48 results about "Betaglucin" patented technology

The invention relates to high-sugar-tolerant beta-glucosaccharase Bg14, and an expressed gene and application thereof. The amino acid sequence is shown as SEQ ID NO.1. The gene of the high-sugar-tolerant beta-glucosaccharase Bg14 of aspergillusniger is cloned, recombined and expressed for the first time; and the glucose-tolerant coefficient Ki of the recombinase Bg14 is 2 mol/L.

The invention discloses a beta-glucosaccharase and application thereof. The beta-glucosaccharase PpCel3E is separated from a cellulase producing bacterium extracellular crude enzyme solution for the first time. The amino acid sequence of the beta-glucosaccharase is disclosed as SEQ ID NO.1. The nucleotide sequence of the expression gene of the beta-glucosaccharase is disclosed as SEQ ID NO.2. The beta-glucosaccharase PpCel3E has unique actions on inducing cellulase or hemicellulase synthesis and enhancing saccharification and hydrolysis efficiency of cellulase producing fungus extracellular cellulase.

The invention relates to the field of genetic engineering, and specifically relates to a novel specific humicola-sourced high-temperature acid beta-glucosidase HiBgl3C as well as a gene and an application thereof. The invention provides a novel high-temperature acid beta-glucosidase HiBgl3C, which has an amino acid sequence shown as SEQ ID No.1 or 2. The invention also provides a gene for coding the high-temperature neutral beta-glucosidase HiBgl3A, a nucleotide sequence of which is shown as SEQ ID NO.4 or 5, as well as a recombinant vector comprising the gene and a recombinant strain and an application thereof. An optimum temperature of the high-temperature acid beta-glucosidase HiBgl3C sourced from the specific humicola is 60 DEG C, and an optimum pH value is 5.5; moreover, the pH stability is good, and the high-temperature acid beta-glucosidase HiBgl3C can resist the alkaline environment; and the high-temperature acid beta-glucosidase HiBgl3C has good resistance to a majority of chemical reagents, metal ions and glucoses and is remarkable in application prospect in various industries such as washing agent, biological ethanol and the like in a complicated environment.

The invention relates to a processing method of roxburgh rose juice. The processing method of the roxburgh rose juice disclosed by the invention is characterized by comprising the following steps: A, draining after cleaning fresh roxburgh roses, which are sufficiently matured and are not decayed and mildewed, and squeezing and filtering through a mechanical squeezing method so as to obtain original roxburgh rose juice; B, adding 20-25 U/L of beta-glucosidase into the roxburgh rose juice, keeping at 45 DEG C for 60-70 min, adding 25-30 U/L of glucose oxidase into the roxburgh rose juice again, and keeping at 35-40 DEG C for 40-50 min; and C, adding 0.03-0.04% of adenylic acid and 0.015-0.020% of sucralose into the processed juice, uniformly mixing, after adjusting by using saccharose till the juice is sour and sweet properly, instantly sterilizing at high temperature, bottling and cooling, wherein the sucralose is added after being dissolved in clear water. The roxburgh rose juice disclosed in the invention is processed under the mild conditions by using a biologic enzymatic technology, so that natural quality of juice is stabilized and strengthened; the sensory characteristics of the roxburgh rose juice are improved by utilizing influence of a substrate to human-body taste receptors; the processing method of the roxburgh rose juice is simple and feasible, high-efficiency and safe; and furthermore, the nutritional components in the roxburgh rose juice are effectively reserved.

The invention provides a Beta-glucosaccharase gene S-bgl3 and application of the Beta-glucosaccharase gene S-bgl3. Beta-glucosaccharase gene S-bgl3 has the nucleotide sequence as shown in SEQ ID NO: 1; and the genetically coded Beta-glucosaccharase S-bgl3 has the amino acid sequence as shown in SEQ ID NO: 2. The Beta-glucosaccharase S-bgl3 can be applied to the decomposition of cellobiose.

The invention relates to the fields of gene engineering and genetic engineering, and in particular relates to beta-glucosaccharase improved mutant E168Q as well as a coding gene and applications of the beta-glucosaccharase improved mutant E168Q. According to the beta-glucosaccharase improved mutant E168Q, high-temperature acid beta-glucosaccharase BGL3A derived from Talaromyces leycettanus JCM12802 is taken as a female parent, site-specific mutagenesis is carried out on the sequence of the beta-glucosaccharase by adopting a molecular biological technology, and expression is carried out. Under the modification condition, the affinity of the mutant for cellobiose is improved by 2.0 times compared with that of the wild type (before mutation), the catalytic efficiency is improved by 1.5 times, and the optimum reaction pH and temperature are invariable. With the adoption of the strategy, the catalytic efficiency of beta-glucosaccharase can be greatly improved, and an application foundation is provided for the beta-glucosaccharase in the industrial production fields including food, bioethanol and the like. The strategy has great guiding significances for the improvement of the catalytic efficiency of beta-glucosaccharase and other enzymes.

The invention discloses [beta]-glucosidase glA2, of which the gene sequence is represented as the Seq ID No.1. An amino acid sequence encoded by the gene sequence is represented as the Seq ID No.2. Comapred with the [beta]-glucosidase in the prior art, the [beta]-glucosidase glA2 has following advantages: (1) the [beta]-glucosidase glA2 can be improved in enzyme activity significantly with glucose, even that the concentration of the glucose is lower than 1.75 mol/L, and when the concentration of the glucose is 0.4 mol/L, the enzyme activity can reach up to 136.8 U/mg, which is 2.2 times as the enzyme activity without glucose; and (2) the [beta]-glucosidase glA2 is excellent in alkali stability, wherein the enzyme activity can be maintained by 92%, 99% and 97% even that the enzyme is incubated under the pH respectively being 8.0, 9.0 and 10.0 for 24 h. The [beta]-glucosidase glA2 can be applied in a catalytic environment contains high-concentration glucose or is alkaline.

The invention discloses a feed additive premixing agent capable of relieving oxidative stress of intestinal tracts of broiler chickens and application of the feed additive premixing agent. The premixing agent is prepared from the following components: 20-50g/kg of beta-glucosidase, 40-80g/kg of glucose oxidase, 5-10g/kg of vitamin B2, 15-30mg/kg of active selenium yeast, 30-60g/kg of chitosan and 50-80g/kg of sticktight extract. The premixing agent disclosed by the invention does not contain any antibiotic and is a green, pollution-free and medicine-residue-free high-quality broiler chicken feed additive premixing agent; the premixing agent has the advantages that no toxic side effect is caused, the growth of the broiler chickens and human health are facilitated, and preparation and application methods are simple and convenient; the feed additive premixing agent has biological functions in the aspects of facilitating the growth of the broiler chickens, improving the feed utilization, improving the anti-oxidization capability of organisms and the like, and the effects of effectively relieving the oxidative stress of the intestinal tracts, improving the immunity of the organisms, reducing the infection rate of intestinal tract diseases including diarrhea of the broiler chickens and the like, the death rate and the like.

The invention discloses a liquid biological polishing enzyme and a preparation method thereof. The liquid biological polishing enzyme contains the following components: 30000-40000mu/mL of beta-1, 4-exoglucanase, 20000-30000mu/mL of beta-1, 4-hydrolytic endoglucanase, 4000-5000mu/mL of beta-glucosaccharase and deionized water. The pH value of the liquid biological polishing enzyme is 4.7-5.2, and the total activity of the enzymes is 1000-2000mu/mL. The liquid biological polishing enzyme has the advantages of obvious biological polishing effect and low loss ratio and generates small damage to fabrics.

The invention relates to a preparation method of diosgenine. The preparation method is a method for preparing diosgenine by using dioscorea zingiberensis as a raw material through enzymatic hydrolysis and belongs to the field of enzyme engineering. The method for preparing diosgenine by enzymatic hydrolysis comprises the following steps: immersing crushed dioscorea zingiberensis in an acetic acid-sodium acetate buffer solution to successively carry out cellulase I enzymolysis and beta-glucosidase I enzymolysis, collecting enzymolysis residue and purifying to prepare diosgenine. The method for extraction of diosgenine has a simple extraction technology, has little environmental pollution and is suitable for large-scale popularization.

The invention relates to white-flower Chinese loropetalum extract which comprises quinate derivative ingredients and glucoside ingredients. The quinate derivative ingredients include one or multiple of chlorogenate methyl ester, chlorogenate ethyl ester and 5-O-p-coumaroyl quinate methyl ester, and the glucoside ingredients include one or multiple of rhodioside, (Z)-3-hexenyl-O-alpha-L-rhamnopyranosyl-(1->6)-beta-D-glucopyranoside, benzyl-O-alpha-L-rhamnopyranosyl-(1->6)-beta-D-glucopyranoside, myricitrin and quercetin-3-O-(6'-O-galloyl)-beta-glucoside. The invention further relates to a preparation method of and a drug combination of the white-flower Chinese loropetalum extract and application of the extract in preparing hemostatic drug or products. Pharmacodynamic and acute toxicity experiments of the extract show that the extract has the advantages of clear active ingredients, strong pharmacodynamic effect, little toxic and side effect, high product purity, low administration dosage and controllable quality.

The invention relates to beta-glucosidase Cel1b, and expression gene and application thereof, and belongs to the technical field of bioengineering. The invention provides a cel1b gene expressing beta-glucosidase Cel1b, and the cel1b gene has a nucleotide sequence shown a sequence SEQ ID NO.1. The invention also provides a beta-glucosidase Cel1b with an amino acid sequence shown as a sequence SEQ ID NO.2. The beta-glucosidase Cel1b of the invention can be used in industrial synthesis of expensive cello-oligosaccharide and be further applied to research on cellulase hydrolysis mechanism and utilization of cellulose by microbes. Besides, the cello-oligosaccharide synthesized by an in vitro biological method can be used as a functional food or food additive as well as sweetener for diabetes patients; and the cello-oligosaccharide can also be applied to cosmetic industry and pharmaceutical industry and has a wide application prospect.

The invention discloses an F85-20 protein, a coding gene thereof and an application of the F85-20 protein as beta-glucosidase. The invention provides the protein shown in the following 1) or 2): 1) a protein formed by amino acid residues shown in a sequence 2 in a sequence table; 2) a protein which is obtained by carrying out substitution and/or deletion and/or addition of one or more amino acid residues on an amino acid residue sequence of the sequence 2 in the sequence table, has the same functions as the protein shown in 1) and is derived from the protein shown in 1). Experiments prove that new beta-glucosidase F85-20 can still retain 80% of activity after being incubated at 50 DEG C for two hours under the conditions that p-nitrophenol glucoside (pNPG) is taken as the substrate and the pH value is 6.0, and the optimum temperature is 65 DEG C; new beta-glucosidase F85-20 can retain more than 70% of residual activity in a pH value range of 4.0-7.5 after being incubated in buffer solutions with different pH values for 24 hours at 4 DEG C.

The invention relates to an application of 6-hydroxy kaempferol-3-oxo-beta-glucoside in preparation of anti-cancer medicines. The experimental study shows that the 6-hydroxy kaempferol-3-oxo-beta-glucoside has very good effects on inhibition of the proliferation of cells of liver cancer, gastric cancer and the like and induction of the apoptosis of cells and very small toxicity on normal cells, can be used for preparing the medicines for resisting liver cancer and gastric cancer or adjuvant chemotherapy medicines and can also be used as a food additive for preparing functional healthcare food for preventing and treating tumors.

The invention discloses a composite biological enzyme for a solvent method bamboo fabric, and a fabric surface cleaning method. The composite biological enzyme for the solvent method bamboo fabric is prepared through mixing the following components, by weight, 20-30 parts of an acidic cellulase, 7-15 parts of an enriched endonuclease, 4-8 parts of beta-glucosidase, 4-6 parts of sucrose, 4-6 parts of sodium chloride, and 35-45 parts of water. When the composite biological enzyme for the solvent method bamboo fabric is adopted to clean the surface of the solvent method bamboo fabric, the losses of the mechanic performances comprising the weight, the dry and wet fracture strengths, the fracture elongation rate and the like of the fabric are less, so the cleaning purpose of fibrillation removal is reached, and the color and the luster of the fabric are not influenced.

The invention belongs to the field of gene engineering, and particularly relates to glucose tolerance beta-glucosidase apbgl 1a and a gene and application thereof. According to the glucose tolerance beta-glucosidase apbgl 1a, the amino acid sequence of the glucose tolerance beta-glucosidase apbgl 1a is shown in SEQ ID NO.2. The glucose inhibiting constant Ki value of the glucose tolerance beta-glucosidase apbgl 1a reaches up to 1,886 mM, the most proper temperature is 45 DEG C, the most proper pH is 6.6, when the glucosidase is expressed in escherichia coli, some glucosidase can be secreted out of cells, the tolerance for SDS, ionic liquid, ethyl alcohol and the like is high, and the glucosidase can be applied to cellulosic ethanol production, feed processing, paper making, textile industry and other plant fiber hydrolytic processes.