189results about "Enzyme stabilisation" patented technology

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 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.

Provided is a method for improving the stability of urate oxidase. The inventors have discovered that combining an active ingredient urate oxidase or chemically modified urate oxidase with a stabilizer xanthine through a non-covalent bond can significantly improve the in vivo and in vitro stability of urate oxidase and chemically modified urate oxidase in the form of a tetramer, thereby effectively improving the stability of urate oxidase.

To provide a solid composition useful for various treatments of a hydrogen bonding material such as a biological sample.SOLUTION: A compound of formula (I) Wherein each R independently represents a linear or branched hydroxyalkyl group having one or more hydroxyl groups and an alkyl moiety having 1 to 10 carbon atoms; N represents an integer of 1 to 3. The solid composition contains the organic ammonium salt and a biological sample, wherein the mass ratio of the organic ammonium salt to the biological sample is 10:1 to 0.1:1.SELECTED DRAWING: None

The application belongs to the technical field of enzyme preparation processing, and specifically provides a preparation method of a gastric-stable enzyme preparation, which comprises the following steps: (1) placing enzyme liquid in a stirrer, adding stabilizers and carriers into the enzyme liquid, uniformly stirring, then adding emulsifiers and emulsion stabilizers, uniformly stirring again, obtaining enzyme mixture, and heating and keeping warm; (2) heating hot-melt type packaging materials to completely melt into liquid state, and keeping the packaging materials in liquid state; (3) starting the stirrer, slowly pouring the liquid hot-melt type packaging materials into the stirrer while stirring, and obtaining a material liquid; (4) spray drying the material liquid, and obtaining the gastric-stable enzyme preparation. The preparation method provided by the application effectively avoids the destruction of the prepared enzyme preparation by pepsin after the enzyme preparation enters the stomach of an animal, improves the enzyme activity retention rate of the enzyme preparation product after passing through the stomach, and further improves the stability of the enzyme preparation in the storage process, especially the storage stability in a humid environment.

[Problem] To provide a measurement reagent which contains lactate dehydrogenase, wherein the stability of the lactate dehydrogenase is improved in order to enable the measurement reagent to be used for a long period of time; and to provide a method for improving the stability of the lactate dehydrogenase. [Solution] An alkali metal compound is included in a reagent containing lactate dehydrogenase.

The application discloses a marine-derived cholesterol oxidase and a preparation method and application thereof, and relates to the technical field of biology. The amino acid sequence of the marine-derived cholesterol oxidase (SkChOx) is shown in SEQ ID NO. 1 or 3, the specific enzyme activity of the marine-derived cholesterol oxidase can reach 31.9 U / mg, the marine-derived cholesterol oxidase has excellent anti-reverse performance, maintains high stability in the pH range of 5.0-10.0, has good temperature tolerance, organic solvent tolerance and metal ion tolerance, and exhibits unique salt activation effect and salt tolerance. The enzyme is compounded with dithiothreitol (DTT) and nonylphenol polyoxyethylene ether (NP-40) to form a liquid enzyme preparation, and after incubation at 37 DEG C for 7 days under accelerated conditions, the catalytic activity of the liquid enzyme preparation still remains about 87%, the liquid enzyme preparation has excellent long-acting storage stability, and has wide application prospects in the fields of clinical diagnosis, food physical and chemical inspection, biosensor development and industrial preparation of steroid drugs.

The invention provides a rapid detection kit and a rapid detection method for phytosterol, and belongs to the field of food detection.The rapid detection kit for phytosterol comprises a phytosterol standard substance, a standard substance diluent, a substrate solution, an enzyme mixed solution, a stop solution and an elisa plate; the standard substance diluent comprises isopropanol or dimethyl sulfoxide; the substrate solution is prepared from TMB (Tetramethylbenzidine) and a substrate buffer solution; the enzyme mixed solution is a mixed solution of a cholesterol oxidase solution and a horse radish peroxidase solution. By optimizing the composition of each working reagent in the kit, the sensitivity and accuracy of phytosterol detection are remarkably improved. Meanwhile, the rapid detection method provided by the invention is simple and convenient to operate, short in detection time and suitable for on-site rapid detection.

The present invention relates to new polypeptides derived from arginase 2. The present invention also relates to uses of said polypeptides and compositions comprising said polypeptides.

Methods and compositions of storing a biological material are described herein. In some embodiments, these methods provide one or more advantages over current methods. For example, methods described herein can be used to prepare and process biological materials for storage at elevated temperatures. In one aspect, a method of storing a biological material comprises providing a preservation composition and exposing the preservation composition to electromagnetic radiation to form an amorphous solid matrix containing the biological material. In some embodiments, the method further comprises monitoring temperature of the preservation composition during the exposure to the electromagnetic radiation.

The present invention relates to a method for preparing an enzyme blend, the method comprising the steps of: providing a fermentation-derived preparation of a first enzyme of interest; exposing the first enzyme of interest preparation to a temperature higher than the fermentation temperature; purifying the first enzyme from the fermentation-derived preparation; and adding at least one second enzyme of interest to the purified first enzyme; thereby obtaining an enzyme blend. Furthermore, the present invention relates to an enzyme blend obtainable or obtained by the method according to the present invention.

The invention provides a liquid boron-free enzyme composition, comprising aliphatic 1,2-diols, which exhibit excellent physical and microbial stability.

An object of the present invention is to provide a technology for inhibiting the decline in nattokinase activity over time and providing excellent storage stability in an oral composition containing nattokinase. [Solution] An oral composition containing nattokinase together with black ginger extract, hesperidin, glycosyl hesperidin, α-linolenic acid, and / or rutin can inhibit the decrease in nattokinase activity during storage and has excellent storage stability.

The invention relates to the technical field of biotechnology, enzyme engineering and biological pharmacy, in particular to a ribonuclease purification production method. According to the method, a deep sea antifreeze polypeptide and rare earth nanocrystal composite bionic system is constructed, quorum sensing signal molecules and a pulsed electric field are introduced in a fermentation stage for two-factor regulation, and a light-operated micro-fluidic chip selective extraction technology is combined, so that efficient separation of target enzyme is realized. A double-ligand magnetic microsphere chromatographic column is innovatively adopted for gradient elution, and the enzyme activity retention rate and the long-term storage stability are remarkably improved through thermotropic liquid crystal capsule stabilization and radio frequency assisted freeze drying processes. According to the invention, the destructiveness of the traditional chromatography technology to enzyme conformation is broken through, the problem of batch fluctuation caused by multi-step purification is solved, a ribonuclease product with high purity, high activity and environmental response characteristic is provided for the field of biological medicine, and the ribonuclease is especially suitable for industrial preparation of gene therapy products and virus vectors.

According to the scheme, the recombinant macrolide enzyme and the preparation method and application thereof are provided, the amino acid sequence of the recombinant macrolide enzyme is shown as SEQ ID NO.1, and the recombinant macrolide enzyme is obtained by site-directed mutagenesis of an erythromycin esterase family protein sequence derived from enterobacter hormaechei; the mutation sites are as follows: the 44 glutamic acid is mutated into asparagine, the 55 tyrosine is mutated into proline, the 153 proline is mutated into alanine, and the 219 serine is mutated into glutamic acid, so that the specific macrolide lactonase which is efficient, stable, easy to prepare on a large scale and more suitable for environmental requirements is prepared, and macrolide antibiotic pollution is removed; and the method has good economic benefits and practical values.

To provide an immobilized enzyme composition for hexose production or an improved process for hexose production. [Solution] The present invention relates to an immobilized enzyme composition for the preparation of hexoses. Examples of hexoses include tagatose, psicose, fructose, allose, mannose, galactose, altrose, talose, sorbose, gross, idose, and inositol. The present invention also relates to an enzymatic process for preparing hexoses from sugars by contacting starch derivatives with the immobilized enzyme composition of the present invention.

To provide methods for increasing specificity of RNA-guided genome editing.SOLUTION: The present invention provides a method of increasing specificity of RNA-guided genome editing in a cell, the method comprising contacting the cell with a guide RNA that includes a complementarity region consisting of 17-18 nucleotides that are complementary to 17-18 consecutive nucleotides of the complementary strand of a selected target genomic sequence.SELECTED DRAWING: Figure 2-6

Proteases of Group IV (+)ssRNA viruses were found to act on a human sequences in addition to the viral sequences. The identity of the cleavable human sequences is disclosed. Detection of these sequences can act as a diagnostic of infection. It is contemplated that these findings could be employed to facilitate post-translational silencing at the level of protein (e.g., removal of existing proteins), thus serving as a protein analog to CRISPR / Cas9 and RNAi / RISC, and further to enable sequence-specific silencing of host functions without the modification of the host genome.

The present invention relates to enhancement and stabilization of proteolytic activity of proteases. The present invention discloses a method for enhancing and / or stabilizing the proteolytic activity of a protease, characterized in that said method comprises (i) contacting the protease with a reducing agent wherein the cysteine residues of the protease are maintained in the reduced state, (ii) removing substantially all of the oxygen from the area surrounding the protease, and (ii) removing the cysteine residues of the protease from the reducing agent. And (iii) binding the protease to an anionic polymer matrix such that the protease is non-covalently bound to the anionic polymer matrix.

To provide telomerase-containing exosomes for the treatment of diseases associated with aging and age-related organ failure. [Solution] This specification provides compositions of lipid-based nanoparticles (e.g., exosomes) containing therapeutic anti-aging agents. Furthermore, methods of using such compositions for treating patients with age-related disorders are also provided. In particular, exosomes containing RNA encoding telomerase, and methods of using them in the treatment of age-related disorders are provided. In one embodiment, this specification provides a composition comprising lipid-based nanoparticles containing a therapeutic agent cargo that enhances the activity of a telomerase complex. In some embodiments, the lipid-based nanoparticles contain CD47 on their surface. In some embodiments, the lipid-based nanoparticles contain a growth factor on their surface.

The present invention provides arginine deiminase mutants, covalent dimers, and complexes thereof, as well as uses thereof. Mutation of amino acid sites on the provided arginine deiminase mutant arginine deiminase results in the formation of covalent disulfide bonds between the arginine deiminase subunits. Covalent complexes and their use in the field of cancer treatment are also provided. Site-specific mutation of amino acid sites promotes the formation of covalent disulfide bonds between the subunits of homologous non-covalent dimeric arginine deiminase, making the structure of the formed dimer more stable. Furthermore, by reducing the exposure of antigen epitopes at the interaction interface, immunogenicity in the body can be reduced, resulting in better antitumor effects.

Provided are mucin-active proteases. In certain embodiments, the mucin-active proteases are stably associated with a targeting moiety. According to some embodiments, the mucin-active protease is stably associated with the targeting moiety via fusion of a protein domain comprising the mucin-active protease and a protein domain comprising the targeting moiety. In other embodiments, the mucin-active protease is stably associated with the targeting moiety via conjugation. Also provided are methods of treating a mucin-associated condition in a subject in need thereof, such methods comprising administering to the subject an effective amount of a mucin-active protease of the present disclosure. Upon administration of the mucin-active protease to the subject, the targeting moiety targets the mucin-active protease to cell surface, extracellular and / or secreted mucins, and the mucin-active protease degrades the mucins.

Provided is the process of producing an immunoligand / payload conjugate, in particularly, relates to a novel enzyme site-specific conjugation technology with dual enzyme orthogonal catalysis, comprising: conjugating a first payload to an immunoligand through the enzymatic catalysis of a first enzyme, conjugating a second payload to the immunoligand through enzymatic catalysis of a second enzyme, wherein the first enzyme is different from the second enzyme.

The application provides application of neutral protease in degradation of fumonisin, and belongs to the technical field of biology, and it is verified through experiments that the neutral protease has good degradation effect on FB1. The application also provides a compound enzyme preparation which comprises the following components: 1-5% neutral protease, 5-20% montmorillonite, 75-94% soluble starch, and only by adding 0.5wt%-1.5wt% of the compound enzyme preparation, the efficient degradation of FB1 in common contaminated feed can be realized; specifically, the degradation rate of the compound enzyme preparation on FB1 in corn flour can reach 95.73%, the degradation rate of the compound enzyme preparation on FB1 in DDGS can reach 96.43%, the degradation rate of the compound enzyme preparation on FB1 in corn steep liquor can reach 64.74%, and the degradation rate of the compound enzyme preparation on FB1 in corn cob powder can reach 93.74%.

Hybrid nuclease molecules and methods for treating an immune-related disease or disorder in a mammal, and a pharmaceutical composition for treating an immune-related disease in a mammal.

To provide methods for treating cellulosic biomass to produce cellulosic sugars, and products thereof.SOLUTION: A two-step method for activating cellulosic feedstock is described. The feedstock is subjected to a first high-temperature activation step at a temperature above 190°C. and a second activation step at a lower temperature under alkaline conditions. Also described are methods and compositions for the enzymatic hydrolysis of activated cellulose using one or more cellulase enzymes, a surfactant and polyaspartic acid. Also described are products of the methods.SELECTED DRAWING: None

To provide a type of hypoglycosylated modified kallikrein 1 and its PEG-modified derivatives and their application in medicine. The present invention provides KLK1 with no or only a small amount of glycosylation modification in the NFS sequence, which realizes high activity. The present invention also provides a recombinant KLK1 mutant with N-glycosylation modification only in NMS and NHT, which has the advantages of consistent sugar modification, uniform product molecular weight, high yield, simple purification, high biological activity and quality control. The present invention also provides PEGylated KLK1 with long-acting action, quality control, low immunogenicity and high biological activity, which reduces the frequency of administration and improves patient compliance, and realizes the application of drugs in the entire disease process, such as prevention, treatment, prognosis recovery, and recurrence prevention of acute ischemic stroke, peripheral neuropathy, retinopathy, ocular fundus disease, hypertension, diabetic nephropathy, IgA nephritis, chronic kidney disease, etc.