40results about How to "Improve the stability of enzyme activity" patented technology

The invention discloses an acid-stable glutamic acid decarboxylase (GAD) mutant with pH stability migrating to neutral range, and belongs to the field of biological engineering. The encoding gene of glutamic acid decarboxylase derived from actobacillus plantarum GB01-21 glutamic acid decarboxylase is subjected to site-specific mutagenesis, and the glutamate E on the 89th site is mutated to arginine R or alanine A. The glutamic acid decarboxylase mutant has relative enzyme in pH value of 6.5 increased from the original 38% up to 72% or 84%, and the enzyme activity stability in the neutral pH range is increased significantly. For the transformation with a glutamic acid decarboxylase mutant synthesized by recombinant escherichia coli, the GABA yield reaches 260 g / L, and the yield is 99.6%; and for the transformation with a glutamic acid decarboxylase mutant synthesized by recombinant Corynebacterium glutamicum, the GABA yield reaches 116 g / L, and the yield is 99.5%. The invention reduces the fermentation equipment loss under acidic conditions, and lays foundation for the efficient synthesis of gamma-aminobutyric acid.

The invention discloses a preparation method of immobilized beta-glucosidase in the field of enzyme preparations. According to the method, fructose is adopted as a pore-foaming agent, and the immobilized beta-glucosidase is prepared through the tetraethoxysilane hydrolysis reaction sol-gel method. Different immobilized beta-glucosidase samples are prepared by adding fructose water solutions with different concentrations and beta-glucosidase of different dosages. For the obtained immobilized beta-glucosidase, the invalid adsorption in the enzymolysis process of cellulose can be avoided, so that the enzymolysis conversion efficiency of cellulose is obviously improved, the immobilized enzyme has the advantages of good mechanical strength and multiple times of recycling, and the hydrolysis and saccharifying costs of cellulose are reduced.

A special-effect biological enzyme formaldehyde-removing odor-removing agent and a preparing method thereof are disclosed. The agent includes, by weight, 2-6% of laccase, 0.5-2% of formaldehyde dehydrogenase, 0.5-2% of formate dehydrogenase, 2-5% of pectase, 0.1-0.2% of cis-benzene dihydrodiol dehydrogenase, 0.1-0.5% of epoxide hydrolase, 0.1-0.5% of NADH, 0.5-1.5% of an amino compound, 0.01-0.05%of an activator, 1-2% of a stabilizer and 10-15% of a plant extractant, with the balance being water. The formaldehyde-removing odor-removing agent is safe, environmentally friendly and convenient tooperate. Furniture, wallpaper, leather, carpets, floor, curtains, and other house decoration substrates can be sprayed with the formaldehyde-removing odor-removing agent directly, and formaldehyde, amino, TVOC and other pollution gas in air can be decomposed.

The invention relates to the field of genetic engineering, in particular to an acidophil Beta-glucanase GLU7A and gene and application thereof. The invention provides a glucanase GLU7A from acidophil bispora Bisporasp, and the amino acid sequence thereof is shown as SEQIDNO.1, and the invention provides a genome of coding the glucanase and cDNA coding gene glu7A. The invention obtains an acidophil glucanase which has the optimum pH value of 1.5-5.0, simultaneously remains high enzymatic activity in acid environment, and resists protease hydrolysis. In addition, the glucanase not only hydrolyzes Beta-1, 3-1, 4-glucanase, but also can hydrolyze cellulose. Due to the properties, the acidophil Beta-glucanase GLU7A can be applied in the industries of food, feedstuff and beer.

The invention relates to novel high-temperature resistant alpha-amylase, a preparing method of the novel high-temperature resistant alpha-amylase and an application of the novel high-temperature resistant alpha-amylase. As PCR site-specific mutagenesis is carried out on genes of wild-type high-temperature resistant alpha-amylase, and the genes are efficiently expressed in bacillus subtilis. The novel high-temperature resistant alpha-amylase is high in stability in the high-temperature environment and the acid environment, and can better adapt to industrial production to achieve the effects of saving energy, reducing consumption and improving efficiency. By means of the technical scheme, the genes of the wild-type high-temperature resistant alpha-amylase are separated from bacillus licheniformis, mutagenesis is carried out on His316 amino acid residues of the genes, efficient expression is carried out in the bacillus subtilis, and under the 90-DEG C condition and the pH-4.5 condition, the stability of the novel high-temperature resistant alpha-amylase (His316 to Arg) is improved compared with the wild-type high-temperature resistant alpha-amylase.

The invention discloses a novel firefly luciferase. The luciferase is obtained by adding an amino acid segment at the N terminal of a natural luciferase protein; thus, the luciferase has higher stability of the enzyme activity in comparison with naturally extracted luciferase or recombined natural luciferase. The invention further discloses a DNA molecule coding the firefly luciferase and a method for preparing the luciferase; the DNA molecule of the luciferase is used for constructing a recombinant expression vector; the expression vector is transfected into a host cell to form a transformant; the recombined firefly luciferase is obtained by inducing and expressing the expression vector in the transformant; and the recombined luciferase is separated and purified by high-salt deposition. After recombined luciferase is deposited under high salt condition, the luciferase is separated and purified by centrifuging, and the preparation method of the luciferase has simple operation and high efficiency, and saves time.

The invention relates to genetic engineering field, in particular to eosinophilic lactase BGALA, gene and application thereof. The invention provides a lactase BGALA of eosinophilic Bispora sp.; the amino acid sequence of the lactase BGALA is shown in SEQ ID NO.1; and the invention provides genome and cDNA coding gene bgalA for coding the lactase. The invention obtains an eosinophilic lactase with the most proper pH value of 1.5, which maintains high enzymatic activity in acid environment, has better pH stability and heat stability, and antiprotease hydrolysis. The eosinophilic lactase can effectively hydrolyze the lactose in milk in simulated digestive tract environment. The eosinophilic lactase BGALA with the properties can be used for treating lactose intolerance, diary industry no processing cow milk and whey.

The invention discloses a D-amino acid oxidase mutant, wherein the sequence of the D-amino acid oxidase mutant comprises a sequence obtained by mutating the 54th amino acid residue N, the 58th amino acid residue F, the 211st amino acid residue C and the 213th amino acid residue M of a sequence represented by SEQ ID NO.1 or a sequence having at least 76% identity with the SEQ ID NO.1, and the D-amino acid oxidase mutant has high enzyme activity, high enzyme activity stability and / or high ammonium tolerance compared with wild type D-amino acid oxidase. The invention also discloses applications of the D-amino acid oxidase mutant in preparation of 2-oxo-4-(hydroxymethylphosphinyl)butyric acid. The D-amino acid oxidase mutant is high in enzyme activity, and has the enhanced enzyme activity stability and / or ammonium tolerance, so that the cost is reduced, and industrial production is facilitated.

The invention discloses a soluble fodder enzyme capable of effectively inhibiting bacterial reproduction, and lowering loss of the activity of the enzyme. The invention is a soluble powder prepared by adding soluble carriers into one or more condensed enzyme liquors containing one or more kinds of enzymes, spray drying after dissolving. The weight ratio between the condensed enzyme liquor and the soluble fodder enzyme is 400-500Kg of condensed enzyme liquor, 75-155Kg soluble carrier. The soluble carrier includes 3-6kg of zinc sulfate heptahydrate, 1-3kg of anhydrous calcium chloride, 30-50kg of sorbitol, 30-50kg of lactose, 10-30kg of beta- cyclodextrin, and 1-5kg of sodium carboxymethyl cellulose. The manufacturing method of the invention is that the soluble fodder enzyme powder is prepared by adding the soluble carrier slowly into the condensed enzyme liquor, stirring while heating and controlling the temperature to be not more than 40 DEG C., spraying and drying the liquor. The invention can be applied to the field of fodder additive.

The invention discloses a preparation method of liquid acidic pectinase with strong stability, and belongs to the technical field of preparation of enzyme preparations. The preparation method of the liquid acidic pectinase with strong stability does not need addition of a chemical preservative and low-temperature treatment, and the liquid acidic pectinase with strong stability, which is stable and has a relatively long quality guarantee period, can be obtained by fermenting a crude enzyme solution and blending a concentrated solution by adopting a high-voltage pulse electric field at normal temperature, adding natural plant raw materials including a pectin decomposed product, a Chinese medicinal herb extract, modified dietary fibers and the like during blending, and then performing aseptic filtration and sterile filling. Experiments prove that the liquid acidic pectinase with strong stability, prepared by the method disclosed by the invention, has the total number of bacterial colonies of 75-110CFU / mL after being stored for 12 months at room temperature; and the enzyme activity loss rates of the liquid acidic pectinase which is stored for 12 months at 40 DEG C and 0 DEG C are 1.2-1.4% and 0.5-1.1% respectively.

The invention provides an assay kit for adenosine deaminase. The assay kit comprises a reagent R1 and a reagent R2. The reagent R1 comprises TRIS, HCL, xanthine oxidase, purine nucleoside phosphorylase, 4-aminoantipyrine, peroxidase and sodium aspartate; and the reagent R2 comprises TRIS, HCL, adenosine, N-ethyl-N-(2-hydroxy-3-sulfopropyl)-3-methylaniline sodium slat and glycerol. The assay kit ofthe invention belongs to the technical field of biological detection, is simple in reagent composition, good in stability, rapid in reaction and low in cost, and can accurately detect adenosine deaminase; and the detection results of the assay kit have no obvious difference from the detection results of listed products.

The invention discloses a preparation method of a beer liquid compound enzyme and belongs to the technical field of preparation of liquid compound enzymes. According to the preparation method, a liquid enzyme preparation for beer brewage is taken as a main raw material, stabilizers such as sugar, polyhydric alcohol, an amino acid, a thickener, albumin, metal ions and the like as well as substances such as a hop extract, a Chinese herbal medicine extracting solution, antibacterial peptides and the like which have anti-corrosion effects and can promote the enzyme preparation to be more stable are compounded scientifically, and the addition of a preservative is completely replaced, so that the breeding and the growth of harmful microorganisms are effectively inhibited, the activity of the liquid compound enzyme can be stabilized synergistically together with other components, the biological stability and the enzyme activity stability of the liquid compound enzyme are improved fundamentally, and the shelf life of the liquid enzyme preparation is effectively prolonged. The total number of bacterial colonies is in a range of 168-214 CFU / mL if the prepared liquid compound enzyme is stored at the room temperature for 12 months; enzyme activity loss ratios are in ranges of 2-2.5% and 1-1.7% respectively if the prepared liquid compound enzyme is stored at temperatures of 40 DEG C and 0 DEG C for 12 months.

The invention is suitable for the technical field of cleaning supplies and provides a washing machine slot cleanser and a preparation method and application thereof. The washing machine slot cleansercomprises the following components by weight: 2-5 parts of an anionic surfactant, 24-29.5 parts of a basic inorganic cleaning agent, 10-17 parts of a builder, 1.5-2.5 parts of an enzyme preparation and 0.5-1 part of an enzyme stabilizer, wherein the enzyme preparation is one or a mixture of at least two of protease, lipase, pectinase, cellulase, hemicellulase, mannase, staphylococcal nuclease, catalase and lysozyme. The enzyme preparation and the anionic surfactant has a coordinated function; under the action of the enzyme stabilizer, the enzyme activity stability of the enzyme preparation ishigh; various stains in a washing machine slot can be effectively decomposed and removed; the cleaning effect is good; cleanliness and no residues are achieved after cleaning; secondary pollution cannot be caused; and sanitation and hygiene in a washing machine is guaranteed.

The invention discloses a bromelain antiallergic food and a preparation method thereof. The bromelain antiallergic food disclosed by the invention is a bromelain beverage mainly prepared from bromelain, glucose, citric acid, VB1, L-cysteine and NaCl. By adding glucose into a formula of the bromelain antiallergic food, the enzyme activity stability of a bromelain solution is superior to the stabilities of bromelain solutions of other sugar solutions, so that the enzyme activity is beneficially guaranteed; the other raw materials in the formula do not contain sour substances, and citric acid is added, so that the taste can be well changed, and meanwhile, citric acid is capable of weakening the heat resistance of microorganisms, inhibiting the growth of the microorganisms and improving the performance of an antioxidant; and the bromelain has maximum inhibition ratio to hyaluronidase due to the concentration of the bromelain in the formula, and the enzyme activity decay is within an optimal enzyme activity equivalent range when the concentration is 0.2g / 100mL.

The invention provides a total bile acid assay kit, which comprises a reagent R1 and a reagent R2, wherein the reagent R1 is prepared from the following components with the concentrations: 10-20g / L trishydroxymethylaminomethane, 16-25g / L 6N HCL, 0.6-2g / L thiooxidized coenzyme I and 6-15g / L KCL; the reagent R2 is prepared from the following components with the concentrations: 10-20g / L trishydroxymethylaminomethane, 16-25g / L 6N HCL, 4-8g / L reduced coenzyme I, 6-15KU / L 3 alpha-hydroxysteroid dehydrogenase, 80-130g / L polyethylene glycol and 0.4-1.1ml / L betaine solution. The invention belongs to the technical field of biological detection. According to the total bile acid assay kit provided by the invention, the anti-interference ability is significantly enhanced while the stability of the reagents is improved, and is good in accuracy when being used for determination of total bile acid.

The invention provides a 1, 5-sorbitan determination kit, a preparation method and an application thereof. The kit contains a reagent R1 and a reagent R2, wherein the reagent R1 contains the followingcomponents: a buffer solution, adenosine disodium triphosphate, hexokinase, glucose-6-phosphate dehydrogenase, nicotinamide adenine dinucleotide, phosphoenolpyruvate monopotassium salt, 4-amino antipyrine (4-AA), pyruvate kinase, peroxidase, lactic dehydrogenase, ascorbic acid oxidase, magnesium chloride, potassium chloride, an enzyme stabilizer and a preservative; and the reagent R2 is preparedfrom the following components in concentration: the buffer solution, pyranose oxidase, N-ethyl-N-(2-hydroxy-3-sulfopropyl)-3-methylaniline sodium salt, a surfactant and the preservative. The kit is aliquid kit with strong stability, high accuracy, high sensitivity and a stable glucose elimination capability, can be suitable for a full-automatic biochemical analyzer, and is simple and convenient to operate.

The invention belongs to the technical field of biological enzyme preparations, and particularly relates to a post-treatment process for acidic pectinase with stable enzyme activity. The post-treatment process for the acidic pectinase with the stable enzyme activity comprises the following operation steps: (1) pre-treating feed liquid, wherein distilled water and solid acidic pectinase crude product powder are uniformly stirred; (2) adjusting a pH value to be between 3.5 and 4.5; (3) adjusting the pH value to be between 4.5 and 5.5; (4) adjusting the pH value to be between 3.5 and 4.5; (5) filtering a mixed solution obtained in step (4) by adopting a plate frame and performing ultra-filtration concentration; and (6) adding a carrier into the mixed solution obtained in step (5), mixing andperforming spray drying to obtain solid acidic pectinase with the stable enzyme activity. The acidic pectinase prepared by adopting the preparation method has relatively high enzyme activity in the same condition, is relatively short in production cycle, and can be applied to feed industry and fruit juice industry.

The invention discloses a mutant of D-amino acid oxidase, the sequence of which comprises amino acid residue N at position 54 of the sequence shown in SEQ ID NO.1 or a sequence having at least 76% identity with SEQ ID NO.1, The mutated sequence of the 58th amino acid residue F, the 211th amino acid residue C and the 213th amino acid residue M; the D-amino acid oxidase mutant has a higher enzyme than the wild-type D-amino acid oxidase activity, enzymatic stability and / or ammonium resistance. The invention also discloses the application of the D-amino acid oxidase mutant in the preparation of 2-oxo-4-(hydroxymethylphosphinyl)butyric acid. The D-amino acid oxidase mutant of the present invention has high enzyme activity, improved enzyme activity stability and / or enhanced ammonium resistance, thereby reducing costs and being beneficial to industrial production.

The invention provides an enzyme manufacture method, which comprises the following working procedures of: complex acquisition: enabling a solid enzyme and a high-molecular adsorbing material to be in contact under the condition that the pH value is 6-8 to obtain a solid enzyme-high-molecular adsorbing material complex; contact: enabling the solid enzyme-high-molecular adsorbing material complex to be in contact with a reducing sugar; and separation: carrying out separation from a mixed system obtained in the working procedure of the contact to obtain the enzyme, wherein the high-molecular adsorbing material comprises at least one of the materials selected from the group consisting of a non-polar macroporous adsorbent resin, a non-polar skeleton high-molecular polymer and a non-ionic hydrophobic cross-linked polymer. The enzyme manufacture method can effectively prevent enzyme activity from being reduced, provides the enzyme with high enzyme activity and excellent enzyme activity stability, prolongs the service life of the enzyme, has simple manufacture working procedures, is easy to control the process, can meet the requirements of high-efficiency and stable production, and effectively reduces the production cost of enterprises.

The invention discloses a high-activity peanut shell polysaccharide and a preparation method thereof and belongs to the technical field of natural product preparation. Mutants of an endoglucanase and a cellobiohydrolase are obtained by a site-directed mutation way, compounding is performed, and an active polysaccharide and a flavonoid compound are synchronously obtained from peanut shells by an ultrasonic assisted enzymolysis and extraction way. The optimum hydrolysis temperature and enzyme activity of the complex enzymes are improved by the complex enzymes and the preparation process, operation steps are simplified, extraction time is reduced, synchronous preparation of the flavonoid compound and the water-soluble polysaccharide from peanut shells is realized, synchronous enzymolysis and extraction of the polysaccharide under a medium-high temperature condition is also realized, the obtained active polysaccharide is high in flavonoid content, and strong in antioxidant activity and antibacterial activity, and has a plurality of physiological functions and a wide application range.

The invention provides a preservation method of phospholipase C. By using the preservation method, the phospholipase C has good enzyme activity stability. When the preservation method of the phospholipase C provided by the invention is used in the practical application process of the phospholipase C, the production energy consumption can be reduced; and meanwhile, the activity loss of the phospholipase C is avoided.

The invention relates to a glutamate decarboxylase mutant with improved thermal stability and an application thereof, belonging to the field of bioengineering. The mutant is prepared primarily by the following steps: performing saturated mutation of glutamine Q, valine V and threonine T on the sites 5-7 of the amino acid sequence of glutamate decarboxylase, and screening to obtain high-stability mutants Q5E / V6S / T7V, Q5Y / V6R / T7K and Q5N / V6Y / T7V. In the glutamate decarboxylase mutant prepared in the invention, the half-inactivation temperature is 45-50.5 DEG C which is 4.9-10.2 DEG C higher than that of wild type mutant; and the half-life period at 45 DEG C is 76-129min, which is 3.2-4.3 times higher than 24min of wild type mutant. By transforming glutamic acid for 12h with the whole cell of glutamate decarboxylase mutant synthesized from recombinant escherichia coli, 260-350g / L gamma-aminobutyric acid (GABA) can be obtained, and the molar yield is 76.6-97.8%. In the glutamate decarboxylase mutant prepared in the invention, the thermal stability is obviously improved, the production of gamma-aminobutyric acid is facilitated, and a foundation is laid for efficient synthesis of gamma-aminobutyric acid.

The invention discloses a preparation method of immobilized beta-glucosidase in the field of enzyme preparations. According to the method, fructose is adopted as a pore-foaming agent, and the immobilized beta-glucosidase is prepared through the tetraethoxysilane hydrolysis reaction sol-gel method. Different immobilized beta-glucosidase samples are prepared by adding fructose water solutions with different concentrations and beta-glucosidase of different dosages. For the obtained immobilized beta-glucosidase, the invalid adsorption in the enzymolysis process of cellulose can be avoided, so that the enzymolysis conversion efficiency of cellulose is obviously improved, the immobilized enzyme has the advantages of good mechanical strength and multiple times of recycling, and the hydrolysis and saccharifying costs of cellulose are reduced.

The invention discloses a freeze-drying protective agent of glycosaminoglycan synthetase and application of the freeze-drying protective agent. The freeze-drying protective agent is prepared from trehalose, hydroxypropyl-beta-cyclodextrin and ectoine. The formula of the freeze-drying protective agent is different from the formula of the traditional freeze-drying protective agent, the components of the formula are simple, the freeze-dried glycosaminoglycan synthase is loose in structure, regular in shape and appearance and good in solubility, and particularly, the enzyme activity of the freeze-dried glycosaminoglycan synthase is slightly different from that of the freeze-dried glycosaminoglycan synthase before freeze-drying. And the enzyme activity can be kept above 90% after being stored at 4 DEG C and 25 DEG C for 90 days, which indicates that the freeze-drying protective agent can effectively reduce the activity loss of the glycosaminoglycan synthase in the freeze-drying process, and is beneficial to the storage and transportation of the glycosaminoglycan synthase.

The invention discloses a high-activity peanut shell polysaccharide and a preparation method thereof and belongs to the technical field of natural product preparation. Mutants of an endoglucanase and a cellobiohydrolase are obtained by a site-directed mutation way, compounding is performed, and an active polysaccharide and a flavonoid compound are synchronously obtained from peanut shells by an ultrasonic assisted enzymolysis and extraction way. The optimum hydrolysis temperature and enzyme activity of the complex enzymes are improved by the complex enzymes and the preparation process, operation steps are simplified, extraction time is reduced, synchronous preparation of the flavonoid compound and the water-soluble polysaccharide from peanut shells is realized, synchronous enzymolysis and extraction of the polysaccharide under a medium-high temperature condition is also realized, the obtained active polysaccharide is high in flavonoid content, and strong in antioxidant activity and antibacterial activity, and has a plurality of physiological functions and a wide application range.

The invention discloses a beer liquid compound enzyme and a preparation method thereof and belongs to the technical field of preparation of liquid compound enzymes. According to the beer liquid compound enzyme, a liquid enzyme preparation for beer brewage is taken as a main raw material, stabilizers such as sugar, polyhydric alcohol, an amino acid, a thickener, albumin, metal ions and the like as well as substances such as a hop extract, a Chinese herbal medicine extracting solution, antibacterial peptides and the like which have anti-corrosion effects and can promote the enzyme preparation to be more stable are compounded scientifically, and the addition of a preservative is completely replaced, so that the breeding and the growth of harmful microorganisms are effectively inhibited, the activity of the liquid compound enzyme can be stabilized synergistically together with other components, the biological stability and the enzyme activity stability of the liquid compound enzyme are improved fundamentally, and the shelf life of the liquid enzyme preparation is effectively prolonged. The total number of bacterial colonies is in a range of 168-214 CFU / mL if the prepared liquid compound enzyme is stored at the room temperature for 12 months; enzyme activity loss ratios are in ranges of 2-2.5% and 1-1.7% respectively if the prepared liquid compound enzyme is stored at temperatures of 40 DEG C and 0 DEG C for 12 months.

The invention provides a preservation method of phospholipase C. By using the preservation method, the phospholipase C has good enzyme activity stability. When the preservation method of the phospholipase C provided by the invention is used in the practical application process of the phospholipase C, the production energy consumption can be reduced; and meanwhile, the activity loss of the phospholipase C is avoided.

The invention relates to novel high-temperature resistant alpha-amylase, a preparing method of the novel high-temperature resistant alpha-amylase and an application of the novel high-temperature resistant alpha-amylase. As PCR site-specific mutagenesis is carried out on genes of wild-type high-temperature resistant alpha-amylase, and the genes are efficiently expressed in bacillus subtilis. The novel high-temperature resistant alpha-amylase is high in stability in the high-temperature environment and the acid environment, and can better adapt to industrial production to achieve the effects of saving energy, reducing consumption and improving efficiency. By means of the technical scheme, the genes of the wild-type high-temperature resistant alpha-amylase are separated from bacillus licheniformis, mutagenesis is carried out on His316 amino acid residues of the genes, efficient expression is carried out in the bacillus subtilis, and under the 90-DEG C condition and the pH-4.5 condition, the stability of the novel high-temperature resistant alpha-amylase (His316 to Arg) is improved compared with the wild-type high-temperature resistant alpha-amylase.

Relating to the technical field of chemical industry, the invention discloses a preparation method and application of high-tolerance beta-glucosidase. The method includes: separating beta-glucosidasefrom aspergillus aculeatus, and subjecting immobilized beta-glucosidase to degelatinization treatment to obtain a beta-glucosidase liquid, selecting 15% of aloe, 1.5% of an alcohol extracted solution,0.2% of hyaluronic acid, and the balance deionized water, respectively adding 0, 10U / L, 20U / L, 30U / L and 40U / L distribution collection enzyme solutions subjected to 0.25 sodium chloride gradient elution after DEAE chromatography, standing the mixed solution for 40 days at an environment temperature of 45-55DEG C, cooling the mixed solution subjected to standing for 2-3d, and conducting subpackaging and bottling so as to obtain a moisturizing essence finished product. Through gelatinization of the prepared beta-glucosidase, high enzyme loading capacity of the beta-glucosidase is guaranteed, sothat the tolerance of the beta-glucosidase is substantially improved, at the same time, the operation is simple, the preparation time is short, the influence on the enzyme activity is low, the biochemical properties of the enzyme are enhanced, and the production cost is reduced.