67 results about "Serine protease" patented technology

The invention discloses bacillus subtilis Bs1 as well as an antagonistic substance and application thereof. According to the invention, Bs1 with antagonism on colletotrichum gloeosporioides is separated and screened for the first time, an antagonistic substance is clear as Bs1 serine-producing protease Vpr, a Bs1 bacteriostasis mechanism and biological control potential excavation are analyzed in a multi-omics manner, a peripheral colonization rule of Bs1-Rif is clear, and an indoor control strategy of the strain Bs1 on cunninghamia lanceolata anthracnose is optimized. When the strain Bs1 is applied on the day when pathogenic bacteria are inoculated, a certain prevention and treatment effect is achieved, and it is indicated that the strain Bs1 can rapidly occupy the ecological niche; the average antibacterial rate of the strain Bs1 can reach 66.69%. The biocontrol strain and theoretical basis are provided for prevention and control of Chinese fir diseases, the application of biological prevention and control in forestry is promoted, the interaction mechanism of biocontrol bacteria and pathogenic bacteria can be deeply understood, and the sustainable development requirement of modern forestry is met.

The invention discloses a casein peptide composition containing multifunctional peptide and a preparation method of the casein peptide composition. The present invention provides a casein peptide composition containing a multifunctional peptide, characterized in that the casein peptide composition is obtained by enzymatic hydrolysis of a casein liquid, in the casein peptide composition, the relative strength of total functional peptides is 25% or more, the relative strength of casein phosphopeptides is 9% or more, and the relative strength of the casein phosphopeptides is 9% or more. The relative strength of the functional peptides except the casein phosphopeptides is above 11%, and the enzyme in the enzymolysis at least comprises serine protease.

A method for treatment of one or more toxin(s) in a subject, that includes administering to the subject a therapeutically effective amount of a serine protease that enzymatically cleaves certain toxins. Also, a method for preventing disease progression in a subject infected by Clostridioides difficile (CD), diarrhea, or infectious colitis, which includes administering to the subject a therapeutically effective amount of the protease. The protease retains its activity up to 65° C. Treatment with the protease in mice infected with CD conferred a 10-fold survival benefit compared to mice infected with CD and untreated.

An object of the present invention is to provide a therapeutic or preventive agent for myocardial infarction, cardiac fibrosis, or heart failure using Htra3 as a therapeutic target. According to the present invention, there is provided a therapeutic or preventive agent for myocardial infarction, cardiac fibrosis, or heart failure containing at least one of (a) serine protease HtrA3, (b) a nucleic acid encoding HtrA3, (c) an expression vector containing a nucleic acid encoding HtrA3, (d) a cell transformed with the nucleic acid or the expression vector, and (e) an antibody that binds to serine protease HtrA3.

To provide an antigen-binding protein comprising an antigen-binding domain that binds to plasmin. Also provided are compositions comprising the antigen binding proteins, as well as uses thereof and methods of treatment comprising the same.SOLUTION: To provide antigen-binding proteins or antigen-binding fragments thereof that specifically bind to the serine protease domain of plasmin and inhibit or reduce plasmin activity via interaction with the catalytic site of the protein.SELECTED DRAWING: None

This invention discloses a highly efficient serine protease for degrading α-keratin, its degradation method, and its applications. The serine protease is named PliKerS, and its full-length amino acid sequence is shown in SEQ ID No. 2, with the corresponding coding gene sequence shown in SEQ ID No. 1. The amino acid sequence of the recombinant serine protease rPliKerS, which has its N-terminal signal peptide removed and a purification tag attached to its C-terminus, is shown in SEQ ID No. 4, with the corresponding coding gene sequence shown in SEQ ID No. 3. The recombinant serine protease rPliKerS degrades α-keratin under mild conditions, avoiding the environmental burden of strong alkaline treatment. It is particularly suitable for applications involving pet hair, hair waste, and leather pretreatment. The degradation products are soluble proteins and peptides, which can be used as high-value-added amino acid raw materials, functional peptide raw materials, biodegradable materials, bio-based material precursors, bio-feed proteins, fertilizers, etc., exhibiting high resource utilization value and promising industrial application prospects.

The present invention provides a method for improving the digestibility of a carbohydrate by a carbohydrase in an animal feed such as soybean-meal, corn, wheat, wheat middlings, oats, rye, barley and sorghum; and / or roughages such as hay and pasture plants, or mixture thereof by adding one or more proteases, preferably a serine protease such as a Nocardiopsis serine protease or a S8 serine protease. The present invention also provides a feed composition suitable for the above methods.

The present invention relates generally to a method of detecting inhibitory effects of health supplements on serine protease in cell lines derived from human carcinomas. More, particularly, the present invention relates to inhibitory analysis of health supplementary products taken from market and / or chemically purified forms, in order to determine their competitors and / or inhibitory effects on serine protease such as trypsin so that these supplements can be used for the treatment once someone develop intense inflammatory reactions either due to infections like COVID-19 and / or pathological conditions such as cancer. The present invention further provides therapeutic applications for agents and / or condition which utilize human enzymatic system and / or cellular components for the development of pathological conditions.

Provided herein are polypeptides, nucleic acids, and cells comprising antigen-binding domains that specifically bind to Solute Carrier Family 34 Member 2 (SLC34A2) or Transmembrane protease, serine 4 (TMPRSS4), and methods of use thereof. Also provided are polypeptides, systems, nucleic acids, and cells comprising priming receptors comprising an antigen-binding domain that specifically binds Solute Carrier Family 34 Member 2 (SLC34A2) and chimeric antigen receptors (CAR) comprising an antigen-binding domain that specifically binds to Transmembrane protease, serine 4 (TMPRSS4).

The invention relates generally to polypeptides that include at least a first cleavable moiety (CM1) that is a substrate for at least one matrix metalloprotease (MMP) and at least a second cleavable moiety (CM2) that is a substrate for at least one serine protease (SP), to activatable antibodies and other larger molecules that include these polypeptides that include at least a CM1 that is a substrate for at least one MMP protease and at least a CM2 that is a substrate for at least one SP protease, and to methods of making and using these polypeptides that include at least a CM1 that is a substrate for at least one MMP protease and at least a CM2 that is a substrate for at least one SP protease in a variety of therapeutic, diagnostic and prophylactic indications.

The present disclosure provides synthetic compositions useful as inhibitors of mannan-binding lectin-associated serine protease-2 (MASP-2), including compositions that selectively inhibit MASP-2 over thrombin, as well as methods for their production and use.

The invention belongs to the technical field of biological medicines, and particularly relates to application of ackermania muciniphila and recombinant trichina serine protease carried by a derivative of the ackermania muciniphila to preparation of a medicine for treating intestinal inflammation symptoms. According to the present invention, the ackermann muciniphila and the ackermann muciniphila derivative carrying recombinant trichina serine are firstly disclosed, such that the physical barrier of the intestinal mucosa is repaired through the synergistic effect, the expression of TNF-alpha, IL-6, IL-1beta and other proinflammatory factors is specifically regulated and inhibited, the intestinal flora structure is remodeled, and the intestinal inflammation state is significantly improved; experimental results show that the Ackerman muciniphila and the derivative thereof carrying the recombinant trichina serine protease can significantly relieve weight loss of mice with intestinal inflammation induced by DSS, reduce DAI score, and reverse the phenomena of shortened colon and abnormal swelling of spleen. According to the invention, the probiotics and the parasite-derived protein are combined, so that the method has the advantages of high efficiency, safety and easiness in large-scale production, and a new biological preparation strategy is provided for accurate treatment of IBD.

The application discloses a latex-enhanced immunoturbidimetric detection reagent and application of a serine protease in the latex-enhanced immunoturbidimetric detection reagent, relates to the technical field of biological detection, and can reduce the interference of a matrix component on the binding of a target and an antibody, reduce the probability of non-specific binding, and improve the accuracy of detection by pretreating a to-be-detected sample by using a reagent R1 containing the serine protease; the difference between a sample matrix and a quality control product matrix can be avoided, the accuracy and reliability of a detection result are improved; the difference between different quality control product matrices can be eliminated, the difference between standard curves obtained by using different matrix quality control products is reduced, and the compatibility of three-party quality control is enhanced.

It provides an inhibitor of complement activation. [Solution] An isolated monoclonal antibody and its antigen-binding fragment are provided that specifically bind to an epitope within the serine protease domain of human MASP-2. In some embodiments, the antibody or its antigen-binding fragment inhibits lectin pathway complement activation. Polynucleotides encoding the monoclonal antibody or its antigen-binding fragment, and cloning vectors or expression cassettes containing such polynucleotides are also provided. Methods for inhibiting lectin pathway complement activation and methods for treating diseases and disorders of the lectin pathway are further provided.

The invention belongs to the field of enzyme engineering and agricultural waste conversion, and particularly relates to a preparation method and application of a keratinase mutant for efficiently degrading feather feed in an acidic gastric juice environment. The method comprises the following steps: replacing amino acid Arg247 with positive charges on the zymoprotein surface based on cotG-KERQ7 in an environment with the pH value of 4, then carrying out rational design on the chemical property of a KERQ7 oxygen negative ion cave, and directly introducing acidic amino acid, so that a mechanism that the serine protease oxygen negative ion cave actively dynamically adjusts the charge density through pH-dependent protonation is introduced, and the pH-dependent protonation of the serine protease oxygen negative ion cave is changed into the pH-dependent protonation of the serine protease oxygen negative ion cave. According to the method, the keratinase is used as a raw material, the oxygen anion hole adaptive low-pH environment mutant is obtained, the acid stability and activity of the keratinase mutant are both improved, an efficient mutant enzyme preparation with activity and acid resistance remarkably improved in the low-pH environment is finally obtained, reference is provided for subsequent improvement of the application value of the keratinase in the feed industry, and the method has a wide application prospect. Wide market application prospects are realized.

This application relates to a wastewater treatment device for the preparation of recombinant plasmids of serine protease, comprising, in sequence: an inactivation module, a chemical pretreatment process, and a biodegradation process; the inactivation module includes: a pre-inactivation collection tank for receiving wastewater; a heat exchange device for heating the wastewater with high-temperature steam; and an inactivation tank for inactivation operations through heat preservation and pressure maintenance; the heat exchange device includes: a heat exchange cylinder with a shell and tube containing high-temperature steam and connecting the pre-inactivation collection tank and the inactivation tank; a cleaning mechanism for scraping the tube wall by rotation; and a power mechanism for converting the kinetic energy of the fluid inside the heat exchange cylinder into the power for the rotation of the cleaning mechanism. This application automatically cleans the scale and fouling on the inner wall of the heat exchange cylinder, and can also clean the heat exchange cylinder in a cold state, ensuring an extended service life and increased efficiency of the heat exchange cylinder during wastewater treatment.

The invention belongs to the field of biological medicine and protein engineering, and particularly relates to a preparation method of a protease cryoelectron microscope sample and a protease structure analysis method. The preparation method comprises the following steps: providing an enzyme solution of target protease, adding an enzyme inhibitor of the target protease, incubating an obtained mixture, and collecting an incubation product supernatant; and sucking the incubation product supernatant to prepare a cryoelectron microscope sample, the target protease comprises serine protease, the target protease is located on a cell membrane, or / and the target protease depends on ATP (adenosine triphosphate). According to the method, the freezing electron microscope sample is prepared after the enzyme inhibitor of the target protease is added into the enzyme liquid of the target protease for incubation, so that the problems of depolymerization of the membrane protease and instability of a protein soluble region can be solved, and a freezing electron microscope structure of the full-length membrane protease can be successfully analyzed in electron microscope observation; and accurate reference is provided for subsequent design of specific targeted drugs.

The present invention relates to a genetically modified plant or plant cell derived from a wild-type plant or plant cell, said wild-type plant or plant cell producing at least one serine protease comprising the motif SSRGPX1LKPDX2X3APGX4SGTSMSCPHX5PX6WSPX7AX8X9SAX10MTT (SEQ ID No. 1), whereinX1 is a peptide consisting of 7 amino acid residues, X2 is I or L, X3 is T or M, X4 is a peptide consisting of 27 or 28 amino acid residues, X5 is a peptide consisting of 12 amino acid residues, X6 is T or E, X7 is S or A, X8 is V or I, X9 is K or R and X10 is I or M, wherein the proteolytic activity of the at least one serine protease in the genetically modified plant or plant cell is reduced compared to its activity in the wild-type plant or plant cell, wherein the genetically modified plant or plant cell comprises at least one exogenous nucleic acid molecule encoding for at least one protein or polypeptide of interest.

The invention relates to the technical field of marine technology and enzyme, and particularly discloses alkaline serine protease and application thereof. The brand-new alkaline serine protease is successfully mined by using a marine-derived microbial metagenome database, the limitation of conventional microbial isolated culture is overcome, and the source selection range of the alkaline serine protease is greatly widened. Moreover, the alkaline serine protease has excellent protease activity and detergent tolerance, and can be effectively used for protein degradation or used as a detergent component.

The invention discloses a sweet protein homotrimer as well as a preparation method and application thereof, and belongs to the technical field of genetic engineering. According to the technical scheme, the strategy of self-assembly of interchain disulfide bonds mediated by a PCA trimerization structural domain is adopted, the PCA trimerization structural domain is derived from a C-terminal fragment of snake venom serine protease, a stable homotrimer is spontaneously formed through the interchain disulfide bonds under the oxidation condition, and the stable homotrimer is used as an artificial trimerization'molecular rivet '; the PCA trimerization structural domain fragment is fused with sweet protein, controllable trimer assembly can be achieved in cells and / or outside cells, and no extra cross-linking agent is needed. Based on this, a sweet protein homotrimer is obtained from a sweet protein monomer; the sweet protein homotrimer has good thermal stability and pH tolerance, and a new technical platform is provided for industrial production of high-sweetness and high-stability functional protein.

The invention relates to a preparation method of a biodegradable medical suture with gradient mechanical properties, and belongs to the field of medical materials. Adding the polylactic acid suture line into absolute ethyl alcohol for ultrasonic treatment; putting the pretreated polylactic acid suture into a serine protease solution, adding cassia oil and baking soda, sealing, performing constant-temperature oscillation treatment, fully washing with distilled water, airing, and drying; the serine protease surface modified polylactic acid suture line is twisted by using twisting equipment, and the mechanical property of the suture line is adjusted by adjusting the number of twists to form a gradient. According to the biodegradable medical suture with the gradient mechanical property, the high-strength end has the high mechanical property, and wound closure can be effectively maintained; the mechanical property of the low-strength end is low, the degradation rate is gradually increased, and wound healing is promoted.

The application belongs to the field of biological medicine and protein engineering, and particularly relates to a preparation method of a proteinase cryo-EM sample and a structural analysis method of the proteinase. The preparation method comprises the following steps: providing an enzyme solution of a target proteinase, adding an enzyme inhibitor of the target proteinase, collecting an incubation product supernatant after the obtained mixture is incubated, and preparing a cryo-EM sample by sucking the incubation product supernatant; the target proteinase comprises a serine protease, the target proteinase is located on a cell membrane, and / or the target proteinase is dependent on ATP. The application prepares a cryo-EM sample after the enzyme solution of the target proteinase is incubated by adding the enzyme inhibitor of the target proteinase, so that the problems of depolymerization of a membrane proteinase and instability of a protein soluble region can be overcome, the cryo-EM structure of a full-length membrane proteinase is successfully analyzed in electron microscope observation, and a precise reference is provided for subsequent design of specific targeted drugs.

The invention discloses application of a casein peptide composition based on lactoalbumin hydrolysate to intestinal protection and / or auxiliary improvement of an enteritis discomfort state. The invention provides an application of a casein peptide composition in preparation of a product for intestinal protection and / or auxiliary improvement of an uncomfortable state of enteritis, and the casein peptide composition is prepared by the following method: an enzymolysis step: carrying out enzymolysis on a casein solution by adopting compound protease; wherein the compound protease comprises serine protease and flavourzyme. Through the casein peptide composition provided by the invention, reasonable molecular weight distribution control is realized, and the casein peptide composition has more excellent effects of protecting intestinal tracts and / or assisting in improving the discomfort state of enteritis.

The present invention relates to a composition comprising a laccase and optionally a serine protease, and to the use of said composition in the treatment of melanin and / or phenolic organic compounds, for example as a laundry composition, a cleaning composition, a whitening cosmetic composition.

The present application relates to a guppy trichodinid third generation recombinant kunitz protein and a preparation method and application thereof, and belongs to the technical field of fish parasite protein expression and functional application research.The serine protease inhibitor of the guppy trichodinid third generation in the present application is a GcKSI protein, and the amino acid sequence of the GcKSI protein is shown as SEQ ID NO:2.The amino acid sequence of the GcKSI protein is optimized in the present application, and a GcKSI recombinant protein rGcKSI is obtained through prokaryotic expression.rGcKSI can inhibit the complement activity of a host fish in vitro, and has an obvious inhibitory effect on serine protease.The infection rate and average infection intensity of rohu fish injected with rGcKSI and then subjected to trichodinid infection experiment are significantly lower than those of a control group, proving that rGcKSI has good immunoprotective properties for trichodinid infection, and indicating that the serine protease inhibitor GcKSI gene and the GcKSI protein encoded by the GcKSI gene can be used as a new target for drug research and development.

This invention provides a method and composition for preparing a composition derived from Carica papaya. [Solution] A method is provided for preparing a composition derived from the fruit of the Carica papaya plant, wherein the composition has a pH of about 7.5 to 9.5, and the method comprises the steps of treating ripe fruit pulp of the Carica papaya plant with alkali without subjecting it to a heating step, and separating soluble proteases from insoluble plant material after the alkali treatment. A composition is also provided comprising one or more serine proteases of proteolytic activity obtainable by the method.

This invention relates to an expression vector, engineered bacteria, and method for inducing expression of a serine protease. The expression vector contains a nucleic acid sequence encoding a serine protease, and the amino acid sequence of the serine protease includes the sequence shown in SEQ ID NO.1. This invention transforms the expression vector into a host bacterium and utilizes its unique high-efficiency expression system for protein expression. By optimizing culture and induction conditions, high-efficiency expression of the serine protease was successfully induced. This serine protease exhibits highly efficient hydrolytic ability, with an enzyme activity reaching 925 U / mL.

The application discloses application of serine protease AprE and a coding gene thereof in prevention and treatment of rice blast, and belongs to the technical field of biotechnology.The amino acid sequence of the serine protease AprE is shown as SEQ ID NO.13, and the nucleotide sequence of the coding gene is shown as SEQ ID NO.14.It is found by the application that after the serine protease encoded by the aprE gene is used to treat blast fungus hypha cells, abnormal ROS accumulation occurs in the cells, and the hypha cells are caused to be apoptotic, broken and abnormally expanded, so that the pathogenic bacteria are finally killed.The aprE gene can be used to study biochemical nature of inhibition of the blast fungus, and can also be used as a target gene of a high-efficiency biocontrol strain and applied to biological prevention and treatment of rice blast.The recombinant serine protease can also be directly used for prevention and treatment of rice blast and reduction of pathogenicity of pathogenic bacteria.

The present application relates to a serine protease for selectively degrading mucin and use thereof. The serine protease is serine protease EatA, and the protein thereof comprises a passenger domain with serine protease EatA activity. The passenger domain has an amino acid sequence with at least 90% identity with SEQ ID NO. 2, and is preferably an amino acid sequence set forth in SEQ ID NO. 2. The serine protease EatA can selectively degrade mucin in disease-related mucus, and has relatively high and lasting stability.