536results about "Enzyme stabilisation" patented technology

The invention discloses a recombinant C factor protein protective agent and application thereof. The recombinant factor C protein protective agent is prepared from the following components according to the final concentration of each component: 0.05 to 0.2 percent (w / v) of ProClin 300, 100 to 300 mM of sodium chloride, 1 to 10 mg / mL of bovine serum albumin, 5 to 20 percent (w / v) of trehalose, 10 to 50 percent (v / v) of glycerol, 0.1 to 0.5 percent (w / v) of tween-20 and 0.1 to 1 mM of ethylene glycol diethyl ether diamine tetraacetic acid with the pH value of 8.0. The invention also discloses an application of the recombinant factor C protein protective agent in refrigerated preservation of recombinant factor C protein. After the recombinant C-factor protein protective agent and the recombinant C-factor protein are mixed, the recombinant C-factor protein is prevented from being influenced by conditions such as aggregation, oxidation, freeze thawing and metal ion dependent inactivation, the stability of the recombinant C-factor protein in refrigeration storage is improved, and the activity retention rate of the recombinant C-factor protein after refrigeration storage for 12 months is greater than or equal to 90%; and the accuracy and sensitivity of endotoxin detection are maintained.

Provided herein are methods of inserting a nucleic acid encoding a polypeptide of interest into a target genomic locus in a cell or a population of cells in a subject, methods of expressing a polypeptide of interest from a target genomic locus in a cell or a population of cells in a subject, methods of treating an enzyme deficiency in a subject in need thereof, and methods of preventing or reducing the onset of a sign or symptom of an enzyme deficiency in a subject in need thereof. Some methods, such as when a subject has preexisting against an immunogen to be administered, use plasma cell depleting agents or combinations comprising plasma cell depleting agents to mitigate immune response and facilitate redosing of nucleic acid constructs encoding a polypeptide of interest and nuclease agents targeting a target genomic locus to achieve, for example, a step-wise increase in expression of a polypeptide of interest in a subject following insertion of the nucleic acid construct without overshooting. Other methods, such as when a subject has no preexisting immunity against an immunogen to be administered, use B cell depleting agents (e.g., anti-CD20xCD3 antibody or functional fragment thereof) to mitigate immune response and facilitate redosing of nucleic acid constructs encoding a polypeptide of interest and nuclease agents targeting a target genomic locus to achieve, for example, a step-wise increase in expression of a polypeptide of interest in a subject following insertion of the nucleic acid construct without overshooting.

The invention discloses a polypeptide ligand for improving the thermal stability of MMLV reverse transcriptase and application of the polypeptide ligand, and relates to the technical field of biology. The invention specifically discloses a polypeptide ligand with an amino acid sequence as shown in SEQ ID NO: 1. The polypeptide ligand can obviously improve the thermal stability of MMLV RT. After being combined with the polypeptide ligand, the MMLV RT can effectively maintain the activity of the MMLV RT at 45-60 DEG C and maintain good activity in a freeze-thaw cycle, and the Ct value change is small after the MMLV RT is placed at 37 DEG C for more than 15 days, so that the polypeptide has a very good application prospect in industrial production and commercial application.

The present invention provides an enzyme preparation for laundry detergent that can effectively improve the washing effect. The enzyme preparation for laundry detergent includes a protease component, a lipase component, and polyethylene glycol. The protease component includes a protease and a protease carrier for immobilizing the protease. The protease carrier includes a porous nanomaterial and polydopamine formed on the surface of the porous nanomaterial. The lipase component includes a lipase and sodium polyoxyalkylene sulfosuccinate. In the enzyme preparation for laundry detergent provided in this solution, the protease and the lipase can maintain good activity for a long time. Therefore, when the enzyme preparation for laundry detergent provided in this solution is applied to the preparation of laundry detergent, the washing effect of the laundry detergent can be effectively improved.

An object of the present invention is to provide a lactase solution showing good permeation through a filtration filter, a lactase solution showing good permeation through a filtration filter and having a good residual lactase activity, and a lactase solution showing good permeation through a filtration filter and having a good residual lactase activity even when a lactase solution having a low protease activity and a low arylsulfatase activity as contaminant enzymes is used.A lactase solution containing any of (i) to (iii) below.(i) 0.0001 to 0.1 mass % of an unsaturated fatty acid or a salt thereof(ii) 0.0001 to 0.1 mass % of a saturated fatty acid salt(iii) 0.01 to 10 mass % of at least one selected from yeast extract, soybean peptone, pea protein, a casein degradation product, and corn steep liquor

The invention discloses a bacterium-enzyme mixed preparation for PET plastic degradation and a preparation method thereof, and belongs to the technical field of enzyme preparations, a lanthanum metal framework is formed, loaded on the surface of titanium dioxide and carbonized to obtain a lanthanum-doped porous carbon layer, and then nitric acid treatment and silane coupling agent treatment are performed to significantly increase the specific surface area and roughness, so that the specific surface area is increased; the calcium-based diatomite is taken as a carrier to form a sodium alginate microcapsule taking an enzyme preparation as an inclusion, and the sodium alginate microcapsule is loaded on the surface of the calcium-based diatomite, so that the situation that titanium dioxide generates hydroxyl free radicals in photocatalysis to directly attack the enzyme preparation is avoided, and the degradation effect on the PET plastic is prolonged; calcium ions in the calcium-based diatomite can increase the crosslinking degree with the sodium alginate, the load rate of the sodium alginate microcapsule is increased, the strength of the microcapsule is improved, and the slow release effect of an enzyme preparation in the microcapsule is further improved.

The invention belongs to the technical field of bioengineering and food safety, and particularly relates to a fusion enzyme for degrading aflatoxin B1 (AFB1) and / or zearalenone (ZEN) and application of the fusion enzyme. The fusion enzyme S1-AsDPP III disclosed by the invention can effectively degrade AFB1 and ZEN, the fusion enzyme is obtained by fusing a section of self-assembled amphiphilic oligopeptide S1 sequence at the N end of wild type AsDPP III, and the thermal stability of the fusion enzyme and the amphipathy of the fusion enzyme in an oil-water coexistence system can be remarkably improved. Under mild reaction conditions, the fusion enzyme can efficiently degrade AFB1 and ZEN in vegetable oil, and is especially suitable for detoxification treatment of common edible oil such as peanut oil and corn oil. The invention provides a green, safe and efficient scheme for removing fungaltoxin from grease food, and the method has a good industrial application prospect.

The invention relates to the technical field of molecular biology, and provides a DNA origami structure with enhanced stability in a DNA polymerase environment as well as preparation and application of the DNA origami structure. An optional number of conventional staple chains; one or more anti-enzymolysis staple chains, wherein the anti-enzymolysis staple chain comprises a staple section and a suspension section for preventing DNA polymerase degradation; wherein staple sections of the skeleton chain, the conventional staple chain and the anti-enzymolysis staple chain form a DNA origami body, and the DNA origami body comprises a plane or curved surface structure; in addition, the hanging section of the anti-enzymolysis staple chain is exposed out of the DNA origami body, and the hanging section is provided with a polyT block. The stability of the DNA origami structure in a DNA polymerase environment is effectively improved, characterization and analysis are facilitated, and the application range of the DNA origami structure in different enzyme systems is widened.

According to the scheme, the invention provides the recombinant macrolide enzyme as well as the preparation method and the application thereof, the amino acid sequence of the recombinant macrolide enzyme is as shown in SEQ ID NO.1, and the recombinant macrolide enzyme is derived from an EreC esterase family of enterobacter hormaechei and is obtained through site-specific mutagenesis; the mutation sites are as follows: glutamic acid at the 44th site is mutated into asparagine, tyrosine at the 55th site is mutated into proline, proline at the 76th site is mutated into arginine, phenylalanine at the 153rd site is mutated into alanine, and serine at the 219th site is mutated into glutamic acid. The method is expected to remove macrolide antibiotic pollution, and has good economic benefits and practical values.

The invention discloses a polypeptide ligand of MMLV reverse transcriptase and application of the polypeptide ligand, and relates to the technical field of biology. The invention specifically discloses a polypeptide ligand with an amino acid sequence as shown in SEQ ID NO: 1, the stability of MMLV reverse transcriptase can be remarkably improved, the MMLV reverse transcriptase can be placed at 37 DEG C for more than 15 days, and the Ct value difference is lower than 2; in addition, the MMLV reverse transcriptase activity can be maintained under a high-temperature condition (45-60 DEG C); the activity loss of the MMLV reverse transcriptase in a freeze-thaw cycle is reduced, and the industrial production and commercial application of the MMLV reverse transcriptase are effectively promoted.

The invention relates to the technical field of pepsin preparation, in particular to a chemical modifier and a method for preparing pepsin through the chemical modifier, a novel composite modifier Mal-PEG-CMC is synthesized, and the modifier with good water solubility and high coupling rate is obtained by optimizing the molecular weight of PEG, the molar ratio of PEG to maleic anhydride, the substitution degree of CMC and the coupling ratio; the chemically modified pepsin is prepared based on the modifier, and the modified pepsin is obtained through the steps of pepsin purification, sulfydryl exposure through DTT pretreatment, targeted modification reaction and purification. The performance of the modified pepsase is remarkably improved, the pepsase is suitable for animal source and recombinant expression pepsase, the application bottleneck of natural enzyme is effectively broken through, and the pepsase has important value in the fields of food processing, medicine and the like.

The invention discloses an anti-Taq DNA polymerase antibody or an antigen binding fragment thereof and application thereof, and relates to the technical field of biology. The antibody or the antigen binding fragment of the antibody can be specifically bound with Taq DNA polymerase, the polymerization activity and / or excision activity of the Taq DNA polymerase are / is blocked, and the stability of the Taq DNA polymerase is improved.

The present invention relates to aqueous compositions, and more specifically aqueous compositions for replicating a nucleic acid template, wherein the composition comprises D2O, as well as to methods and uses relating to such compositions. The composition can be used, for example, in a method of storing the composition, or a method for replicating a nucleic acid template, for instance for the synthesis of Xpandomers for sequencing by expansion.

The invention provides a preparation method and application of an anti-caking agent for amylase, and the preparation method comprises the following steps: step 1, uniformly mixing metered calcium silicate, calcium stearate and water to obtain a first treated substance; step 2, performing ball milling on the first treated object in a ball mill to obtain a second treated object; and 3, carrying out suction filtration on the second treated substance, and drying to obtain the target anti-caking agent. Hydrophobic long chains of calcium stearate are adsorbed on the surface of calcium silicate to form a hydrophobic coating layer, and are uniformly dispersed on the surfaces of amylase particles, so that water contact is blocked, and moisture absorption and caking are reduced; on the other hand, the hydrophilic end of calcium stearate and ions on the surface of calcium silicate are subjected to weak ion exchange or coordination, the microenvironment around amylase is changed, the hydrophilicity of the amylase is reduced, meanwhile, the surface activity of the anti-caking agent is enhanced through structural change generated by ball milling, and the anti-caking agent can be used for improving the anti-caking effect through hydrogen bonds formed with amylase molecules, Van der Waals force and other interactions. The starch is tightly attached to the surfaces of amylase particles to prevent moisture absorption and caking, so that the performance of the amylase is ensured.

The invention provides a polydopamine cross-linked lipase aggregate and a preparation method thereof, and relates to the technical field of enzyme immobilization. The polydopamine cross-linked lipase aggregate is mainly prepared from lipase and a dopamine hydrochloride cross-linking agent through a Schiff base and Michael addition reaction and a cross-linked enzyme aggregate technology. The preparation method of the polydopamine cross-linked lipase aggregate is simple, convenient and controllable; the prepared polydopamine cross-linked lipase aggregate still has excellent enzyme activity in a heavy metal salt solution.

The invention relates to the technical field of cyanobacterial bloom control in water, and particularly discloses a compound enzyme-bacterium synergistic preparation for cyanobacterial bloom control, a preparation method and a use method. The preparation comprises the following components in percentage by mass: compound enzymes (10-20% of cellulase, 8-12% of beta-1, 3-glucanase and 3-8% of lipase), functional bacteria (10-20% of bacillus subtilis, 8-15% of trichoderma harzianum and 5-10% of bacillus amyloliquefaciens), an enzyme stabilizer (3-8% of trehalose), an adsorption carrier (15-25% of Fe < 3 + > modified charcoal and 8-15% of diatomite) and auxiliary components. The preparation method comprises the steps of carrier modification, solid fermentation and microcapsule embedding. During use, 3-20kg / 1000m < 3 > of water is added for the first time, 2-10kg / 1000m < 3 > of water is added every 7-14 days in the maintenance stage, and synchronous aeration is performed. Through the synergistic effect of beta-1, 3-glucanase and trichoderma harzianum, the algicidal rate is 92%, and the spore germination inhibition rate is 82%; the Fe < 3 + > modified charcoal improves the stability of the enzyme in an alkaline environment (80% of activity is retained when the pH value is 9); the method is suitable for eutrophic water with chlorophyll a greater than or equal to 30 [mu] g / L, and has no chemical residue risk.

The invention relates to the technical field of enzyme preparations, in particular to an agricultural biological compound enzyme preparation and a preparation method thereof.The agricultural biological compound enzyme preparation is prepared from, by weight, 30-50 parts of compound enzyme, 5-8 parts of trehalose, 3-5 parts of glycerin, 15-20 parts of copolymer carrier, 5-8 parts of humic acid, 5-10 parts of bran, 3-5 parts of dipotassium phosphate and 85-124 parts of water. The compound enzyme contains various enzymes such as cellulase, lysozyme and protease, can synchronously decompose various organic substances such as cellulose, microbial cell walls and protein in soil and release nutrients such as nitrogen, phosphorus and potassium, has more comprehensive functions compared with a single enzyme preparation, and can meet the requirements of complex soil and crops in agricultural production.

Described are methods for producing recombinant Arginase, such as PEGylated, cobalt-substituted recombinant human Arginase 1. Also described are pharmaceutical compositions comprising such recombinant Arginase, as well as methods of treatment and uses of such recombinant Arginase.

Provided are freeze-drying auxiliary materials, a freeze-drying preservation solution and the use thereof. The freeze-drying auxiliary materials comprise a carbohydrate, an amino acid and an adjuvant in a mass ratio of (4-20):(2-12):(3-15), wherein the adjuvant comprises one or more of polyvinylpyrrolidone, polyethylene glycol, mannitol and bovine serum albumin. By selecting carbohydrates and amino acids at specific concentrations, along with particular types of adjuvants as the freeze-drying auxiliary materials, where the components cooperate with each other and work together, the resulting freeze-drying preservation solution prepared therefrom, when used for storing an ALP enzyme, can seal and store the ALP enzyme at ambient temperature for 18 months or more, and keep the preservation rate of enzyme activity at 87% or more after the ALP enzyme is placed at the high temperature of 50℃ for 3 weeks.

The invention discloses lysozyme condensed microdroplets as well as a preparation method and application thereof. The lysozyme condensed microdroplet comprises egg white source lysozyme, food protein, edible inorganic salt and water, wherein the food protein comprises at least one of beta-conglycinin and beta-lactoglobulin. The preparation method of the lysozyme condensed microdroplet comprises the following steps: 1) preparing an egg white source lysozyme dispersion liquid and a food protein dispersion liquid; and 2) mixing the two dispersion liquids, and stirring until liquid-liquid phase separation occurs. The lysozyme condensed microdroplet is good in thermodynamic stability and long-term storage stability, the lysozyme is high in mobility in the condensed microdroplet and high in accessibility to a substrate, has long-acting antibacterial and preservative effects, is suitable for being used as a food additive, and is simple in preparation method, green and environment-friendly in process, wide in raw material source, low in production cost, low in energy consumption and suitable for industrial production. The method is suitable for large-scale industrial production and application.

The present disclosure provides adenosine deaminases that are capable of deaminating adenosine in DNA. [Solution] The present disclosure also provides fusion proteins comprising a Cas9 (e.g., Cas9 nickase) domain and an adenosine deaminase that deaminates adenosine in DNA. In some embodiments, the fusion protein further comprises a nuclear localization sequence (NLS) and / or an inhibitor of base repair, such as a nuclease-inactive inosine-specific nuclease (dISN).

The present compositions and methods relate to thermostabilization of phytase with phosphate and increasing the recovery of phytase during the production of heat-treated food or animal feed pellets that contain phytase.

The present invention proposes a method and use for stabilizing a simple agglomerate for pH and salt and with adjustable size. In phosphoric acid buffer solutions with different salt concentrations and pH values, the polyacrylic acid hydroxypropyl group condensation body has specific stability; hydrophobic thermal response blocks are introduced into a hydroxypropyl acrylate monomer through reversible addition-fragmentation chain transfer polymerization to regulate and control the size of a condensation body, and a phase separation behavior is shown at different temperatures; a hydrophobic block without thermal response is introduced to regulate and control the size of the aggregate, and no thermal response behavior is shown. Continuous regulation and control of the size of the aggregate from the micron level to the nano level are achieved, and the requirements of different application scenes are met. The hydroxypropyl polyacrylate condensation body can be used for packaging various dyes and drugs; high-efficiency enzyme protection is achieved, formed aggregates can protect glucose oxidase, and the retention rate of enzyme activity reaches 85% or above after treatment is conducted for 3 hours at 60 DEG C; as a micro-reactor for the reaction of generating p-nitrobenzaldehyde phenylhydrazone from p-nitrobenzaldehyde and phenylhydrazine, the reaction rate is greatly improved.

The present invention relates to methods and cross-linkers for the macrocyclization of proteins. The invention is useful for increasing the stability of a protein.

The present invention relates to novel enzyme nanoparticles capable of converting methane into methanol, in which key active sites of methane-oxidizing bacteria are fused with each other and expressed on a protein that can be self-assembled in cells to form nanoparticles, and specifically to enzyme nanoparticles including a protein having methane monooxygenase (MMO) activity and active sites of the methane oxidase, a method for production thereof, a recombinant microorganism into which a nucleic acid encoding the protein and the active site of the methane oxidase is introduced, and immobilized enzyme nanoparticles including the enzyme nanoparticles loaded on a carrier.

The present application relates to the technical field of small molecule peptide preparation, and specifically discloses a preparation process of selenium-rich antioxidant pig lung polypeptide. The preparation process of the selenium-rich antioxidant pig lung polypeptide comprises the following steps: washing and decontaminating fresh pig lung, peeling off the trachea, removing grease, and twisting into a minced meat shape to obtain pig lung pre-preparation material; mixing the pig lung pre-preparation material with a vitamin C aqueous solution, adding nano-silicon dioxide powder and eugenol to the mixture, and performing ultrasonic treatment; cooling to-10 to-30 DEG C, keeping for 1 to 2 hours, and then increasing the temperature to room temperature; homogenizing treatment, filtration, collecting the precipitate, and obtaining pretreated pig lung; adding water to the pretreated pig lung and stirring until uniform; adjusting the pH value of the system; adding a stabilizing alkaline protease for treatment; adjusting the system to be neutral; adding a neutral protease for enzymolysis; and cooling to room temperature to obtain pig lung enzymolysis liquid; centrifuging the pig lung enzymolysis liquid, ultrafiltering, collecting the permeate, nanofiltrating, collecting the concentrated liquid, and drying.

The invention belongs to the technical field of bioengineering, and particularly provides a stable liquid alkaline protease preparation which comprises liquid alkaline protease, NaCl, polysaccharide and histidine. Based on the mass of the liquid alkaline protease, the addition amount of NaCl is 5%-10%, the addition amount of polysaccharide is 0.1%-0.5%, and the addition amount of histidine is 0.02%-0.1%. According to the stable liquid alkaline protease preparation provided by the invention, NaCl, polysaccharide and histidine are added into alkaline protease, filtration and sterilization are performed after pH is adjusted, the stability of the liquid alkaline protease is obviously improved, heat preservation is performed for 6 months at the temperature of 45 DEG C, and the enzyme activity is basically free of loss. The preparation has simple components and is especially suitable for feed and food industries.

The present invention relates to hybrid nuclease molecules and methods for treating immune-related diseases or conditions in mammals, as well as pharmaceutical compositions for treating immune-related diseases in mammals.

The invention relates to the technical field of reagent preservation, in particular to biotinylated tyrosine phosphatase antigen preservation liquid as well as a preparation method and application thereof. The pH value of the biotinylated tyrosine phosphatase antigen preserving fluid is 7.0-7.5, and the biotinylated tyrosine phosphatase antigen preserving fluid is prepared from the following raw material components: a buffering agent, soluble metal salt, an organic dispersing agent, poly (ethylene glycol)-block-poly (propylene glycol)-block-poly (ethylene glycol) 8400, a metal ion complexing agent, bovine serum albumin, a protein protective agent and a preservative. By optimizing the components of the biotinylated tyrosine phosphatase antigen preserving fluid, when the prepared antigen preserving fluid is used for preserving a biotin-labeled tyrosine phosphatase antigen, the storage life is greatly prolonged under the condition of 2-8 DEG C. The biotinylated tyrosine phosphatase antigen preserving fluid prepared by the method is convenient to use, stable to store, economical and practical, and simple to prepare.