1103 results about "Threonine" patented technology

The invention relates to a recombinant escherichia coli THRS and a method for synthesizing L-threonine by using the recombinant escherichia coli THRS. The invention belongs to the technical field of bioengineering, and provides a recombinant escherichia coli THRS which overexpresses encoding genes of ppc, aspC, aspA, thrAmutBC, asd, rhtC, rhtA, asdtm and thrAmut, knockout an encoding gene of fnr and knockout an encoding gene of iclR, the recombinant escherichia coli THRS takes glucose as a substrate for fermentation, and the yield and conversion rate of L-threonine are obviously improved; the L-threonine strain has the advantages that the L-threonine strain does not contain exogenous plasmids, all modification sites are integrated onto a genome, higher stability is achieved, antibiotics do not need to be added into a fermentation culture medium of the strain, and the produced L-threonine product is free of antibiotic residues and higher in safety.

The invention belongs to the technical field of gene engineering, and particularly relates to applications of OpgG and a mutant thereof in production of human milk oligosaccharide. The invention provides a dextran biosynthetic protein OpgG mutant, and the OpgG mutant is obtained by mutating the 443rd amino acid from threonine to proline on the basis of a wild type dextran biosynthetic protein OpgG as shown in SEQ ID NO.1. The invention also provides a preparation method of the dextran biosynthetic protein OpgG mutant. An opgG gene and / or a T443P mutant coding gene are / is introduced into a human milk oligosaccharide production strain and applied to production of human milk oligosaccharide, and the yield of 3 '-SL, 6'-SL, LNT II, LNnT and LNT is greatly increased.

The invention discloses recombinant escherichia coli for inactivating or weakly expressing SPMB family inner membrane protein and application of the recombinant escherichia coli in production of L-amino acid. The invention relates to the technical field of gene engineering, and provides recombinant escherichia coli, and SPMB family inner membrane protein in the recombinant escherichia coli is inactivated or reduced in activity. According to the invention, the yjiG gene (coding gene of SPMB family inner membrane protein) in escherichia coli is knocked out, so that the expression intensity of the yjiG gene is weakened, and fermentation production strains of L-threonine, L-tryptophan, L-arginine and L-valine, which are more cost-effective, can be produced. The invention has important significance for improving the fermentation yield of bacteria, namely L-threonine, L-tryptophan, L-arginine and L-valine.

The invention discloses a formate dehydrogenase mutant and application thereof in catalytic synthesis of D-mannitol, and belongs to the technical field of bioengineering. According to the formate dehydrogenase mutant provided by the invention, the 18th-site glutamic acid of wild-type formate dehydrogenase with an amino acid sequence shown as SEQ ID NO.2 is mutated into proline, the 57th-site asparagine is mutated into glutamic acid, the 70th-site histidine is mutated into tryptophan, the 235th-site serine is mutated into threonine, and the 316th-site valine is mutated into threonine, so that the formate dehydrogenase mutant is high in enzyme activity and catalytic activity; the coenzyme circulation efficiency during the production of D-mannitol can be obviously improved, so that the yield of D-mannitol can be effectively improved. When the genetically engineered bacterium co-expressed by the formate dehydrogenase mutant and the mannitol dehydrogenase mutant is used for catalyzing 150 g / L fructose to produce D-mannitol, the yield of D-mannitol within 15 h can reach 140 g / L or above.

The invention relates to the field of polypeptide compositions, in particular to a polypeptide metal chelate and application thereof in the field of cosmetics, and the polypeptide metal chelate is formed by chelating a polypeptide compound and a metal ion compound. The structure of the polypeptide compound is [gamma-Glu] n-AA, n is greater than or equal to 1, and AA is selected from glycine, alanine, valine, leucine, isoleucine, methionine (methionine), proline, tryptophan, serine, tyrosine, cysteine, phenylalanine, asparagine, glutamine, threonine, asparaginic acid, glutamic acid, lysine, arginine or histidine; the polypeptide chelated zinc prepared by the invention has remarkable oil control and anti-inflammatory effects, and can be compounded with other raw materials to form cosmetics with oil control and acne removal effects.

Composition for use in the prevention and / or treatment of a liver disease in a mammal, the composition comprising an active agent, said active agent containing the amino acids leucine, isoleucine, valine, threonine, lysine and the carboxylic acids citric acid, succinic acid, malic acid.

The invention relates to the technical field of biology, and discloses a carbonyl reductase mutant and application thereof in enzymatic synthesis of chiral alcohol. The amino acid sequence as shown in SEQ ID NO.2 is subjected to mutation that 36th lysine is mutated into any one of aspartic acid, threonine and valine, or / and 125th histidine is mutated into any one of lysine, serine and leucine, or 170th histidine is mutated into any one of lysine, cysteine and leucine. The carbonyl reductase mutants, especially single-site mutants Mut-T75K, Mut-T75D and Mut-E216M and a combined mutant Mut-T75K-E216M, with activity improved to different extents compared with that of a wild type are obtained, have excellent relative enzyme activity, thermal stability and substrate tolerance, have relatively high activity and stability for various chiral alcohols, and can be used for preparing the carbonyl reductase mutants. The catalyst has the advantages of high catalytic activity, high thermal stability, strong substrate tolerance, easiness in fermentation and the like.

The invention belongs to the field of feeds, and discloses a biological feed containing a microbial microcapsule preparation and a preparation method of the biological feed. The biological feed is prepared from the following components in parts by weight: 90 to 93 parts of wall-broken rhodopseudomonas palustris powder, 2 to 3 parts of lysine hydrochloride, 0.1 to 0.5 part of methionine, 0.1 to 0.5 part of threonine, 0.3 to 1 part of arginine, 2 to 3 parts of calcium hydrophosphate, 1 to 2 parts of calcium carbonate, 0.5 to 1.2 parts of an antioxidant additive, 0.3 to 0.8 part of modified nano montmorillonite and 1 to 5 parts of a microbial microcapsule preparation. According to the biological feed, the wall-broken rhodopseudomonas palustris serves as basic nutrition and a main microorganism source of the feed and is matched with the compound probiotics of the microorganism micro-capsule preparation, the intestinal nutrition utilization rate is effectively increased, meanwhile, the antioxidant additive is added, and the problems that a single additive is narrow in function and prone to oxidation are solved; the modified nano montmorillonite is added to solve the problem of antagonism of toxin adsorption and mineral absorption.

A boron carrying agent, a preparation method therefor, and a pharmaceutical formulation. The boron carrying agent contains compound 1, N-4-carboxyphenylboronic acid amide-threonine-phenylalanine-phenylalanine-tyrosine-glycine-glycine-serine-arginine-glycine-lysine-arginine-aspartic acid-aspartic acid-phenylalanine-lysine-threonine-glutamic acid-glutamic acid-tyrosine-cysteine, having a molecular formula of C114H158BN30O35S1 and a molecular weight of 2552.4, and further contains compound 2, N-4-carboxyphenylboronic acid amide-arginine-lysine-lysine-lysine-arginine-arginine-glutamine-arginine-arginine-arginine, and / or compound 3, N-4-carboxyphenylboronic acid amide-methionine-alanine-serine-methionine-threonine-glycine-glycine-glutamine-glutamine-methionine-glycine. Compounds 1-3 can serve as a targeted medicament for boron neutron capture therapy used for treating a cerebral glioma and a head and neck tumor.

The invention belongs to the technical field of microbial fermentation, and discloses torulopsis variabilis and application thereof. Wild torulopsis variabilis is separated from soy sauce mash, a strain of torulopsis variabilis with high yield of aspartic acid, threonine, glutamic acid, valine, methionine, isoleucine, leucine and lysine is obtained through ARTP mutagenesis, the collection number of the torulopsis variabilis ZB444 is GDMCC No: 65240, the classification name of the Latin name of the torulopsis variabilis is Wickhamiella versitis, the collection number of the torulopsis variabilis ZB444 is CGMCC No: 65240, and the collection number of the torulopsis variabilis ZB444 is CGMCC No: 65240. The strain is preserved in Guangdong Microbial Culture Collection Center on October 12, 2024. The strain is applied to soy sauce fermentation, the content of various amino acids and the content of total amino acids in soy sauce can be increased, the nutritional value of the soy sauce can be increased, and meanwhile the flavor of the soy sauce is enhanced.

The invention belongs to the technical field of plant heredity and genetic engineering, and particularly relates to a wheat saline-alkaline tolerant protein kinase gene TaCRCK and application thereof. Specifically, the invention discloses a wheat saline-alkaline tolerant protein kinase gene TaCRCK, and the nucleotide sequence of cDNA of the gene is as shown in SEQ ID NO. 1. The invention also discloses a plant expression vector containing the gene TaCRCK and application of the gene and the plant expression vector in cultivation of saline-alkali resistant plants. Tests prove that silent expression of the gene promotes the resistance of wheat to saline-alkaline stress, and the saline-alkaline tolerance of transgenic plants is obviously improved. The gene has a negative regulation effect on the salt and alkali tolerance of plants, provides a new tool and method for improving the salt tolerance of crops by using a genetic engineering means, and has important scientific significance and application prospects.

Provided is a compound of formula (I), or a pharmaceutically acceptable salt thereof, or a pharmaceutical composition thereof, having membrane associated tyrosine and threonine kinase inhibitory activity, and the use of the compound of formula (I) or the pharmaceutically acceptable salt thereof as a membrane associated tyrosine and threonine kinase inhibitor for the prevention or treatment of diseases mediated by membrane associated tyrosine and threonine kinase, such as tumors. # imgabs0 #

The invention belongs to the technical field of bioengineering, and relates to a transaminase mutant, a recombinant genetically engineered bacterium and application of the transaminase mutant in catalytic synthesis of (R)-1-Boc-3-aminopiperidine.The transaminase mutant is obtained by conducting single-point or combined mutation on the 131 site and / or the 197 site of an amino acid sequence shown in SEQ ID NO.2; the mutation sites comprise that the 131 phenylalanine is mutated into aspartic acid, threonine or tyrosine, and / or the 197 lysine is mutated into arginine or leucine. Experimental results show that compared with wild type transaminase, the catalytic activity, the thermal stability and the organic solvent tolerance of the obtained mutants, especially single-point mutants MyTA1-F131Y and MyTA1-K197R and a combined mutant MyTA1-F131Y-K197R, are all remarkably improved, and compared with the wild type transaminase, the catalytic activity, the thermal stability and the organic solvent tolerance of the obtained mutants are all remarkably improved. The mutant MyTA1-F131Y-K197R can be used for efficiently catalyzing asymmetric amination of N-Boc-3-piperidone to synthesize (R)-1-Boc-3-aminopiperidine, the conversion rate of the (R)-1-Boc-3-aminopiperidine after the (R)-1-Boc-3-aminopiperidine reacts for 24 hours under the condition that the substrate concentration is 100 g / L can reach 90% or above, and the mutant MyTA1-F131Y-K197R has a good industrial application prospect.

The invention provides p-hydroxymandelic acid synthetase, a gene, a mutant of the p-hydroxymandelic acid synthetase and application of the p-hydroxymandelic acid synthetase in asymmetric synthesis of (S)-mandelic acid. The p-hydroxymandelic acid synthetase disclosed by the invention is derived from actinomycetes Actinokineospora auranticola, the amino acid sequence of the p-hydroxymandelic acid synthetase is as shown in SEQ ID NO.1, and a mutant of the p-hydroxymandelic acid synthetase is obtained by performing single-point mutation or multi-point combined mutation on glutamic acid at the 187th site, isoleucine at the 189th site and threonine at the 211th site of the amino acid sequence as shown in SEQ ID NO.1. The p-hydroxymandelic acid synthetase and the mutant thereof can convert phenylpyruvic acid into (S)-mandelic acid with high optical purity, have the advantages of mild reaction conditions, simplicity and convenience in operation, safety, environment friendliness and the like, and have a very good industrial application prospect.

The invention relates to a mutant based on cytochrome P450BM3 and application of the mutant in chloroaniline biodegradation, and belongs to the field of enzymology. The mutant is obtained by mutating threonine at the 268 site of an amino acid sequence shown in SEQ ID NO.1 into aspartic acid or glutamic acid, mutating alanine at the 328 site into phenylalanine, and mutating alanine at the 328 site into phenylalanine. According to the present invention, the amino acid at the 87 site is mutated into alanine, and the valine at the 78 site is mutated into alanine, such that a variety of mutants such as T268D / A328F, T268E / A328F, T268D / A328F / F87A, T268E / A328F / F87A, T268D / A328F / F87A / V78A and T268E / A328F / F87A / V78A are obtained; according to the present invention, the degradation rate of the mutant on 4-chloroaniline, 2-chloroaniline, 2, 4-dichloroaniline, 3, 4-dichloroaniline and 3, 5-dichloroaniline is achieved; the method has important significance and application value for promoting rapid degradation of chloroaniline pollutants in a water environment and maintaining ecological balance.

The invention discloses a polypeptide with a whitening effect and a preparation method and application thereof.The polypeptide is obtained from hydrolyzed protein of babylonia areolata, the amino acid sequence of the polypeptide is cysteine-arginine-proline-threonine-cysteine-serine-arginine-leucine-alanine-cysteine, and the amino acid sequence of the polypeptide is cysteine-arginine-proline-threonine-cysteine-serine-arginine-leucine-alanine. The compound can obviously inhibit the generation of melanin in cells and the activity of tyrosinase in vitro, has the characteristics of low toxicity, low irritation, good stability, safety and high efficiency, and can be applied to whitening cosmetics.

The invention relates to a Kluyveromyces marxianus strain with high protein yield and application of the Kluyveromyces marxianus strain, which is characterized in that the Kluyveromyces marxianus strain is firstly cultured on a slant, then is transferred into a seed culture medium for seed preparation, and then is inoculated into a fermentation tank, and yeast protein is obtained by adopting index feeding; the bacterial strain is a dominant mutant strain Kluyveromyces marxianus YWX-1, the protein content in a dry thallus reaches 55% or above and is increased by 26% or above compared with that of an original bacterial strain, the bacterial strain can be used for production of single-cell protein, the essential amino acid index (EAAI) value in the protein reaches 1.2, and the bacterial strain is rich in arginine, threonine and lysine and can be applied to production of single-cell protein. These amino acids play a key role in immune regulation, intestinal mucosal barrier function and muscle protein synthesis of young animals. The YWX-1 kluyveromyces marxianus strain has a wide application prospect in the production of neoplasm protein.

This application relates the use of a combination of a membrane-associated tyrosine and threonine- specific CDC2-inhibitory kinase (Myt1) inhibitor with a Weel inhibitors in treating cancer or inducing cell death. The synergistic effect of the combination results in a subtherapeutic dose or a reduced dosing schedule of the Myt1 inhibitor, the Wee1 inhibitor, or both relative to a monotherapy of either the Myt1 inhibitor or the Wee1 inhibitor in isolation.

The invention discloses a gelator and a preparation method and application thereof, the structural formula of the gelator is # imgabs0 #, R1 is a side chain group connected to an amino acid central carbon atom except an amino group, a carboxyl group and a hydrogen atom; the amino acid is selected from one of glycine, alanine, valine, leucine, isoleucine, methionine, proline, tryptophan, serine, tyrosine, cysteine, phenylalanine, asparagine, glutamine, threonine, aspartic acid, glutamic acid, lysine, arginine, histidine, selenocysteine and pyrrole lysine; the amino acid is selected from one of glycine, alanine, valine, leucine, isoleucine, methionine, proline, tryptophan, serine, tyrosine, cysteine, phenylalanine, asparagine, glutamine, threonine, aspartic acid, glutamic acid, lysine, arginine, histidine, selenocysteine and pyrrole lysine; r2 is alkyl with the carbon atom number of 16 to 19; and R3 is 9-fluorenyl methoxy carbonyl group or t-butyloxycarbonyl group. The gelator has a hydrophobic long alkyl tail chain, can spontaneously gather and assemble into a three-dimensional network structure through hydrogen bonds, pi-pi interaction and hydrophobic force, and fixes an oil phase in an oil solvent or an oil-water mixture in an effective manner to form high-strength gel.

The invention discloses a high-stability carbonyl reductase mutant and application of the high-stability carbonyl reductase mutant in chiral alcohol synthesis. An amino acid sequence as shown in SEQ ID NO.2 is mutated as follows: 20th leucine is replaced by any one of lysine, threonine, aspartic acid or isoleucine, and / or 55th leucine is replaced by any one of methionine, serine, lysine or isoleucine, and / or 55th leucine is replaced by any one of methionine, serine, lysine or isoleucine. Compared with a wild type enzyme, the stability of the obtained mutant is remarkably improved, particularly, single-point mutants Mut-L20I and Mut-L55I and a combined mutant Mut-L20I-L55I show excellent relative enzyme activity, thermal stability and substrate tolerance. The mutant has high catalytic activity and stability to various chiral alcohols, has the advantages of high catalytic efficiency, high thermal stability, strong substrate tolerance, easiness in fermentation production and the like, and is suitable for industrial application of enzymatic synthesis of chiral alcohols.

The invention discloses a method for synthesizing a high-purity pseudo proline dipeptide heterocyclic ring. The method comprises the following steps: (1) preparing L-serine or L-threonine into corresponding methyl ester hydrochloride; (2) condensing the methyl ester hydrochloride obtained in the step (1) with a condensation reagent to form a corresponding pseudo proline ring; and (3) condensing the pseudo-proline ring formed in the step (2) and related amino acid protected by Fmoc to obtain the corresponding pseudo-proline dipeptide heterocyclic ring. The total yield of the target product synthesized by the reaction can reach more than 80%. The method solves the problems of long reaction time, low yield, high safety risk and the like in the reported route, and has the advantages of cheap and easily available raw materials, lower production cost, simplicity in operation, environmental friendliness, high yield, short reaction time, simplicity in post-treatment and the like.

The present invention provides modified aminoacyl-tRNA synthetases (ARSs) having increased reactivity with N-methyl amino acids compared to natural aminoacyl-tRNA synthetases. The modified aminoacyl-tRNA synthetases according to the present invention can aminoacylate tRNAs with their corresponding N-methyl-substituted amino acids such as N-methyl-phenylalanine, N-methyl-valine, N-methyl-serine, N-methyl-threonine, N-methyl-tryptophan and N-methyl-leucine more efficiently than natural aminoacyl-tRNA synthetases. The present invention enables a more efficient production of polypeptides containing N-methyl amino acids.

The invention discloses a method for producing feed by using corn sugar residues, and belongs to the technical field of fermentation. The method comprises the following steps: pretreating, proportioning, adding an antibacterial agent, fermenting, drying and crushing, coating, cooling and the like, mixing corn sugar residues, corn germ meal and threonine mother liquor according to a specific ratio, adding zinc oxide and a chitosan antibacterial agent, and inoculating Saccharomyces cerevisiae ATCC 9763 for fermenting. And performing multi-stage drying and crushing on the fermentation product, spraying a coating emulsion prepared from a defatted soybean meal extract, curcumin, vitamin E, lecithin and sophorolipid, and performing air cooling to prepare the feed. According to the method, by-products are fully utilized, the crude protein content of the feed is 32-34.5%, the diameter of an inhibition zone is 18.1-20.2 mm, the moisture absorption rate is 2.7-3.4%, the palatability score is 8.0-8.6, and the fermentation yield is 92-94%. The innovation point lies in specific strain fermentation and functional coating, and is suitable for industrial production.

The present application relates to a pyridoxal kinase mutant, a recombinant expression vector and a microbial cell and their applications, and belongs to the technical field of biological catalysis. In order to solve the problem of low product concentration in existing enzyme catalysis, a pyridoxal kinase mutant is provided, the amino acid sequence is selected from the amino acid sequence shown in SEQ ID NO. 1, the lysine at position 229 is mutated to alanine, phenylalanine, methionine, arginine, threonine, histidine, serine, tyrosine, valine, leucine, isoleucine, proline, asparagine, aspartic acid or glutamic acid; the pyridoxal kinase mutant is used for catalyzing pyridoxal to synthesize pyridoxal phosphate, and a recombinant expression vector and a microbial cell can be further formed. The present application has good enzyme activity, high product conversion rate, high concentration of pyridoxal phosphate obtained, and the concentration of the product catalyzed by the wild-type pyridoxal kinase to phosphorylate pyridoxal is obviously improved.

The invention provides refractory concrete and a preparation method thereof, and belongs to the technical field of concrete. The preparation method comprises the following steps: modifying basalt fiber, modifying granite stone powder, grafting and mixing. The step of modifying the granite stone powder comprises the following steps: putting the granite stone powder into an ethanol solution, adding sorbitol laurate and polyoxyethylene sorbitan monolaurate, stirring at the stirring temperature of 46-50 DEG C, uniformly stirring, adding threonine, carrying out ball milling treatment for 26-30 minutes at the ball milling rotating speed of 114-125rpm according to the ball-to-material ratio of (3-5): 1, and after the ball milling is finished, cooling to room temperature to obtain the modified granite stone powder. Filtering and drying to obtain modified granite stone powder; the particle size of the granite stone powder is 135 to 145 nm; the mass concentration of the ethanol solution is 45-50%; the mass ratio of the granite stone powder to the ethanol solution to the sorbitol laurate to the polyoxyethylene sorbitan monolaurate to the threonine is (8.3 to 8.7) to (90 to 97) to (1.0 to 1.2) to (1.1 to 1.5) to (4.5 to 4.9); the prepared refractory concrete is high in strength, excellent in water permeability resistance, good in high-temperature corrosion resistance and low in linear shrinkage rate.

The invention discloses isavuconazole sulfate for injection. The isavuconazole sulfate comprises the following raw materials and auxiliary materials: isavuconazole sulfate, an excipient, a proper amount of a sulfuric acid solution (the pH value is adjusted to 1.3-1.5) and water for injection. And the excipient is mannitol, threonine and povidone. By adding mannitol, threonine and povidone and controlling the reasonable proportion of the components, the pH value of the environment where the medicine is located is adjusted, and rapid dissolution of isavuconazole sulfate is achieved. The excipient adopts three components for synergistic interaction, so that the stability of the isavuconazole sulfate for injection is improved, and the generation of impurities is reduced. The prepared isavuconazole sulfate for injection has good stability under the environments of long-term storage, strong light illumination, high temperature, high humidity and the like.

The present invention provides modified arninoacyl-tRNA synthetases (ARSs) having increased reactivity with N-methyl amino acids compared to natural aminoacyl-tRNA synthetases. The modified aminoacyI-tRNA synthetases according to the present invention can aminoacylate tRNAs with their corresponding N-methyl-substituted amino acids such as N-methyl-phenylalanine, N-methyl-valine, N-methyl-serine, N-methyl-threonine, N-methyl-tryptophan, and N-methyl-leucine more efficiently than natural aminoacyl-tRNA synthetases. The present invention enables a more efficient production of polypeptides containing N-methyl amino acids.

According to the infant amino acid nutritional rice flour and the preparation method thereof, four proteases including flavourzyme, pepsase, papain and bromelain are provided, and the proteases have very high hydrolytic activity and can fully hydrolyze protein in rice and whole milk powder to form various amino acids and polypeptide fragments, so that the nutritional rice flour is prepared; the rice flour is beneficial to digestion and absorption of infants, does not cause protein allergy, also improves the utilization rate of protein, and also can increase the flavor of the rice flour. Through detection, all 16 amino acids listed in GB5009.124-2016 Measurement of Amino Acid In Food National Standard for Food Safety can be detected in the infant amino acid nutritional rice flour prepared by the method disclosed by the invention; the amino acids are respectively alanine, valine, leucine, isoleucine, phenylalanine, proline, glycine, serine, threonine, tyrosine, methionine, lysine, arginine, histidine, aspartic acid and glutamic acid, the content of the glutamic acid is the highest, and the total amount of the amino acids can reach 10.5-11.2 g / 100g.

The invention relates to the technical field of polypeptide preparation, in particular to cyclic hexapeptide as well as a preparation method and application thereof. The preparation method comprises the following steps: reacting fluorenylmethoxycarbonyl-N6-trimethylsilylethoxycarbonyl acyl-L-lysine with 2-chlorotrityl chloride, and removing the protection of trimethylsilylethoxycarbonyl, so that amino is connected to dichloro resin; the preparation method comprises the following steps: taking fluorenylmethoxycarbonyl-O-tert-butyl-L-threonine, fluorenylmethoxycarbonyl-L-proline, fluorenylmethoxycarbonyl-L-alanine, fluorenylmethoxycarbonyl-aspartic acid-4-tert-butyl ester and fluorenylmethoxycarbonyl-L-leucine as a starting point, and then removing amino protection of terminal amino acid and carboxyl protection of the first amino acid; and carrying out condensation reaction and peptide cutting reaction to obtain the cyclic hexapeptide. The preparation method disclosed by the invention is simple in steps and simple and convenient to operate, the use of tetraphenylphosphine palladium is avoided, and the defects of low efficiency, high cost and low yield of the traditional liquid-phase cyclization method and solid-phase cyclization method are overcome.

The invention discloses a pyrrole lysyl-tRNA (transfer ribonucleic acid) synthetase mutant and application of the pyrrole lysyl-tRNA synthetase mutant. On the basis of the amino acid sequence of pyrrole lysyl-tRNA synthetase, the mutant comprises one or more of the following mutations: aspartic acid at the second site is mutated into asparagine, valine at the 31st site is mutated into isoleucine, threonine at the 56th site is mutated into proline, arginine at the 61st site is mutated into lysine, and arginine at the 61st site is mutated into lysine. Histidine at the 62nd site is mutated into tyrosine, threonine at the 122nd site is mutated into serine, and serine at the 193rd site is mutated into arginine; the amino acid sequence of the pyrrole lysyl-tRNA synthetase is as shown in SEQ ID NO. 1 (sequence identifier number 1). The pyrrole lysyl-tRNA synthetase mutant disclosed by the invention is higher in non-natural amino acid introduction efficiency, has universality to non-natural amino acids, solves the problem of low introduction efficiency of non-natural amino acids in proteins, and greatly expands research on structures and functions of proteins by introduction of non-natural amino acids.