used for desulfurization and denitrification of a boiler, and the method has the advantages of being thorough in treatment, high in resource recovery rate, low in cost and remarkable in environmental benefit.

The present invention discloses a mutant dual-enzyme catalyst, application and (S)-Bosin synthesis method, relating to the field of bioengineering technology, the present invention is based on the methylglyoxal reductase GRE2 (A) of Candida glabrata and the phosphite dehydrogenase PTDH of methylotrophic bacteria as sources for transformation, and its mutants are screened, the key residues affecting the enzymatic properties of the initial methylglyoxal reductase and phosphite dehydrogenase are determined, and methylglyoxal reductase mutants and phosphite dehydrogenase mutants with high activity are obtained. The present invention utilizes the two most efficient mutants to catalyze the reaction of preparing (S)-Bosin from β-acetone xyloside in a 22T reaction system, with good catalytic effect, overall catalytic efficiency is increased by about 43%, and cost is reduced by about 8%.

The utility model provides a continuous flow micro-reactor for a heparinase catalytic reaction, belongs to the technical field of micro-reactors, and aims to solve the problems that the replacement of immobilized heparinase needs a long time and the efficiency of the heparinase catalytic reaction is influenced. Comprising a limiting supporting base, a positioning mounting frame, a reactor main body, a positioning connecting rod, a first storage tank and a second storage tank, the positioning mounting frame is in bolted connection with the right side of the limiting supporting base; the reactor main body is fixedly connected to the left side of the positioning mounting frame; the positioning connecting rod is rotationally connected to the left side of the reactor main body, and a damper is arranged at the joint of the positioning connecting rod and the reactor main body; the first storage tank is fixedly connected to the middle part of the positioning connecting rod; the second storage tank is in bolted connection with the front side of the first storage tank; according to the utility model, the replacement efficiency of the immobilized heparinase is improved, a large amount of time is saved, and the catalytic reaction efficiency of the heparinase is improved.

The application discloses a laccase-producing polyporus brumalis and a method for preparing laccase. The application provides polyporus brumalis CCTCC NO: M 2020809 for fermenting and preparing laccase, and the amino acid sequence of the laccase is shown as SEQ ID NO: 2. The fermentation level of the laccase is high, the fermentation level in a flask reaches 980 U / mL, and the fermentation level in a 70L fermenter reaches 880 U / mL. In order to ensure the food safety of the laccase, the strain and the preferred medium components of the laccase are edible. In addition, the laccase obtained by the application can catalyze the polymerization of film-forming monomers to generate a copolymer film, and is a method for synthesizing a copolymer film by using a biological enzyme catalyst.

The invention discloses a biological catalytic synthesis method of chiral 2-amino-1-methylenepropanamide and an enzyme catalyst of the chiral 2-amino-1-methylenepropanamide. According to the present invention, one or more key amino acids in the amide hydrolase derived from Rhodococcus erythropolis AJ270 are subjected to mutation to obtain the mutant, the mutant has characteristics of high or reverse enantioselectivity when the hydrolysis reaction of the racemization 2-substituted-2-amino-1-methylene propanamide substrate is catalyzed, and the chiral compound is obtained with the high ee value; and an enantiomer of a wild type amide hydrolase catalytic product can be obtained. A method for preparing chiral 2-substituted-2-amino-1-methylene propanamide by using the mutant through biological catalysis has the characteristics of simplicity and convenience in operation, high reaction efficiency, mild reaction conditions, high enantioselectivity, easiness in product separation and high product purity, and has a very good application prospect.

The invention belongs to the technical field of biology, and particularly relates to a pentachloronitrobenzene rapid detection method based on enzyme catalysis reaction, which comprises the following steps: converting pentachloronitrobenzene into pentachlorophenol and nitrate radicals through an enzyme system consisting of iron thioflavin protein reductase, ferredoxin and nitrobenzene dioxygenase; and then nitrate radicals are specifically detected by a Griess reagent method so as to indirectly reflect quintozene. The detection method disclosed by the invention is good in specificity, short in detection time and remarkable in visual detection effect, and can be used for on-site rapid detection of quintozene.

The invention relates to water-soluble polysiloxane as well as a preparation method and application thereof. The preparation method of the water-soluble polysiloxane comprises the following steps: mixing lipase, trehalose and a surfactant to prepare modified lipase; vinyl acetate, alkoxy silane, monomethoxy polyethylene glycol and the modified lipase are mixed, and the water-soluble polysiloxane is prepared. According to the preparation method, the lipase is coated with the trehalose to form the modified lipase, so that the modified lipase can keep efficient catalytic activity for a long time at a relatively high temperature, and further the water-soluble polysiloxane can be efficiently prepared through a lipase catalytic reaction one-step method. Compared with a traditional acid / alkali synthesis method, the preparation method of the water-soluble polysiloxane can obtain a higher conversion rate at a lower reaction temperature, meanwhile, an antioxidant does not need to be added, and the obtained water-soluble polysiloxane is good in water solubility, light transmittance and safety.

The present invention relates to the preparation and use of high-entropy nanozymes with multi-pathway synergistic antibacterial effects, belonging to the field of nanozyme catalytic materials. The present invention, for the first time, utilizes a hydrothermal method and high-temperature calcination method to synthesize oxygen-vacancy-rich high-entropy oxides with haloperoxidase-like, peroxidase-like, and glutathione oxidase-like activities. These oxides can catalyze bromide ions and hydrogen peroxide to generate hypobromous acid, which interferes with bacterial quorum sensing, and hydroxyl radicals, which disrupt structure and function. Furthermore, these oxides consume glutathione, which maintains the internal redox balance of bacteria. This allows for multi-pathway synergistic and efficient bacterial damage and inactivation, helping to address the problems of existing antifouling nanozyme materials, which suffer from a single catalytic pathway and poor component adjustability. This allows for the practical expansion of high-entropy nanozyme coatings, and has potential application prospects in the field of marine biofouling.

The invention relates to the technical field of wind power materials, and discloses a bio-based matrix, a bio-based resin composite material and a preparation method and application of the bio-based matrix and the bio-based resin composite material. The bio-based resin matrix is prepared by carrying out polymerization reaction on vegetable oil under the action of an enzyme catalyst; and an enzyme catalysis-nanometer enhancement synergistic technology is used, so that the problems of high viscosity of the bio-based resin and high modulus and poor water resistance of the composite material are solved at the same time.

The invention belongs to the field of polishing solutions, and particularly relates to a green polishing solution based on an enzymatic Fenton system. The 4H-SiC substrate polishing solution comprises a component A and a component B, the effective component of the component A is an enzyme-catalyst co-immobilized abrasive material, and the enzyme-catalyst co-immobilized abrasive material comprises an abrasive material matrix, laccase and an iron-based catalyst, and the laccase and the iron-based catalyst are loaded on the abrasive material matrix; the active ingredient of the component A is a phenol substrate, the active ingredient of the component B is a phenol substrate, after the component A and the component B are mixed, laccase catalyzes oxidation of the phenol substrate to generate H2O2 in situ, the H2O2 and an iron-based catalyst are subjected to a Fenton reaction, and hydroxyl free radicals are generated at a polishing interface in situ. According to the invention, continuous, efficient and stable supply of hydroxyl radicals is ensured through enzymatic endogenous hydrogen peroxide circulation and catalyst regeneration circulation, so that the polishing solution can realize long-time stable polishing under a nearly neutral condition, and has the advantages of environmental protection, high polishing efficiency, good surface quality and the like.

The application uses cheap and easily available hexose acid as a starting material, first obtains two precursors of 2,5-furan dicarboxylic acid synthesis, namely hexahydroxy acid and 4-deoxy-5-dehydro-hexahydroxy acid through enzyme catalytic reaction, and then 4-deoxy-5-dehydro-hexahydroxy acid is dehydrated under acidic conditions to obtain 2,5-furan dicarboxylic acid.

The invention provides a method for continuously preparing an acrylamide aqueous solution by using a core-shell structure immobilized enzyme, and relates to the field of chemical engineering, the preparation method comprises the following steps: simultaneously introducing an acrylonitrile stock solution and water into a catalytic reaction unit for hydration reaction; the reaction temperature of the catalytic reaction unit is 10-20 DEG C; enabling reaction effluent to enter a primary purification unit, a deep purification unit and a terminal purification unit to obtain an acrylamide aqueous solution; wherein the catalytic reaction unit is a fixed reactor filled with a core-shell structure enzyme catalyst. The method has the advantages of few product impurities, low energy consumption and high safety.

The invention relates to a method for producing esters by reaction between a first reagent chosen from an alcohol or a carboxylic acid, contained in an aqueous solution, and at least one second reagent chosen from a carboxylic acid or an alcohol, in the presence of an enzymatic catalyst. The invention is characterised in that the reaction mixture is in the form of a Pickering emulsion comprising at least one water phase and one oil phase, said oil phase comprising at least one extraction solvent.

This invention relates to the technical field of imiquimod synthesis, specifically to catalysts, methods, and applications for imiquimod synthesis. The invention employs a lipase-immobilized lipase complex carrier to catalyze a transesterification reaction, using vinyl isobutyrate as the acyl donor and tert-butanol as the solvent. The hydroxyl group of 3-(4-amino-1H-imidazo[4,5-C]quinoline-1-yl)-2-methylpropane-1-ol is converted to an isobutyl side chain. Following enzymatic catalysis and pH adjustment, hydrolysis is performed to release the isobutyl group, further generating imiquimod and isobutyric acid. The lipase selectively catalyzes transesterification, avoiding side reactions, and the ester bond is rapidly hydrolyzed to the target product under acidic conditions.

This invention discloses a method for preparing an immobilized ketose 3-epimerase and its application, belonging to the field of immobilized enzyme preparation technology. The invention comprises the following steps: first, pretreatment of anion exchange resin; second, adsorption of the protease onto the ion exchange resin; and third, cross-linking with glutaraldehyde. The immobilized enzyme prepared by this invention is simple to prepare, inexpensive, and requires simple and mild reaction conditions. Immobilization improves the relative activity and stability of the enzyme, and the prepared immobilized enzyme is firmly bound and can undergo multiple enzyme-catalyzed reactions. This discovery has significant research value for the industrial preparation of D-allulose.

A synthesis method for a chiral epoxide catalyzed by styrene monooxygenase. The synthesis method comprises: carrying out an enzyme catalysis reaction on a raw material system comprising oxidase, an olefin compound, reductase, dehydrogenase, a hydrogen donor, FAD, and NAD+ so as to obtain a chiral epoxide. R2 and R3 are each independently selected from substituents such as H, substituted or unsubstituted C1-C6 alkyl, substituted or unsubstituted C1-C6 heteroalkyl, and a substituted or unsubstituted C2-C6 ester group; and R1 is selected from substituents such as halogen, hydroxy, carboxyl, acetoxy, and substituted or unsubstituted C1-C6 alkyl. The raw material system is used for carrying out the enzyme catalysis reaction, and the oxidase in the raw material system is used so as to obtain the chiral epoxide. The synthesis method for the chiral epoxide catalyzed by the oxidase has the advantages of a short synthesis route, a wide range of substrate types, high selectivity, mild reaction conditions, less three wastes, and low costs.

The present application relates to the technical field of polymer material chemical recycling, and in particular to a kind of nano-enzyme catalyst and process for its use in hydrothermal method degradation polycaprolactam.The nano-enzyme catalyst provided by the present application uses specific single metal or double metal combination as metal center, and is combined with specific organic ligand, can be efficiently and deeply degraded PA6 at relatively low temperature, and the catalyst can also be recycled, completely realizing the green recycling of PA6.The nano-enzyme catalyst provided by the present application can make the conversion rate of PA6 molecule reach 100% using hydrothermal method, and the caprolactam yield can be stably above 94%, avoiding the use of organic solvent with high toxicity, and realizing the whole green recycling from " waste containing PA6" to " renewable caprolactam monomer".

The invention discloses a method for rapidly detecting acrylamide in food by using a fluorescent probe, which comprises the following steps of: synthesizing copper and iron-containing phosphomolybdic acid nano-enzyme (Cu, Fe-PMos) with peroxidase-like nano-enzyme activity by using phosphomolybdic acid, copper chloride and ferric chloride as precursors through a microwave method, catalyzing xanthol to react with HCl to generate a fluorescent derivative by using the Cu and Fe-PMos, and detecting the acrylamide in the food by using the fluorescent probe. When acrylamide is added into a fluorescent system, reaction of xanthene alcohol and acrylamide is carried out to generate a xanthene acrylamide fluorescent substance, reaction of Cu, Fe-PMos and xanthene alcohol is inhibited, and the fluorescence intensity of the system is reduced, so that a fluorescent probe rapid detection method of acrylamide is established. Other coexisting substances do not interfere with each other, the detection limit reaches 0.01 mu g / mL, and the method has the characteristics of high sensitivity, strong specificity, simplicity and rapidness in operation and the like.

The present application relates to the technical field of genetic engineering, and particularly provides a Diels-Alder reaction enzyme mutant as well as a preparation method and application thereof. The present application relates to functional modification and strengthening of a Diels-Alder (D-A) reaction enzyme MaDA1 derived from mulberry, so that the enzyme catalyzes intermolecular D-A reaction of a non-natural dienophile containing a ''handle group'' (carboxyl, ester or a precursor thereof) and various dienophiles, so that further modification of the enzymatic D-A product can be realized through decarboxylation functionalization reaction, and diversification and stereoselective synthesis of a cyclohexene skeleton structure are realized.