226 results about "Degradative enzyme" patented technology

The invention discloses application of fucoidin degrading enzyme OUC-MgFucD1 in preparation of fucoidin oligosaccharide, and belongs to the technical field of preparation of the fucoidin oligosaccharide. The amino acid sequence of the fucoidin degrading enzyme OUC-MgFucD1 is as shown in SEQ ID NO. 1, and the fucoidin degrading enzyme OUC-MgFucD1 is as shown The fucose oligosaccharide is fucose, fucodisaccharide and fucotriose, the molecular formula of the fucose is C6H12O8S, the molecular formula of the fucodisaccharide is C12H22O15S2, and the molecular formula of the fucotriose is C18H32O16S. The invention further discloses a preparation method of the fucose oligosaccharide. The fucoidin degrading enzyme OUC-MgFucD1 disclosed by the invention can specifically act on fucoidin, and a specific fucoidin oligosaccharide combination is generated by precisely cutting a main chain glucosidic bond of the fucoidin. The invention provides a key technical support for the development of high-added-value fucoidan oligosaccharide products, and has important significance for promoting the industrial application of the fucoidan oligosaccharide in the fields of functional foods, biological medicines and the like.

The invention discloses a PET hydrolase mutant as well as a preparation method and application thereof, and belongs to the field of enzyme engineering. On the basis of FAST-PETase, in combination with deep learning prediction and enzyme engineering optimization strategies, a plurality of mutants with specific performance advantages are systematically constructed and screened, the method is suitable for application scenes with different temperatures, substrate loads and degradation efficiency requirements, and experimental basis and technical support are provided for constructing a diversified and combinable PET degrading enzyme system. The mutants show diversified advantages in different performance dimensions, for example, the enzyme activity of the K233R mutant is 1.62 times that of FAST-PETase, and the K233R mutant still keeps good thermal stability (1.03 times) after being subjected to heat treatment for 2 hours at the temperature of 50 DEG C; q224K is more remarkably improved in the aspect of thermal stability, and the residual activity after heat treatment is 1.64 times that of FAST-PETase.

The invention provides recombinant escherichia coli for producing chondroitin sulfate A and application of the recombinant escherichia coli, and relates to the technical field of genetic engineering. According to the recombinant escherichia coli disclosed by the invention, chondroitin synthase, chondroitin 4-O-sulfotransferase, N-acetyl glucosamine epimerase, UDP-glucose dehydrogenase and chondroitin sulfate degrading enzyme are overexpressed; wherein the amino acid sequence of the chondroitin sulfate degrading enzyme is as shown in SEQ ID NO. 5. The recombinant escherichia coli is inoculated into a culture medium for fermentation culture, the average molecular weight of the obtained chondroitin sulfate A is 800Da, and the yield is about 12.5 g / L. Therefore, low-molecular-weight chondroitin sulfate A can be obtained and the yield of chondroitin sulfate A can be increased by fermenting the recombinant escherichia coli disclosed by the invention.

The invention belongs to the technical field of protein engineering modification, and particularly relates to a method for improving thermal stability of fumonisins degrading enzyme by forming disulfide bonds. The thermal stability of the fumonisins degrading enzyme FumDPS mutants T194V, T194V-P40C / Y173C, T194V-N43C / D83C and T194V-F71C / S117C related to the invention is obviously improved compared with that of the wild type fumonisins degrading enzyme, and the thermal stability of the fumonisins degrading enzyme FumDPS mutants is obviously improved. The fumonisins enzyme is mainly applied to the industries of livestock feed processing, food production and the like so as to reduce the harm of fumonisins to the health of animals and human beings. The obtained fumonisins degrading enzyme mutant with improved thermal stability is convenient to transport and store, so that the investment of industrial cost can be reduced.

The invention belongs to the technical field of bioengineering, and particularly relates to a zearalenone toxin degrading enzyme variant and application thereof. The amino acid sequence of the zearalenone toxin degrading enzyme is as shown in SEQ ID NO.2, or the zearalenone toxin degrading enzyme with the amino acid sequence as shown in SEQ ID NO.2 is obtained through amino acid mutation. The zearalenone toxin degrading enzyme mutant is obtained through mutation screening, and compared with a wild type, the zearalenone toxin degrading enzyme mutant has the advantages that the zearalenone degrading capability is obviously improved; besides, the zearalenone toxin degrading enzyme is expressed by using alfalfa, the zearalenone toxin degrading enzyme with biological activity is easy to obtain, and the zearalenone toxin degrading enzyme has certain application potential in prevention and treatment of animal poisoning caused by zearalenone toxin pollution in agriculture and animal husbandry production.

The invention belongs to the technical field of microbial resource development and straw biological decomposition. The invention discloses cold-resistant pseudoarthrobacter psychrotolans CKON-4, and the preservation number of the cold-resistant pseudoarthrobacter psychrotolans CKON-4 is CGMCC (China General Microbiological Culture Collection Center) No.29378. The cold-resistant pseudoarthrobacter psychrotolans CKON-4 has the advantages that the preservation number The strain CKON-4 is preserved in the China General Microbiological Culture Collection Center (CGMCC) on December 25, 2023, the China General Microbiological Culture Collection Center is called CGMCC for short, the address of the China General Microbiological Culture Collection Center is No.3, Yard 1, Beichen West Road, Chaoyang District, Beijing, and the preservation number of the strain is CGMCC No.29378. The strain disclosed by the invention has very high lignocellulose degradation activity, and the decomposition rate of straws can be remarkably improved; the strain is separated from rice field soil, can grow in the pH value range of 5-9 and the temperature range of 4-37 DEG C, can tolerate the salt concentration of 10%, and is a bacterium with wide pH application range, salt resistance and cold resistance. The strain can play an important role in lignocellulose degrading enzyme production, straw biological decomposition and compost fermentation.

The invention belongs to the technical field of protein engineering modification, and particularly relates to a fumonisins degrading enzyme mutant with improved specific activity and thermal stability and application. According to the mutants of the fumonisins degrading enzyme FumDSB, which are provided by the invention, the relative activity and the thermal stability of the mutants A373R, A373R / S248P, A373R / Q259P, A373R / T282D, A373R / G321A, A373R / D330P and A373R / A378K are obviously improved compared with those of a wild type fumonisins degrading enzyme. The enzyme is mainly applied to the industries of agricultural products, animal feed, food and the like so as to reduce the harm of fumonisins to the health of animals and human beings. The obtained fumonisins mutant with improved activity and thermal stability is beneficial to reducing the cost of the enzyme in industrial application.

The invention relates to a pesticide residue detection test strip as well as a preparation method and application thereof, in particular to a rapid detection technology based on an enzyme inhibition method and a chitosan non-woven fabric carrier. The test strip can specifically detect organophosphorus and carbamate pesticides such as trichlorfon, malathion and phoxim through the enzyme activity inhibition principle, the detection limit of the pesticides such as phoxim is as low as 0.1 mg / kg, the developing intensity is in negative correlation with the pesticide concentration, and semi-quantitative judgment can be achieved. The preparation process is simple, the chitosan non-woven fabric is adopted as a fixed carrier, the material is environment-friendly and degradable, the enzyme activity recovery rate reaches 90%, the stability is excellent (the enzyme activity recovery rate can be preserved for 60 days at the temperature of 4 DEG C in a dark place), sample pretreatment is not needed in detection operation, a result can be obtained at the normal temperature for 15 min, the stability and repeatability are good, and the problems that a traditional instrument is high in detection cost and long in time consumption are solved; the method has a remarkable basic popularization value.

The invention discloses a bisphenol F degradation gene cluster bpf and application thereof. The strain DN12 is separated and can degrade the BPF and grow by taking the BPF as the unique carbon source and energy. On the basis, a BPF degradation gene cluster bpf is obtained from the strain DN12 by adopting whole genome and comparative transcriptome sequencing analysis. Three different degrading enzymes (two-component oxidase BpfAB, monooxygenase BpfC and hydrolase BpfD) are found in the gene cluster and can catalyze gradual degradation of BPF, and a simple aromatic ring compound p-hydroxybenzoic acid is generated.

The invention relates to the field of microorganisms, and discloses a P.megaterium and an application thereof in pig farm manure treatment, the P.megaterium is preserved in China Center for Type Culture Collection on December 13, 2022, the preservation address is Wuhan, China, the classification name of the P.megaterium is Pristia megaterium 3144, and the preservation number is CCTCC NO: M20221962. The content of pollutants such as total nitrogen, chemical oxygen demand and the like in pig farm feces is reduced by secreting various degrading enzymes such as protease, lipase and the like through the provided Priestia megaterium 3144 strain, and meanwhile, fecal coliforms and roundworm eggs are killed by the strain through metabolism heat production and antibacterial substance secretion.

The invention discloses a dsPETase01 plastic degrading enzyme mutant and application thereof, and relates to the technical field of bioengineering, the amino acid sequence of a wild type plastic degrading enzyme (dsPETase01) is designed and modified, 8 dsPETase01 single mutation sites or 19 combined mutation sites are provided, the thermal stability of the obtained dsPETase01 mutant is improved by about 4-21 DEG C compared with that of the wild type dsPETase01, and the dsPETase01 mutant can be used for preparing a plastic degrading enzyme. And the activity is improved by nearly 1.2-3 times. The invention also provides four preferable mutant proteins which have higher yield, activity and thermal stability compared with wild dsPETase01, have wider application conditions, are more suitable for degrading PET (Polyethylene Terephthalate) plastics, and are beneficial to large-scale production and industrial application.

The invention provides a stem cell exosome for overexpressing A beta degrading enzyme as well as a preparation method and application of the stem cell exosome. Specifically, the invention provides an application of the stem cell exosome overexpressing A beta degrading enzyme in preparation of drugs, and the drugs are used for at least one of the following: prevention, improvement or treatment of cognitive impairment related diseases; neuronal cell damage is improved; wherein the stem cells for overexpressing the A beta degrading enzyme are prepared through lentivirus transfection. According to the stem cell exosome overexpressing the A beta degrading enzyme, the content of the A beta degrading enzyme is obviously higher than that of the exosome prepared by a traditional method. Therefore, when the compound is prepared into a medicine for treating or preventing cognitive impairment related diseases, the medicine can be efficiently conveyed to the brain, and the concentration of the medicine in the brain is remarkably improved, so that the curative effect is enhanced, the dosage of the medicine can be reduced, the side effect is reduced, and the prognosis of brain diseases is effectively improved.

The invention belongs to the technical field of protein engineering modification, and particularly relates to a method for improving thermal stability of fumonisins degrading enzyme by forming disulfide bonds. The thermal stability of the fumonisins degrading enzyme FumD mutant provided by the invention is obviously improved compared with that of wild type fumonisins degrading enzyme. The fumonisins enzyme is mainly applied to the industries of livestock feed processing, food production and the like so as to reduce the harm of fumonisins to the health of animals and human beings. The obtained fumonisins degrading enzyme mutant with improved thermal stability is beneficial to keeping the activity of the enzyme at a higher temperature, adapts to a higher-temperature production environment, reduces the use amount and replacement frequency of the enzyme, and is convenient to transport and store due to the improvement of the stability, so that the investment of industrial cost can be reduced.

The invention discloses a biodegradable light-package high-barrier packaging film and a preparation process, and relates to the technical field of packaging films, the biodegradable light-package high-barrier packaging film comprises the following components by weight: 8-15 parts of modified montmorillonite, 30-50 parts of modified nano cellulose, 5-10 parts of polyvinyl alcohol, 1.5-3 parts of a plasticizer, 0.25-0.6 part of curcumin, and 40-60 parts of deionized water. According to the biodegradable light-package high-barrier packaging film and the preparation process, montmorillonite is modified, so that the montmorillonite can interact with anions on a bacterial cell membrane, the integrity of the cell membrane is destroyed, and bacterial contents are leaked, thereby inhibiting growth and reproduction of bacteria and improving the antibacterial property of the packaging film; montmorillonite is a natural mineral material, is environment-friendly, and can change the crystal structure of polyvinyl alcohol, so that the degrading enzyme is easier to contact with a polymer molecular chain, and the degradation speed is accelerated.

The invention discloses an IsPETase mutant with improved thermal stability and activity and application of the IsPETase mutant. According to the invention, a mutant TS-PETase of PET plastic degrading enzyme IsPETase is taken as a parent, and the IsPETase mutant with improved thermal stability and / or PET degrading activity is obtained by performing single-point mutation or combined mutation on amino acid at a specific site of the mutant TS-PETase. The obtained IsPETase mutant can be used for effectively degrading PET (Polyethylene Terephthalate) plastics under a Tg condition, and can also be prepared into a corresponding preparation for degrading the PET plastics accumulated in the environment and improving the environment polluted by the PET plastics. The obtained IsPETase mutant can also be used for degrading PET-containing plastic products and assisting in harmless treatment of plastics. The IsPETase mutant with improved thermal stability and activity, provided by the invention, has a promoting effect on the development of industrial biodegradation of PET (Polyethylene Terephthalate) plastics.

The invention relates to salt-tolerant paracoccus and application thereof in wastewater treatment, and belongs to the technical field of environmental microorganisms. The Paracoccus sp. S16 is preserved in the China General Microbiological Culture Collection Center on May 28, 2025, the preservation address is No.3, No.1 yard, Beichen West Road, Chaoyang District, Beijing, and the preservation number is CGMCC No.34704. The strain has unique salt tolerance and various degrading enzyme systems, and can be applied to the field of biological engineering, biological engineering and the like. The catalyst can effectively degrade petroleum hydrocarbons, polymers and other organic pollutants with high toxicity in drilling fluid wastewater, has wide environmental adaptability, and has great application potential.

The present invention discloses the use of 3,4-dihydropsoralen in the preparation of a drug for preventing or treating rheumatoid arthritis. The present invention simulates RA by constructing TNF-a-induced SW982 cells. The results show that 3,4-dihydropsoralen (DP) can downregulate the mRNA expression of inflammatory factors, chemokines, and matrix degrading enzymes through the IL-17 signaling pathway, and affect the IL-17 signaling pathway and the NF-κB signaling pathway to jointly exert an anti-inflammatory effect, thereby effectively improving rheumatoid arthritis. This provides a theoretical basis for the application of 3,4-dihydropsoralen in the clinical treatment of rheumatoid arthritis and opens up new therapeutic drugs and approaches.

The invention discloses recombinant bacillus subtilis capable of efficiently expressing a plastic degrading enzyme LCCICCG as well as a construction method and application of the recombinant bacillus subtilis. The recombinant bacillus subtilis is used for overexpressing the plastic degrading enzyme LCCICCG and signal peptide. By constructing plasmids of different signal peptides and promoters, the biomass of the recombinant bacillus subtilis and the protein expression quantity of the LCCICCG in the fermentation culture process are improved, and the industrial production cost of the LCCICCG is reduced.

The invention provides a beautifying composition and application thereof in whitening, anti-inflammatory and anti-aging products, and belongs to the technical field of cosmetics. The beautifying composition is prepared from collagen peptide, sodium hyaluronate and ergothioneine, wherein the mass concentration ratio of the collagen peptide to the sodium hyaluronate to the ergothioneine is (75 to 85) to (3.5 to 10) to (0.4 to 3.5); the beautifying composition shows remarkable advantages in the aspects of collagen regeneration and skin improvement, the collagen content can be remarkably increased, and multi-effect collagen regeneration promotion is achieved by inhibiting collagen degrading enzyme MMP-1 and up-regulating TGF-beta1; the content of AQP3 and HA can be increased, and water locking and moisturizing of the skin are enhanced; by activating an Nrf2 pathway, the SOD2 level is improved, IL-6 and IL-1alpha are inhibited, and the antioxidant, anti-inflammatory and whitening effects are achieved; the thickness of an epidermal layer and the density of dermal fibroblasts can be remarkably improved, wrinkle resistance and repairing are effectively achieved, and the skin structure is improved.

The invention relates to the field of microorganisms, in particular to bacillus subtilis, a fungicide and application of the fungicide. The invention discloses a bacillus subtilis strain, which is classified and named as bacillus subtilis, has a strain number of GXGD-YZ-2483, is preserved in Guangdong Microbial Culture Collection Center on March 13, 2025, and has a preservation number of GDMCC No: 66014. The bacillus subtilis can tolerate the high temperature of 70-90 DEG C, has excellent self-heat production performance, and can produce lignin degrading enzymes (laccase, manganese peroxidase and / or lignin peroxidase) and inhibit the growth of pathogenic bacteria (escherichia coli, salmonella, clostridium perfringens and / or aspergillus flavus). When the bacillus subtilis or the microbial inoculum prepared from the bacillus subtilis is used for biologically composting organic wastes, a lignin barrier can be efficiently cracked by secreting a lignin degrading enzyme system, lignin degradation, nitrogen retention and pathogenic bacteria inactivation can be synchronously realized by virtue of high temperature resistance, self-heat production characteristics and enzyme activity stability, the composting period is shortened, and the yield of the organic wastes is improved. The humification quality is obviously improved.

The invention discloses a PET (Polyethylene Terephthalate) degrading enzyme and an application thereof in the aspect of degrading PET plastics. The hydrolase LfPETase capable of degrading the PET plastic is screened from metagenomes of landfill soil samples of a garbage dump, the amino acid sequence of the hydrolase LfPETase is shown as SEQ ID NO.2, the similarity between the amino acid sequence of the hydrolase LfPETase and the highest sequence of 10 kinds of currently known common PET degrading enzymes is only 39.42%, and the novelty of a sequence skeleton of the hydrolase LfPETase is indicated. According to the invention, a pichia pastoris engineering strain capable of efficiently expressing and coding the PET degrading enzyme gene is constructed, and the specific activity of the recombinant degrading enzyme LfPETase obtained by purification is up to 250 U / mg when p-nitrophenyl octyl ester (pNPO) is taken as a substrate; after consumption, PCW-PET bottle flake plastic is taken as a substrate, degradation is carried out at 70 DEG C for 12 h, the depolymerization rate can reach 92%, and a new enzyme resource is provided for plastic enzymatic depolymerization recycling.

The invention discloses an efficient PET (Polyethylene Terephthalate) degrading enzyme mutant and an application thereof in degrading a PET material for milk, and belongs to the technical field of biology. The method for high-throughput screening of the enzyme for degrading the PET material for milk is convenient to operate, high in throughput, low in cost and short in period. The PET degrading enzyme mutant screened by the method has higher degradation efficiency, the degradation rate of the PET degrading enzyme mutant to a PET material for milk within 6 hours can exceed 95%, and the PET degrading enzyme mutant has a wide application prospect.

The invention discloses polyethylene glycol terephthalate hydrolase PmPETase and application thereof.The hydrolase PmPETase is protein with the amino acid sequence shown in SEQ ID NO.1. An expression system suitable for the PmPETase is constructed, recombinase protein with catalytic activity is obtained, and the polyethylene glycol terephthalate hydrolase PmPETase can be used for preparing the polyethylene glycol terephthalate hydrolase PmPETase. The substrate specificity, the catalytic property and the potential plastic degradation capacity of the PET degrading enzyme are comprehensively analyzed, and a new theoretical basis and application reference are provided for development and utilization of the PET degrading enzyme and a high polymer material green treatment technology.

The invention discloses a tenuilia microspora NB1-3, a leavening agent and application of the tenuilia microspora NB1-3 in preparation of caragana microspora and moringa oleifera fermented protein feed. The strain is classified and named as nicotiana microspora, and is preserved in the China Center for Type Culture Collection (CCTCC), and the preservation number is CCTCC NO: M 20251872. The core of the method is that crude fibers and antinutritional factors (tannin and phytic acid) in moringa oleifera and caragana microspora are efficiently degraded by utilizing a strong lignocellulose degrading enzyme system of the tenuilia microspora NB1-3, and meanwhile, the crude protein content of the feed is increased. The prepared fermented protein feed is high in crude protein content and low in crude fiber content and meets the protein feed standard, efficient and high-value utilization of woody plant resources such as caragana microphylla and moringa oleifera is achieved, and a new high-quality and economical protein feed source is provided for animal husbandry.

This invention relates to the field of enzyme engineering technology, and in particular to a highly efficient lactone hydrolase mutant for degrading zearalenone and its applications. This lactone hydrolase mutant uses the lactone hydrolase gene from Monosporascus sp. GIB2 as a template, and performs a site-directed mutation at amino acid position 134 to obtain L134A, L134V, L134I, and L134M mutants. Under optimal conditions of pH 9.0 and 60℃, these single-point mutants can efficiently degrade zearalenone (ZEN) within 3 minutes. The enzyme activity for degrading zearalenone is significantly improved compared to the original enzyme, with degradation activities increasing by 1.22 (L134A), 1.25 (L134V), 1.17 (L134I), and 1.14 (L134M), respectively, demonstrating significant applications and economic value in the feed industry.

The present invention relates to the technical field of genetic engineering. Provided is a method for constructing an efficient zearalenone-degrading enzyme in the gastric environment of a pig. In the zearalenone-degrading enzyme as shown in SEQ ID NO: 1 that is taken as the parent, the amino acid at position 92, the amino acid at position 114, the amino acid at position 117, the amino acid at position 140, the amino acid at position 153, the amino acid at position 157 and the amino acid at position 220 are respectively mutated into lysine, leucine, tryptophan, arginine, methionine, valine and tryptophan to obtain the mutant. The obtained zearalenone-degrading enzyme mutant has high enzymatic activity and thermal stability, and is better adapted to the internal environment of pigs.

The present invention discloses an application of an IMPDH2 inhibitor in preventing or treating inflammation. The limonoid compound provided by the present invention can bind to and degrade human inosine-5'-monophosphate dehydrogenase 2 (IMPDH2), inhibit the synthesis of intracellular guanine, inhibit the activation of the NF-κB signaling pathway, and can be used as an IMPDH2 inhibitor; the IMPDH2 inhibitor also has a good preventive or therapeutic effect on inflammation. Compared with existing IMPDH2 inhibitors, the limonoid compound provided by the present invention can degrade the IMPDH2 enzyme, has better inhibitory activity, and has stronger activity in inhibiting inflammatory factors.

The present application relates to the field of genetic engineering and PET material degradation, and particularly relates to a PET degrading enzyme mutant and its application in PET material degradation. The present application improves the activity and heat resistance of PET degrading enzyme MuPETase derived from Mumia sp., and screens to obtain mutants Mut1-3, Mut5-8 which show good degradation capacity to PET material under acidic conditions, and the amino acid sequences are shown in SEQ ID NO. 3-5, SEQ ID NO. 7-10 respectively. Compared with the original PET degrading enzyme, the heat stability and / or specific activity of the obtained mutant are significantly improved, and the degradation effect on PET material is greatly improved. The obtained mutant has important application value in the biological degradation treatment of single and mixed PET material waste.

The invention relates to the technical field of microorganisms, in particular to a saline-alkaline-tolerant bacillus velezensis JT6, a cellulose degrading enzyme secreted by the same and application of the saline-alkaline-tolerant bacillus velezensis JT6. The bacillus velezensis JT6 disclosed by the invention is preserved in the China General Microbiological Culture Collection Center, the address is Institute of Microbiology, Chinese Academy of Sciences, 3 #, No.1 yard, West Beichen Road, Chaoyang District, Beijing, the preservation date is December 5, 2025, and the preservation number is CGMCC No.36918. The bacillus velezensis JT6 disclosed by the invention can be used for preparing the bacillus velezensis JT6. The strain has cellulose degradation activity, the degradation rate of corn straw is 48.8%, and the degradation rate of rice straw is 24.92%. The strain provided by the invention is used for rapid decomposition of straw returning, is safe to human and livestock, has no pollution to the environment, and has good development and application prospects.

The invention discloses a modified bio-enzyme preparation and application thereof in synergistic microbial pretreatment production of sticky paper pulp, and belongs to the technical field of paper pulp manufacturing. The modified biological enzyme preparation is prepared from cellulase, hemicellulase, lignin degrading enzyme, hydrophobic amino acid and a surfactant. The modified bio-enzyme preparation cooperates with microorganisms to pre-treat wood pulp fibers, and pulping treatment of a double-screw pulping machine is combined, so that the pulping efficiency can be greatly improved, the pulping energy consumption can be reduced, the prepared sticky paper pulp is high in strength and good in performance, and the tensile index and burst index of paper are improved. The method has the characteristics of energy conservation, environmental protection and high efficiency, responds to a new concept of high-valued sustainable development of biomass, and has high popularization value.