365 results about "Specific enzyme" patented technology

The invention discloses a Candida antarctica lipase B mutant with high transesterification activity and application thereof. The nucleotide sequence of the Candida antarctica lipase B mutant is shown as SEQ ID NO.1, and the amino acid sequence of the expression protein of the Candida antarctica lipase B mutant is shown as SEQ ID NO.2. The invention further discloses a preparation method of the Candida antarctica lipase B mutant. Compared with an original enzyme, the mutant has higher fat hydrolysis activity and transesterification activity, the specific enzyme activity of the fat hydrolysis activity reaches 480.39 U / mg, the specific enzyme activity of the transesterification activity reaches 40.67 U / mg, the biodiesel conversion rate at the temperature of 30 DEG C can reach 92%, low-temperature high catalytic activity is shown, and the mutant can be used for enzymatic preparation of biodiesel and has potential industrial application value.

The invention discloses an arginine decarboxylase diaA enzyme mutant and application thereof in preparation of butanediamine, and belongs to the field of bioengineering. According to the invention, rational charge overturning transformation is simultaneously carried out on a pentamer meridian oligomeric interface and a dimer latitudinal oligomeric interface, so that stable assembly and efficient catalysis of the decamer under the condition of neutral to alkaline pH (7.0-9.0) are realized. Wherein positive charges are introduced into a meridian interface to weaken electrostatic repulsion, and negative charges are introduced into a latitudinal interface to enhance dimer compactness and substrate transfer efficiency. The specific enzyme activity of the representative double mutant AdiAD110K / H736E at pH 8.0 is about 35 times that of a wild type, and the representative double mutant AdiAD110K / H736E keeps a complete decamer state in a pH range of 7.0-9.0. The yield of butanediamine is up to 145.9 g / L under the whole-cell catalysis of the mutant.

The invention belongs to the field of bioengineering, and particularly discloses a glutamate oxidase mutant with improved enzymatic activity. According to the invention, site-specific mutagenesis and saturation mutation are carried out on glutamate oxidase coding genes derived from streptomyces mobaraensis, wherein mutations are C536R, P532R, Q378D, V548E and G236D. After the mutant obtained by the invention is induced and purified, the specific enzyme activity of the optimal glutamate oxidase mutant is 1.69 U / mg and is improved by about 30% compared with that of wild bacteria, which shows that the 378-site amino acid residue has great influence on the catalytic action and stability of the enzyme. In addition, the invention also discloses a construction method of the glutamate oxidase mutant with improved enzymatic activity and application of the glutamate oxidase mutant in production of amino acid derivatives such as alpha-ketoglutaric acid. Therefore, the beneficial mutant provided by the invention can lay a good foundation for industrial fermentation production of alpha-ketoglutaric acid and other products.

The invention discloses a rational copolymerization strategy for improving the stability of an oligomeric structure of acid-induced high-order oligomeric decarboxylase AdiA in a neutral to alkaline environment and application of the rational copolymerization strategy, and belongs to the field of bioengineering. According to the strategy, rational charge overturning transformation is carried out on a pentamer radial oligomeric interface and a dimer weft-wise oligomeric interface at the same time, and stable assembly and efficient catalysis of a decamer under the condition that the pH value is from 7.0 to 9.0 from neutral to alkaline are achieved. Wherein positive charges are introduced into a meridian interface to weaken electrostatic repulsion, and negative charges are introduced into a latitudinal interface to enhance dimer compactness and substrate transfer efficiency. The specific enzyme activity of the representative double mutant AdiAD471K / E467K / H736E is 45.5 times that of a wild type when the pH value is 8.0, and the representative double mutant AdiAD471K / E467K / H736E keeps a complete decamer state when the pH value is 7.0-9.0. The yield of butanediamine is up to 156.5 g / L by using the mutant to catalyze whole cells.

Provided are S-adenosylmethionine synthetase mutants and the use thereof, belonging to the technical field of biological enzyme engineering. Site-directed combinatorial mutations are performed on positions 189, 200, 234, 266 and 371 of S-adenosylmethionine synthetase MAT to obtain a series of mutants with improved enzyme activity, wherein the specific enzyme activity of I189V / V266H and V266H / N371R is increased by more than 10 times relative to the parent. The yields of S-adenosylmethionine synthesized by whole cells of recombinant bacteria expressing mutants I189V / V266H / N371R, V266H / Q234N / N371R and I189V / V266H / Q234N / N371R all reach 1550 mg / L or more. The provided enzyme mutants have broad application prospects in the production of S-adenosylmethionine and the construction of genetically engineered microorganisms for S-adenosylmethionine.

In a small molecule drug discovery method, a transition state for a specific enzyme is modelled using quantum mechanics and molecular dynamics based simulation of the enzyme and substrate reaction; data defining the transition state (a ‘quantum pharmacophore’) is fed to a machine learning engine configured to generate transition state analogues, such as enzyme inhibitors.

An intelligent deformable microneedle includes a supporting seat; a counter electrode provided above the supporting seat; an elastic object with a compressed state and a natural state, where a working electrode is provided on an outer surface of the elastic object, and a specific enzyme that can react with an analyte to be detected is provided on the working electrode; a soluble needle-shaped body fixed on the supporting seat, where the soluble needle-shaped body completely wraps the counter electrode and the elastic object from the outside, and the soluble needle-shaped body has an inner cavity structure that enables the elastic object to be in the compressed state. The microneedle is internally provided with the elastic object, after penetrating into skin, the soluble needle-shaped body is dissolved, the elastic object inside is exposed, length becomes longer, and the working electrode of an electrochemical sensor is attached to the elastic object.

The present invention provides a manganese metal-organic framework material with oxidase properties, a preparation method, and an application thereof. The material is prepared by the following method: using 1,3,5-trimethic acid as an organic ligand, manganese acetate tetrahydrate as a manganese source, and a water-ethanol solution as a solvent, to obtain a manganese metal organic framework (MOF) precursor via a solvothermal synthesis technique; the manganese MOF precursor is post-synthetically modified using an oxidant, wherein the oxidant is a mixed solution of an aqueous alkali metal hydroxide solution and H2O2, and the ratio of the manganese MOF precursor to the alkali metal hydroxide is (400-600) mg:(0.5-2) mmol. By using specific types and amounts of manganese MOF precursors and oxidants, the resulting metal-organic framework nanomaterial has specific enzyme-like properties, can exert the function of uricase, and has optimal and high uricase activity under neutral pH conditions.

The invention discloses a mutant with improved catalytic activity of S-adenosylmethionine synthetase and application of the mutant, and belongs to the technical field of biological enzyme engineering. According to the present invention, the site 189, the site 234, the site 266 and the site 371 of the S-adenosylmethionine synthetase MAT are subjected to site-specific combinatorial mutation to obtain a series of mutants with improved enzyme activity, the I189V / V266H improvement is the most obvious, and the specific enzyme activity is 3.5833 + / -0.1373 U.mg <-1 >, which is improved by 1353.08% compared to the parent WT; and for a whole-cell catalysis system, the yield of S-ademetionine synthesized by the mutant I189V / V266H / Q234N / N371R reaches 1751.01 mg / L, and the increase is most obvious. The enzyme mutant provided by the invention has a wide application prospect in the production of S-adenosylmethionine and the construction of genetic engineering microorganisms of S-adenosylmethionine.

The invention relates to the field of genetic engineering and immobilized enzymes, in particular to a sucrose isomerase recombinant as well as a construction method and application thereof. Wild type sucrose isomerase (Sase) from dispersed pantoea is subjected to molecular modification, fusion expression is performed after screening of affinity peptide ligands, the specific enzyme activity of the obtained sucrose isomerase recombinant is 88% higher than that of sucrose isomerase, the enzyme activity level of the sucrose isomerase recombinant is remarkably improved, and the specific catalysis efficiency of the sucrose isomerase recombinant on a sucrose substrate is improved; and reference is provided for improving molecular modification of other enzymes. The sucrose isomerase recombinant has good thermal stability, and finally, research on embedding system optimization is performed on one-step purification and immobilization of SIase, so that the affinity directional immobilized enzyme microspheres which have high hardness and strength and can effectively reduce leakage or loss of enzyme molecules are prepared. The reusability of the sucrose isomerase recombinant is obviously improved.

The invention discloses a laccase mutant and application of the laccase mutant in preparation of polyflavone by oxidative conversion of daidzein. According to the invention, laccase Lcc5 of coprinus cinerea is used as a starting enzyme, and through molecular docking, a position structure is analyzed, and mutation is designed. Synthesizing a mutant gene, and constructing a recombinant expression engineering bacterium of the mutant gene. After engineering bacteria containing mutant genes are subjected to induced expression, the Lcc5 mutant Lcc5-T485E is obtained through separation and purification, the specific enzyme activity and ethanol tolerance of the mutant are improved, and the conversion rate of daidzein is increased to about 1.26 times under the same enzyme activity; the antioxidant activity, the enzyme inhibition activity and the antibacterial activity of the obtained conversion product are also remarkably improved. The mutant enzyme has potential application value in oxidative conversion of daidzein and improvement of biological value of daidzein.

The application discloses a galactosyltransferase mutant and application thereof in preparation of flavonoid compounds, and belongs to the technical field of enzymology. The application provides a UDP-galactosyltransferase mutant, which is obtained by site-directed mutation of one amino acid in the amino acid sequence of wild-type galactosyltransferase VcUFGT into alanine (A). The effects of a series of mutants H82A, V139A, G141A, P186A, N245A, V282A and S307A are verified in the examples, the mutants can perform enzyme catalysis reaction with quercetin and UDP-galactoside as substrates, and generate flavonoid compound hyperoside, and the specific enzyme activity of the mutants is more than 1.5 times that of the wild type, thereby providing an effective application basis for biosynthesis of flavonoid compounds.

The invention belongs to the field of gene engineering, and discloses a sucrose isomerase mutant, a high-yield isomaltulose engineering bacterium and a construction method and application thereof. According to the sucrose isomerase mutant obtained through rational design of an enzyme molecular structure, the enzyme activity and the isomaltulose conversion rate of the sucrose isomerase mutant are remarkably improved, compared with a wild enzyme, the specific enzyme activity of the sucrose isomerase mutant is improved by 2.29 times, the isomaltulose conversion rate is improved to 98.9% from 91.1%, the impurity content is lower, and therefore the sucrose isomerase mutant is more suitable for synthesis of isomaltulose. A recombinant engineering bacterium of the high-yield isomaltulose engineering bacterium is further constructed; the recombinant engineering bacterium capable of efficiently expressing the sucrose isomerase is constructed by utilizing ubiquitin-like protein modified molecular genes to be fused with sucrose isomerase mutant coding genes, the enzyme activity of the prepared sucrose isomerase can reach 40.5 U / mg wet cells, and the recombinant engineering bacterium has a great application prospect in industrial production.

The invention discloses a glutathione bifunctional synthetase mutant with improved catalytic activity and application, and belongs to the field of gene engineering and fermentation engineering. A series of mutants with improved enzyme activity are obtained by carrying out site-specific combinatorial mutation on a site 61, a site 136, a site 485, a site 498 and a site 722 of the glutathione bifunctional synthetase GshFst, the specific enzyme activity reaches 13.58 U.mg <-1 >-27.34 U.mg <-1 >, the half-life period at 37 DEG C reaches 195-320 min, and the enzyme activity and the thermal stability are remarkably improved compared with those of a wild type. The enzyme mutant provided by the invention has a wide application prospect in the production of glutathione and the construction of genetically engineered microorganisms for producing glutathione.

The invention discloses a T7 RNA polymerase mutant capable of being used for preparing mRNA vaccines and improving thermal stability and transcription performance and a preparation method of the T7 RNA polymerase mutant, relates to the technical field of biology, and particularly discloses a T7 RNA polymerase mutant containing mutation sites K8G, H27K, A70N, K180D and S192P / S192G relative to wild type T7 RNA polymerase. The amino acid sequence of the wild type T7 RNA polymerase is as shown in SEQ ID NO: 1. Compared with wild type T7 RNA polymerase, the T7 RNA polymerase has higher specific enzyme activity and heat stability, the heat resistance of one mutant is improved, a large number of transcription products can still be obtained at 45 DEG C, and transcription by-products of the other mutant are reduced. The mutant T7 RNA polymerase disclosed by the invention has a good application prospect in the fields of RNA vaccines and medicines, in-vitro transcription, gene editing and the like.

The invention discloses a detection method and application of whole genome 5-hydroxymethylcytosine, and relates to the technical field of biochemical detection. Comprising the following steps: 1, closing a 3 '-OH end of DNA to be detected; 2, preparation of glycosylated 5hmC DNA (Deoxyribose Nucleic Acid); 3, carrying out TdT mediated DNA (Deoxyribonucleic Acid) amplification; and 4, fluorescence measurement. According to the invention, a homogeneous and non-template dependent type signal amplification method for detecting the 5-hydroxymethylcytosine in the whole genome is constructed. The method is based on a specific enzyme catalytic reaction and a multiple signal amplification strategy, and has the characteristics of high sensitivity, good specificity, no need of a separation step, no sequence dependence in amplification and capability of detecting 5hmC at any position in a whole genome. In addition, accurate and sensitive detection of actual clinical samples can be realized.

The invention provides a high-activity collagen peptide and a preparation method thereof, and aims at improving the product yield of the collagen peptide by finely controlling enzymolysis conditions and adopting a specific enzyme activator and effectively controlling the average molecular weight of the collagen peptide so as to enhance the bioavailability and functionality. The preparation method comprises the following steps: S1, crushing fish skin at low temperature, adding the crushed fish skin into an enzyme reaction kettle, adjusting the pH value, and adding composite alkaline protease and an enzyme activator to carry out enzymolysis twice at different temperatures; s2, centrifuging the enzymatic hydrolysate at a high speed, adding activated carbon and citric acid, and filtering to obtain a collagen peptide solution; and S3, carrying out freeze drying on the concentrated solution subjected to ultrafiltration and nanofiltration in the step S3 to obtain the high-activity collagen peptide. The collagen peptide prepared by the method has high DPPH free radical scavenging rate, the molecular weight is lower than 1000Da, the distribution is concentrated, and the product yield and functionality are remarkably improved.

The invention discloses a method for preparing butanediamine and spermidine by an enzyme method, and belongs to the field of bioengineering. The novel arginine decarboxylase mutant is successfully provided, the mutant shows excellent catalytic performance under the alkaline condition, and the specific enzyme activity of the mutant reaches 24.9 U / g and is improved by 8.3 times compared with that of wild type enzyme. The invention develops a two-step synthesis process based on the constructed arginine decarboxylase mutant, and the two-step synthesis process is used for efficiently preparing spermidine. Experimental results show that the process successfully realizes the remarkable increase of the yield of spermidine, and the final yield reaches 200.4 mg / L.

The invention discloses a mycobacterium tuberculosis tyrosine phenol lyase mutant and application thereof, and belongs to the field of molecular biology and the technical field of biological catalysis. The mutant is obtained by mutating 384 isoleucine of tyrosine phenol lyase from mycobacterium tuberculosis into valine, and is marked as a mutant I384V. The I384V and wild type tyrosine phenol lyase have similar optimum temperature and optimum pH, but the I384V shows higher specific enzyme activity and catalytic efficiency than the wild type tyrosine phenol lyase. Compared with a wild type, the tyrosine phenol lyase mutant I384V has the advantages that the synthesis efficiency of the tyrosine phenol lyase mutant I384V on the synthesis of levodopa is improved by 38.4%, and the tyrosine phenol lyase mutant I384V has wide prospects in large-scale industrial application.

The invention relates to the technical field of plant-based beverages, in particular to a chickpea beverage based on enzymolysis regulation and a preparation method thereof. The preparation method of the chickpea beverage comprises the step of performing enzymolysis on chickpeas by adopting alpha-amylase, acidic lipase and flavourzyme. According to the method, the sugar spectrum of the chickpea beverage is accurately regulated and controlled through a specific enzyme combination and enzymolysis process, the sugar composition of the chickpea beverage is improved, the beverage contains low sugar, medium sugar and oligosaccharide at the same time, the proportion of the low sugar, the medium sugar and the oligosaccharide is moderate, the flavor and taste are improved while the sweetness is well controlled, and the chickpea beverage is made to better conform to the taste preference of consumers and has good market prospects. Meanwhile, the nutritional value and the stability of the product are improved, and the market requirements can be better met.

[Problem] To provide a novel compound promising as a prodrug-type anticancer agent that exhibits a sufficient anticancer effect and is capable of reducing adverse effects. [Solution] A compound represented by general formula (I) or a pharmaceutically acceptable salt of the compound. Formula (I): Y-T-(X1)n

The invention discloses a fluorescent probe device with high-sensitivity detection in the field of biological fluorescence detection.The fluorescent probe device comprises a micro-fluidic chip, a closed micro-channel allowing a sample to flow is arranged in the micro-fluidic chip, and the micro-channel comprises a reaction bin, a sample bin and an enzyme liquid bin; the sample bin and the enzyme liquid bin are symmetrically distributed on the two sides of the reaction bin, delay channels of zigzag structures are communicated between the sample bin and the reaction bin and between the enzyme liquid bin and the reaction bin, the sample bin and the enzyme liquid bin are provided with a first filling port and a second filling port respectively, the reaction bin is provided with vent holes communicated with the outside, and a plurality of aptamer fluorescent probes are fixed to the bottom wall of the reaction bin. A nucleic acid aptamer fluorescent probe is fixed in the micro-fluidic chip, a CRISPR-Cas12a enzyme digestion system is added, a plurality of signal fragments are released in the process that a single aptamer is combined with antibiotics, signal cascade amplification of CRISPR-Cas12a non-specific enzyme digestion activation is achieved, and the micro-fluidic chip has the function of detecting existence of drug-resistant genes. And the possibility of occurrence of false negative detection results is reduced as much as possible.

The invention provides a manganese metal organic framework material with oxidase characteristics as well as a preparation method and application thereof, and the material is prepared by the following method: taking 1, 3, 5-trimesic acid as an organic ligand, manganese acetate tetrahydrate as a manganese source and a water-ethanol solution as a solvent, and obtaining a manganese MOFs precursor through a solvothermal method synthesis technology; the manganese MOFs precursor is subjected to post-synthesis modification with an oxidizing agent, the oxidizing agent is a mixed solution of an alkali metal hydroxide aqueous solution and H2O2, and the dosage ratio of the manganese MOFs precursor to the alkali metal hydroxide is (400-600) mg: (0.5-2) mmol. The manganese MOFs precursor and the oxidizing agent with specific types and using amounts are adopted, so that the obtained metal organic framework nano material has specific enzyme-like characteristics, can play a role of urate oxidase, has optimal urate oxidase activity under a neutral pH condition, and is relatively high in activity.

The invention discloses a Taq DNA polymerase mutant with improved thermal stability and inhibition resistance as well as a preparation method and application of the Taq DNA polymerase mutant, and relates to the technical field of biology. According to the Taq DNA polymerase mutant, amino acid mutation is carried out on an amino acid sequence of wild type Taq DNA polymerase, and amino acid mutation sites comprise F73S and P93A; the amino acid sequence of the wild type Taq DNA polymerase is as shown in SEQ ID NO: 1. Compared with wild type Taq DNA polymerase, the Taq DNA polymerase has the advantages that the resistance to inhibitors such as heme, ethanol and EDTA (Ethylene Diamine Tetraacetic Acid) is improved, and meanwhile, the Taq DNA polymerase has higher specific enzyme activity and heat stability.

The invention provides a glutaminase mutant and application of the glutaminase mutant. Wherein the glutaminase mutant comprises (a) a protein which is subjected to amino acid mutation and has a glutaminase activity function on at least one of the following sites of S467, Y334, K400, N521, R337, E402 or D447 of an amino acid sequence as shown in SEQ ID NO: 2, and (b) a protein which is subjected to amino acid mutation on at least one of the following sites of S334, Y334, K400, N521, R337, E402 or D447 of the amino acid sequence as shown in SEQ ID NO: 2; and (b) a protein which has 80% or more homology with the amino acid sequence limited by (a) and has a glutaminase function. The glutaminase mutant with the amino acid sequence disclosed by the invention has relatively high specific enzyme activity during enzyme catalytic reaction, and is low in cost and strong in market competitiveness when being used for commercial food processing.

The present invention relates to enzymatic detergents and cleaning compositions comprising specific enzyme stabilizers and having improved enzyme stability. More specifically, the present invention relates to detergent and cleaning compositions comprising an enzyme and an effective amount of a specific type of enzyme stabilizer, such as an alkanediol having a carbon chain of 5 to 14 carbon atoms, caprylin, 4-hydroxyacetophenone, ethylhexylglycerol, tropolone or a mixture of said enzyme stabilizers, and a surfactant, and to the use of said detergent and cleaning compositions for the preparation of detergent and cleaning products for household, public institution and industrial applications. In addition, the present invention relates to the use of specific enzyme stabilizing substances as defined herein for stabilizing enzymes in detergents and cleaning compositions. Furthermore, the present invention relates to a process for the preparation of a detergent and cleaning composition by adding to the detergent and cleaning composition an effective amount of a specific type of enzyme stabilizer such as an alkanediol having a carbon chain of 5 to 14 carbon atoms, caprylin, 4-hydroxyacetophenone, ethylhexylglycerin, or a mixture thereof. A method of stabilizing an enzyme in the detergent and cleaning composition by a mixture of a cycloheptenolone or the enzyme stabilizer. Finally, the invention relates to an enzyme composition comprising a particular type of enzyme stabilizer.

The invention discloses a microsphere entrapped with probiotics and ginsenoside as well as a preparation method and application of the microsphere, and aims to realize efficient treatment of flora imbalance inflammatory bowel disease (IBD). The microspheres adopt a bi-component synergistic entrapment technology, can stably bear probiotics and ginsenoside, effectively avoid inactivation or degradation of the probiotics and ginsenoside in gastric acid and cholate environments, and ensure directional release and efficient utilization of the probiotics and ginsenoside in intestinal tracts. The microspheres not only provide a protection effect as a delivery carrier, but also construct a'microreactor 'system, and provide a suitable microenvironment for survival of probiotics and conversion of ginsenoside. Probiotics secrete a specific enzyme to promote prototype ginsenoside to be converted into rare ginsenoside with higher activity and stronger solubility while regulating intestinal flora balance and relieving intestinal inflammation, so that the bioavailability and efficacy of the rare ginsenoside are remarkably improved. According to the microsphere system, the technical bottlenecks of the existing treatment means in the aspects of activity maintenance, directional release and conversion utilization are broken through by realizing the synergistic effect of the probiotics and the ginsenoside, and a brand-new strategy and a technical platform are provided for treatment of flora imbalance related diseases such as IBD.

The invention discloses a type III pullulan hydrolase mutant with improved enzyme activity and a construction method thereof, and relates to the technical field of gene engineering and enzyme engineering. The amino acid sequence of the III type pullulan hydrolase mutant is as shown in SEQ ID NO. 3. According to the present invention, on the basis of the type III pullulan hydrolase TK-PUL from Thermococcus kodakarensis, the type III pullulan hydrolase mutant with the improved enzyme activity is developed through the site-specific mutagenesis, such that the type III pullulan hydrolase mutant with the improved enzyme activity is provided; the specific enzyme activity of the III type pullulan hydrolase mutant to cassava starch is improved by 1.83 times. The cassava starch degradation capacity of the III type pullulan hydrolase mutant is obviously improved, the enzymatic property of the III type pullulan hydrolase mutant meets the requirements of the production and preparation process of the straight-chain maltooligosacharide, and the application potential of the III type pullulan hydrolase mutant in the production and preparation of the straight-chain maltooligosacharide is improved.

The invention discloses a serine hydroxymethyltransferase mutant and an application thereof in production of L-serin.The serine hydroxymethyltransferase mutant with the specific enzyme activity remarkably improved is obtained by conducting saturated mutation on serine hydroxymethyltransferase from escherichia coli and conducting screening, and the serine hydroxymethyltransferase mutant is applied to synthesis of L-serine. The serine hydroxymethyltransferase disclosed by the invention can be used for effectively improving the efficiency of catalyzing glycine and formaldehyde to synthesize L-serine by using the serine hydroxymethyltransferase, reducing the enzyme dosage, remarkably reducing the production cost and reducing the separation difficulty of downstream products.

The invention relates to the field of biology, and discloses an enzyme linked immunosorbent assay kit for detecting human metapneumovirus antigens and a quantitative detection method.The enzyme linked immunosorbent assay kit for detecting the human metapneumovirus antigens comprises a capture antibody which is a human metapneumovirus specific antibody HMPV01 or an antigen binding fragment thereof and comprises an HMPV01 antibody light chain amino acid sequence SEQ ID NO: 1 and an HMPV01 antibody heavy chain amino acid sequence SEQ ID NO: 2; the recognition antibody is a human metapneumovirus specific enzyme-labeled antibody HMPV02-HRP or an antigen binding fragment of the human metapneumovirus specific enzyme-labeled antibody HMPV02-HRP. A capture antibody HMPV01 and a recognition antibody HMPV02-HRP with specific amino acid sequences are screened, the antibody is efficiently prepared by using a mammalian cell expression system, and an optimized detection method is combined, so that the binding efficiency of the antibody and the antigen is remarkably improved, and the kit can detect the low-concentration human metapneumovirus antigen.