707 results about "Enzyme catalysis" patented technology

The invention discloses a high-performance carbonyl reductase mutant and application thereof in synthesis of a series of chiral alcohols. The high-performance carbonyl reductase mutant is obtained by performing the following mutations on an amino acid sequence as shown in SEQ ID NO.2: the 69th alanine mutates into any one of lysine, leucine, aspartic acid or asparagine, and the 69th alanine mutates into any one of lysine, leucine, aspartic acid or asparagine; and / or the 100th glycine is mutated into any one of glutamic acid, serine, lysine or asparagine. Compared with a wild type enzyme, the thermal stability and the catalytic activity of the obtained mutant are remarkably improved, particularly, single point mutants Mut-A69N, Mut-G100E and Mut-G100N and a combined mutant Mut-A69N-G100N show excellent relative enzyme activity, thermal stability and substrate tolerance. The mutant has high catalytic activity and stability to various chiral alcohols, and the contradiction that the traditional carbonyl reductase is easy to inactivate at high temperature and the catalytic efficiency is difficult to achieve at the same time is solved. The invention provides an efficient and stable enzyme catalysis tool for green biological preparation of chiral drug intermediates.

The present disclosure describes a Pseudococcus preparation and a preparation method and application thereof, the Pseudococcus preparation comprises an active ingredient, the active ingredient comprises a specific pro-inflammatory regression mediator (SPMs) and a pro-inflammatory regression mediator (PRMs), the specific proinflammatory regression medium and the proinflammatory regression medium are generated by catalyzing unsaturated fatty acid synthesized by micrococcus by own enzyme. According to the invention, the invention can provide the micrococcus preparation containing the specific proinflammatory regression medium and the proinflammatory regression medium as well as the preparation method and the application of the micrococcus preparation.

The invention belongs to the technical field of engineered probiotics, and particularly relates to engineered probiotics for radiosensitization and tumor metabolism regulation as well as a preparation method and application of the engineered probiotics. The engineering probiotics comprise probiotics and core-shell type metal nanoparticles which are loaded on the probiotics and are synthesized through a biological directional mineralization effect; the core of the core-shell type metal nanoparticle is a palladium element, and the outer layer of the core-shell type metal nanoparticle is a palladium element and a gold element. The engineering probiotics provided by the invention have excellent enzyme catalysis performance and can target and retain in tumor sites, and through the synergistic effect of all components in the engineering probiotics, adenosine metabolism is effectively inhibited, secretion of pro-inflammatory cytokines is enhanced, tumor microenvironment is promoted to be converted into an inflammatory state, up-regulation of immune checkpoints is inhibited, and the immune checkpoints are inhibited. And T cells are inhibited from being transformed into depletion phenotype and transformed into effect type from depletion type. After the SBRT and the immune checkpoint inhibitor are combined for use, the growth of tumors can be effectively inhibited, and the effect of enhancing immune radiotherapy is achieved.

The invention discloses an endoglucanase truncated mutant and an application of the endoglucanase truncated mutant. According to the invention, based on endoglucanase BsEGL from bacillus subtilis DLG, a truncated mutant is constructed by deleting a carbohydrate binding domain (CBM) of the endoglucanase BsEGL, and the truncated mutant is named as BsEGL [delta] CBM. Compared with BsEGL, the truncated mutant BsEGL delta CBM has the advantages that the thermal stability, the pH stability, the organic solvent tolerance and the like are remarkably improved, and the activity of degrading phosphoric acid expanded cellulose and corncob xylan is obtained. In addition, the enzymatic activity of the truncated mutant BsEGL delta CBM is remarkably improved by 6.41%, and the catalytic efficiency is remarkably improved. Due to the characteristics, the mutant can be suitable for industrial processes such as feed processing, papermaking, biological energy sources, spinning and food brewing, and is particularly suitable for enzyme catalytic reaction under extreme environments such as high temperature and low pH. The invention provides an enzyme preparation tool with excellent performance for efficient degradation of cellulose biomass, and has important application value.

The application discloses a galactosyltransferase mutant and application thereof in preparation of flavonoid compounds, and belongs to the technical field of enzymology. The application provides a UDP-galactosyltransferase mutant, which is obtained by site-directed mutation of one amino acid in the amino acid sequence of wild-type galactosyltransferase VcUFGT into alanine (A). The effects of a series of mutants H82A, V139A, G141A, P186A, N245A, V282A and S307A are verified in the examples, the mutants can perform enzyme catalysis reaction with quercetin and UDP-galactoside as substrates, and generate flavonoid compound hyperoside, and the specific enzyme activity of the mutants is more than 1.5 times that of the wild type, thereby providing an effective application basis for biosynthesis of flavonoid compounds.

The invention provides a carbonyl reductase mutant and application thereof in preparation of chiral alcohol compounds, and belongs to the technical field of gene engineering and enzyme catalysis. According to the invention, on the basis of the wild carbonyl reductase, the mutant with activity obviously superior to that of the wild carbonyl reductase is obtained through specific mutation, the selectivity and stability of the enzyme are improved, and the mutant has a wide application prospect in catalytic synthesis of chiral alcohol compounds.

The present application relates to the technical field of biocatalysis and biosynthesis, and specifically discloses a blue pigment and a biosynthesis method thereof. In the present application, an indigoidine synthetase and a 4′-phosphopantetheinyl transferase are expressed by a metabolically engineered strain to catalyze the biosynthesis of the blue pigment N-acetyl-indigoidine from glutamine and N-acetylglutamine, and a molecular structure of the blue pigment is inferred by mass spectrometry, nuclear magnetic resonance spectroscopy, etc. The present application achieves the catalytic synthesis of N-acetyl-indigoidine from glutamine and N-acetylglutamine in Escherichia coli (E. coli), Corynebacterium glutamicum (C. glutamicum), Saccharomyces cerevisiae (S. cerevisiae), and Streptomyces. Compared with indigoidine, N-acetyl-indigoidine has a maximum absorption wavelength of 584 nm, and a stable color having high brightness that is not easy to fade. Thus, the blue pigment shows an extensive application range and a promising industrial production prospect.

The invention provides a saccharomyces cerevisiae engineering strain HYB05 capable of releasing astaxanthin in a controllable self-splitting manner. The saccharomyces cerevisiae engineering strain HYB05 is constructed by taking a basic strain for producing astaxanthin as a starting strain, introducing a coding sequence comprising cell wall lyase Lyc, a coding sequence of a signal peptide mutant F8A and a recombinant nucleic acid construct for expressing a regulatory element, and knocking out an SSD1 gene to relieve a translation inhibition effect. The cell wall lyase Lyc is found and disclosed by the inventor for the first time, and the amino acid sequence is shown as SEQ ID NO: 6; the amino acid sequence of the signal peptide mutant F8A is as shown in SEQ ID NO: 8. According to the engineering strain HYB05, by introducing the recombinant nucleic acid construct, the activation of the catalytic activity of cell wall lyase under specific conditions is realized, so that the cell wall of the saccharomyces cerevisiae is broken, and the astaxanthin synthesized by the saccharomyces cerevisiae is released. Compared with the prior art, the astaxanthin is produced through fermentation of the strain, the extraction steps are simplified, extraction of the astaxanthin in the yeast is achieved to the maximum extent, the yield of the astaxanthin is remarkably increased, and the technical effect is remarkable.

The invention discloses a method for synthesizing ceramide NP through two-step enzyme catalysis, which comprises the following steps of: firstly, adding lipase into vegetable oil to catalyze and combine fatty acid to decompose into free fatty acid, and centrifuging to remove the lipase; a small amount of phytosphingosine is added into the hydrolyzed vegetable oil, the raw material vegetable oil is used as a solvent or a squalane system solvent for incubation, and then immobilized lipase is added for catalytic synthesis of ceramide. The invention establishes a two-enzyme method for efficiently synthesizing the ceramide NP compound, and the process is natural, environment-friendly and non-toxic. The reaction conditions are optimized through response surface analysis, meanwhile, the immobilized lipase shows excellent cycle performance, and the method is easy to operate, environmentally friendly, green and economical and has wide application prospects in the fields of cosmetics, health care products, biological medicine and the like.

The invention discloses an enzyme catalytic synthesis method of a luliconazole chiral intermediate, which comprises the following steps: adding a recombinant escherichia coli wet cell for expressing alcohol dehydrogenase, a recombinant escherichia coli wet cell for expressing formate dehydrogenase, a buffer solution, a substrate, a cosolvent, ammonium formate and a coenzyme into a reaction container, reacting at 25-35 DEG C for 2-24 hours, extracting, separating, and carrying out rotary evaporation, thereby obtaining the luliconazole chiral intermediate. The luliconazole chiral intermediate is obtained; the substrate is 2, 2 ', 4'-trichloroacetophenone; the alcohol dehydrogenase is a mutant of AKR3. The method is mild in reaction condition, environmentally friendly, high in regioselectivity and stereoselectivity, high in conversion rate, high in chiral purity, small in enzyme dosage, low in preparation cost and suitable for industrial production.

The invention belongs to the technical field of drug delivery systems, and discloses a two-dimensional vermiculite-based drug delivery system and a preparation method and application thereof. The preparation method comprises the following steps: carrying out ion exchange on expanded vermiculite, NaCl and LiCl, stripping by using a mechanical stripping sheet, centrifuging to obtain a two-dimensional vermiculite nanosheet dispersion liquid, dispersing a drug in the two-dimensional vermiculite nanosheet dispersion liquid, and forming a film to obtain the two-dimensional vermiculite-based drug delivery unit. The drug is synergistically loaded between layers and on the surface of the vermiculite; rich hydroxyl groups and interlayer cations on the end surface of the vermiculite interact with the drug, so that the drug release time is relatively long; the vermiculite-based drug delivery system can realize gradient order release of drugs according to a sequence from the surface to the interlayer through pH response of an affected part. Meanwhile, the vermiculite-based drug delivery system provides an antibacterial effect through enzyme-like catalytic activity, and avoids the problems of abuse of antibiotics and drug resistance.

The present application relates to a pyridoxal kinase mutant, a recombinant expression vector and a microbial cell and their applications, and belongs to the technical field of biological catalysis. In order to solve the problem of low product concentration in existing enzyme catalysis, a pyridoxal kinase mutant is provided, the amino acid sequence is selected from the amino acid sequence shown in SEQ ID NO. 1, the lysine at position 229 is mutated to alanine, phenylalanine, methionine, arginine, threonine, histidine, serine, tyrosine, valine, leucine, isoleucine, proline, asparagine, aspartic acid or glutamic acid; the pyridoxal kinase mutant is used for catalyzing pyridoxal to synthesize pyridoxal phosphate, and a recombinant expression vector and a microbial cell can be further formed. The present application has good enzyme activity, high product conversion rate, high concentration of pyridoxal phosphate obtained, and the concentration of the product catalyzed by the wild-type pyridoxal kinase to phosphorylate pyridoxal is obviously improved.

The invention belongs to the technical field of enzyme catalysis, and particularly relates to a dehydrogenase mutant, a gene, an engineering bacterium and application, the dehydrogenase mutant is obtained through mutation of original dehydrogenase, the sequence of the original dehydrogenase is SEQ ID NO.1, and the mutation mode is that the 344 site is mutated from A to W, K, F, S or N, or the 130 site is mutated from H to T, W or F; the dehydrogenase mutation diagram provided by the invention has higher conversion rate, stronger specificity and faster reaction speed.

The invention relates to a method for preparing (S)-chiral amine through asymmetric catalysis of imine reductase, and belongs to the technical field of biological pharmacy. Comprising the following steps that imine reductase catalyzes imine to be subjected to a reductive hydrogenation reaction under the conditions of coenzyme and a coenzyme regeneration system, and the (S)-chiral amine compound is generated. According to the method, imine reductase is utilized to catalyze imine asymmetric reduction to prepare the innovative drug (S)-chiral amine compound, and compared with a traditional chemical synthesis method, the method has the advantages of being high in reaction efficiency, good in stereoselectivity, mild in reaction condition, environmentally friendly and the like, and is a method meeting the green production requirement.

The invention relates to the technical field of organic synthesis, in particular to a method for constructing Orforglipron tetrahydropyran ring chirality through enzyme catalysis, which comprises the following steps: step S1, taking SM1 as a raw material, and carrying out hydrolysis resolution in a solvent, a buffer salt system and enzyme catalysis to obtain a chiral pure intermediate INT-1; step S2; performing ring closing on the INT-1 through Grignard reaction to synthesize a lactone intermediate; s3, carrying out Diball-H reduction, quenching, dichloromethane extraction and anhydrous sodium sulfate drying on the INT-4, and then reducing the INT-4 by using triethyl silane to obtain an intermediate INT3; step S4, coupling the INT-3 in the presence of a catalyst and a ligand to obtain an intermediate INT-4; step S5, carrying out deprotection and salification on the INT-4 to obtain an intermediate INT5; s6, closing an indole ring from INT5 to obtain a compound of which the general formula is A; chirality is constructed through enzyme catalysis, isomer impurities do not need to be split and separated through SFC when the chirality is constructed, the loss is reduced, the yield is increased, and a target product is obtained with high chiral selectivity; meanwhile, the cost is relatively reduced, and the cost is saved.

The invention discloses an enzyme catalysis preparation method of a milobalin intermediate. According to the method, racemization 3-ethyl bicyclo [3.2. 0] hept-3-ene-6-ketone is used as a substrate, specific ketoreductase is used as a catalyst, (1S, 5R)-3-ethyl bicyclo [3.2. 0] hept-3-ene-6-ketone is selectively reduced into (1S, 5R)-3-ethyl bicyclo [3.2. 0] hept-3-ene-6-alcohol, and a target compound milobalin intermediate (1R, 5S)-3-ethyl bicyclo [3.2. 0] hept-3-ene-6-ketone is reserved. According to the method disclosed by the invention, only one enzyme is used, the concentration of a conversion substrate can reach 200g / L, the yield can reach 47.4%, the ee value can reach 99.8%, the operation is simple, the resolution efficiency is high, the selectivity is good, and the method can be used for industrial production.

The invention relates to the technical field of prebiotics preparation, and discloses a preparation method of prebiotics applied to reproduced areca catechu, and the preparation method comprises the following steps: carrying out enzyme catalysis reaction on sucrose by adopting fructosyl transferase to prepare fructo-oligosaccharide; according to the method, beta-galactosidase is adopted to carry out enzyme catalysis reaction on lactose, so that galactooligosaccharide is prepared; respectively carrying out decoloration, ion exchange, nanofiltration concentration and spray drying on the candy oligosaccharide and the galactooligosaccharide to obtain powder; the method comprises the following steps: mixing fructo-oligosaccharide powder and galactooligosaccharide powder according to a ratio, and uniformly distributing the mixture in a reproduced areca-nut matrix by adopting a spray-drying blending or low-temperature vacuum mixing mode to form a functional reproduced areca-nut product; according to the invention, low-temperature drying is carried out on the product after blending or vacuum mixing, so that the prebiotic areca nuts are released along with saliva in the chewing process, and are selectively utilized by bifidobacteria and lactic acid bacteria after entering the stomach and intestine, thereby achieving the purposes of regulating intestinal flora and improving the health-care function.

The invention discloses an integrated nano platform for bimodal detection and synergistic sterilization of pathogenic bacteria as well as a preparation method and application of the integrated nano platform, and belongs to the technical field of food safety. The platform is composed of a multifunctional nano probe (MPDA / Pd SA-DA-CDs / Apt) and a magnetic separation assembly (MNRs / PGA / AM). The probe integrates enzyme-like catalysis and photo-thermal performance and is used for generating colorimetric and photo-thermal dual-mode signals so as to realize high-sensitivity and high-reliability detection of pathogenic bacteria. The magnetic separation assembly is used for specifically capturing and enriching target bacteria and eliminating matrix interference. After detection is positive, the platform can immediately start secondary propulsion synergistic sterilization: firstly, the action distance is shortened through magnetic aggregation, and then pathogenic bacteria are efficiently inactivated and biological membranes are disintegrated by utilizing the synergistic effect of near-infrared laser excitation photothermal effect and active oxygen. According to the invention, the integration of detection and disinfection is realized, the operation is convenient, and the method has important application value in the fields of food safety and biomedicine.

The invention discloses an enzyme catalysis constant kcat prediction method and system based on multi-modal feature fusion, and the method comprises the steps: S1, obtaining an enzyme-substrate pair which comprises an amino acid sequence of a target enzyme and a chemical structure expression of a corresponding substrate; s2, inputting the amino acid sequence into a pre-trained protein language model, and carrying out average pooling treatment on hidden layer state vectors of amino acid residues in the sequence by the protein language model to obtain enzyme feature vectors for representing functional features of enzyme; s3, on the basis of the chemical structure representation of the substrate, coding the chemical structure through the set radius parameter and bit length parameter by adopting an extended connectivity chemical fingerprint algorithm to obtain a substrate feature vector for representing the structural features of the substrate; s4, splicing the enzyme feature vector and the substrate feature vector to obtain a fused feature vector; and S5, inputting the fusion feature vector into a random forest regression model, and outputting a predicted value of the catalytic constant kcat of the enzyme-substrate pair.

The invention provides a seawater soaking wound hydrogel dressing and a preparation method thereof, a drug-loaded nano system 4OI (at) ZIF-8 (at) PAD with a core-shell structure is constructed, an anti-inflammatory drug 4-octyl itaconic acid and zinc ions are jointly encapsulated in a ZIF-8 framework, and a polydopamine coating is wrapped, so that synergistic loading and controllable release of the drug and metal ions are realized. According to the dressing, dopamine modified hyaluronic acid is used as a matrix, a temperature-sensitive material and an enzyme catalysis cross-linking system are combined, stable gel can be rapidly formed in situ within 5 seconds, and the dressing has excellent tissue adhesion performance (the adhesion strength reaches 6.7 kPa). Experiments prove that the hydrogel dressing has the characteristics of broad-spectrum antibiosis, inflammation regulation and control and long-acting release. Animal experiments prove that the healing rate of seawater soaking wounds treated by the dressing on the twelfth day is as high as 95.7% and is remarkably superior to that of a commercial silver ion gel control group, scars are less after healing, and an efficient, safe and easy-to-implement scheme is provided for marine environment wound nursing.

This invention provides a nitrile hydrolase mutant and its application in the synthesis of p-cyanobenzoic acid. The invention provides a nitrile hydrolase mutant that enhances the catalytic activity for the synthesis of p-cyanobenzoic acid. The mutant protein is a non-natural protein, and it exhibits significantly enhanced activity in catalyzing the conversion of terephthalonitrile to p-cyanobenzoic acid. Furthermore, the mutant protein contains mutations in two or more core amino acids related to the enzyme's catalytic activity in the wild-type nitrile hydrolase. The nitrile hydrolase mutant of this invention can significantly improve the yield of the synthesized product catalyzed by the nitrile hydrolase.

The invention provides a preparation method of a (S)-5-(2, 2-dimethyl tetrahydro-2H-pyran-4-yl)-N-methyl-N-phenyl-1H-indole-2-formamide compound, which comprises the following steps: by taking a compound 1 as an initial raw material, reacting the compound 1 with a boric acid ester reagent to obtain a boric acid ester compound 2; the method comprises the following steps: by taking a compound 3 as an initial raw material, reducing carbonyl through enzyme catalysis to obtain a compound 4, then protecting alcoholic hydroxyl through a sulfonylation reagent to obtain a compound 5, and finally, directly coupling the compound 5 with a compound 2 under the action of a catalyst to obtain a target product compound 6. The whole process is low in experimental condition requirement, simple to operate, high in yield and suitable for process amplification.

The invention relates to high-strength degradable self-healing hydrogel and a preparation method thereof, and belongs to the technical field of high polymer materials. The hydrogel is prepared from the following components in percentage by mass: 15 to 20 percent of carboxymethyl cellulose, 10 to 14 percent of acrylic acid, 15 to 20 percent of N-isopropylacrylamide, 4 to 8 percent of tannic acid, 2 to 4 percent of borax, 0.06 to 0.1 percent of laccase, 0.5 to 1 percent of N, N-methylene bisacrylamide, 0.4 to 0.6 percent of potassium persulfate and the balance of phosphate buffer solution. According to the hydrogel disclosed by the invention, through dual-network structure design, dynamic covalent bond crosslinking and enzyme catalysis green synthesis, collaborative optimization of high strength, high self-healing property, degradability and multi-responsiveness is realized, and the problems of poor mechanical property, low repairing efficiency, environmental unfriendliness and the like of traditional hydrogel are solved; the method has wide application potential in the fields of biomedicine, flexible electronics, intelligent packaging and the like.

The invention discloses soft Maotai-flavor liquor and a preparation method thereof. The method comprises the following steps: raw material preparation, yeast material preparation, sand feeding and feeding, sand insertion and feeding, distillation and aging. In the raw material preparation step, sorghum is crushed and then mixed with hot water and white spirit vinasse, and grain fermentation and water airing treatment are carried out; mixing the broomcorn material for sand feeding with Maotai-flavor yeast powder and an enzyme catalyst, and fermenting; in the sand insertion and feeding step, sand insertion fermented grains are mixed with a sorghum material for sand feeding, Maotai-flavor yeast powder, a functional agent and a synergist, and fermentation is performed again; in the distillation step, the sand-inserted fermented grains and steamed rice husks are mixed and then distilled; and finally, aging for a period of time to obtain the soft Maotai-flavor liquor. Compared with the prior art, efficient preparation of the soft Maotai-flavor liquor can be achieved, the taste of the obtained soft Maotai-flavor liquor is further blended and improved, and the soft Maotai-flavor liquor is higher in quality.

The invention discloses a method for detecting glyphosate in coffee through Cu-CDs / ABEI (at) Ag nano-enzyme catalytic chemiluminescence, and belongs to the technical field of chemical analysis and detection.The method comprises the steps that 4-aminoantipyrine serves as a precursor, Cu < 2 + > serves as a doping element, copper-doped carbon dots (Cu-CDs) are synthesized through a microwave method, Cu-CDs and ABEI serve as reducing agents to synthesize the Cu-CDs / ABEI (at) Ag nano-enzyme, and the Cu-CDs / ABEI (at) Ag nano-enzyme is used for detecting glyphosate in coffee through Cu-CDs / ABEI (at) Ag nano-enzyme. The Cu-CDs / ABEI (at) Ag nano-enzyme has excellent peroxidase (POD-like) activity, so that H2O2 decomposition is promoted, and a chemiluminescence signal is enhanced; the glyphosate can interact with the Cu-CDs / ABEI (at) Ag nano-enzyme to inhibit the POD-like activity of the nano-enzyme, so that the chemiluminescence intensity generated by oxidation of ABEI is reduced; on the basis, the method is used for detecting glyphosate in a coffee sample, and has the characteristics of high specificity, simplicity in operation and sensitivity.

The present invention relates to the technical field of organic synthesis, and specifically relates to a method for constructing the chirality of a pyran ring in Orforglipron by means of enzymatic catalysis, the method comprising the following steps: step S1, by using SM1 and SM2 as starting materials, carrying out a reaction under the action of a palladium catalyst and a ligand to obtain INT-1; step S2, under the catalysis of Pd / C, subjecting INT-1 to double bond hydrogenation reduction to obtain INT-2; step S3, in the presence of a solvent, a buffer salt system and enzymatic catalysis, subjecting INT-2 to hydrolysis and resolution to obtain a chirally pure intermediate INT-3; step S4, subjecting INT-3 to a Grignard reaction for cyclization, so as to synthesize a lactone intermediate INT-4; and step S5, subjecting INT-4 to reduction by means of Dibal-H, quenching same, performing extraction with dichloromethane, drying same with anhydrous sodium sulfate, and then performing reduction by means of triethylsilane to obtain a compound of general formula A. In the present invention, the chirality is constructed by means of enzymatic catalysis without the need of SFC resolution for separating isomeric impurities during the construction of the chirality, thereby reducing losses and improving yield, obtaining the target product at high yield and high chiral selectivity, and further saving expenses and reducing costs.

The invention provides a tyrosine ammonia lyase mutant and application thereof in production of p-coumaric acid. The tyrosine ammonia lyase mutant is obtained by mutating wild type tyrosine ammonia lyase with an amino acid sequence as shown in SEQ ID No.1, and a mutation site is selected from at least one of Q108S, Y340Q and P375H. The catalytic activity center of wild type tyrosine ammonia lyase is analyzed, and site-directed mutagenesis is carried out on five catalytic activity center sites, so that the mutant shows different enzyme catalytic activity when the mutation sites are different, the mutation sites are the same but the mutation targets are different; q108S, Y340Q and P375H single mutations can significantly improve the enzyme catalytic activity of the tyrosine ammonia lyase mutant, and the tyrosine ammonia lyase mutant having any two mutation sites, especially having three mutation sites, also has better enzyme catalytic activity than the wild type, and has great application potential.

The invention provides a method for preparing (R)-4-chloro-3-hydroxybutyric acid ethyl ester ((R)-CHBE) through enzyme catalysis, which comprises the following steps: isopropanol is used as a hydrogen donor, a ketoreductase mutant is used for carrying out catalytic reduction reaction of COBE to prepare (R)-CHBE, and the ketoreductase mutant has amino acid mutation at the 83rd site on the basis of an amino acid sequence shown as SEQ ID NO.1. The invention also provides a preparation method of (R)-4-chloro-3-hydroxybutyric acid ethyl ester ((R)-CHBE). The thermal stability, namely heat resistance, of the ketoreductase mutant is improved, and by combining with the use of a rectifying tower, the method disclosed by the invention improves the utilization rate of isopropanol and can discharge a byproduct acetone in time, so that the substrate conversion rate and the product concentration are improved. The invention also provides an enzyme catalysis device used in the method.

The invention provides an enzyme catalysis performance prediction method and system based on chemical reaction and a storage medium. The enzyme catalysis performance prediction method based on the chemical reaction comprises the following steps: inputting a to-be-detected sample; inputting the SMILES character string of the reaction in the to-be-tested sample into a pre-fine-tuned reaction encoder in a pre-trained VenusRXN model to obtain an atom embedding matrix formed by stacking all atom embedding vectors in a reaction compression graph of the reaction; inputting the atom embedding matrix and an enzyme sequence corresponding to the reaction in the to-be-detected sample into a reaction-protein joint encoder which is finely adjusted in advance in the VenusRXN model to obtain a reaction-protein joint CLS embedding vector; inputting the combined CLS embedding vector into a matching head, and calculating a matching score between the reaction and the corresponding enzyme sequence; and outputting the matching score.

The invention discloses a biological enzyme catalytic reaction continuous flow temperature control device, and relates to the field of biological enzyme reaction, the biological enzyme catalytic reaction continuous flow temperature control device comprises a support frame, and the middle part of the support frame is fixedly connected with a reaction temperature measurement mechanism. According to the present invention, the reaction temperature measurement mechanism, the inlet monitoring mechanism and the outlet monitoring mechanism are arranged, the inlet section second electric heating pipe is used for heating, the second temperature sensor is used for monitoring the temperature of the fixed cylinder, and the feeding channel is preheated so as to ensure the matching of the feeding temperature and the reaction section; the power of an electric heating wire and a first electric heating tube is dynamically adjusted, so that the temperature in a temperature control cylinder is stabilized at the initial temperature of enzyme catalysis, an outlet section controls the internal temperature of an outlet monitoring mechanism, the outlet temperature of enzyme reaction is regulated, and the inlet section, the reaction section and the outlet section are independently provided with heating elements and temperature sensors. Full-flow regulation and control of feed preheating, reaction temperature control and product temperature stabilization are realized, and the requirement of enzyme catalysis on temperature sensitivity is met.