318 results about "Pichia" patented technology

The invention belongs to the technical field of protein engineering, and discloses a Brazilian sweet protein mutant and application thereof. According to the invention, lysine is used for replacing aspartic acid at the 29th site of Brazilian sweet protein, and / or arginine is used for replacing glutamic acid at the 36th site, and / or alanine is used for replacing aspartic acid at the 50th site, amino acid mutation at the sites is carried out to construct a Brazilian sweet protein mutant, and the Brazilian sweet protein mutant is subjected to heterologous expression in pichia pastoris GS115, so that the Brazilian sweet protein mutant is obtained. And carrying out sweetness performance evaluation on the expressed Brazilian sweet protein mutant. The sweetness property of the double mutant Asp29Lys-Asp50Ala protein is improved by 240% compared with the sweetness property of the Brazilian sweet protein before mutation.

The invention provides cat serum albumin and application thereof, and relates to the technical field of protein engineering. According to the invention, mutation is carried out on the cat serum albumin for the first time to obtain a beneficial mutation site, so that the cat serum albumin mutant which can be highly expressed in a pichia pastoris system is obtained. In addition, the cat serum albumin mutant I31L also has the effect of treating ascites due to cirrhosis, and the treatment effect is obviously higher than that in the prior art. A new biological material is provided for application of the cat serum albumin, and a foundation is laid for genetic engineering modification of the cat serum albumin.

The invention provides a recombinant XVII type collagen and application thereof, and relates to the technical field of protein engineering. The novel recombinant human XVII type collagen is obtained by optimizing and screening collagen structural domain sequences of the human XVII type collagen and then combining the sequences. The recombinant human XVII type collagen is consistent with the corresponding part of the amino acid sequence of the human XVII type collagen, does not generate immunological rejection when being applied to a human body, and can be widely applied to the industries of surgical medical treatment and medical beauty. In addition, the recombinant human XVII type collagen is high in stability, and the problem of protein degradation in the process of expressing recombinant protein by pichia pastoris can be avoided. In addition, the recombinant human XVII type collagen also has the effects of high biological activity, high biological safety, promotion of cell proliferation and differentiation and promotion of hair growth, and can be applied to the field of cosmetics or medicines as a functional component.

The invention relates to the technical field of synthetic biology, in particular to recombinant XVII type collagen as well as a preparation method and application thereof.The amino acid sequence of the recombinant XVII type collagen comprises a sequence shown in any one of SEQ ID NO.1-SEQ ID NO.3. The recombinant XVII type collagen can be highly expressed in an escherichia coli and pichia pastoris system, the expression system is simple, the cost is low, and the recombinant XVII type collagen is suitable for industrial production. The yield is high; the biological activity is good. The protein can be compounded with other proteins to form raw materials of tissue engineering products, cosmetics, health care products or medicines, so that the protein can be widely applied to the fields of medicines, medical instruments, biological materials, tissue engineering, cosmetics and the like.

The invention discloses a multi-effect repair type collagen and application thereof, and belongs to the technical field of synthetic biology. Transdermal peptide TD-1, a transmembrane region of human XVII type collagen, an extracellular sixteenth non-collagen region, an extracellular fifteenth collagen region and a coding gene of a His tag are selected to be connected in series, and a gene sequence is optimized through pichia pastoris codon selection preference; and then the T-COL17R3 is constructed and expressed to obtain the T-COL17R3. Efficacy experiments prove that compared with similar products sold in the market, T-COL17R3 not only has excellent transdermal performance, but also has better cell proliferation and migration promoting capability, better capability of resisting early saccharification product ketoamine and later saccharification product dicarbonyl compounds, better capability of scavenging free radicals and resisting elastase, and can be used for preparing the anti-epidermal drug. In addition, synthesis of melanin in B16-F10 cells can be reduced, so that T-COL17R3 has excellent application potential in development of pharmaceutical compositions or skin care products with repairing, anti-wrinkle and firming or whitening and brightening effects.

The invention discloses a high-transdermal recombinant humanized XVII type collagen as well as a preparation method and application thereof, and belongs to the technical field of synthetic biology. According to the preparation method, transdermal peptide TD-1, different functional fragments of human XVII type collagen and coding genes of His tags are selected to be connected in series, gene sequences are optimized through pichia pastoris codon selection preference firstly, and then the high-transdermal recombinant humanized XVII type collagen is obtained; and then the recombinant humanized XVII type collagen T-COL17-NC16 and the recombinant humanized XVII type collagen T-COL17 are constructed by expression of the recombinant humanized XVII type collagen T-COL17. Effect experiments prove that compared with similar products sold in the market, the skin-care product has more excellent transdermal performance, can improve cell proliferation and migration ability, also has obvious ability of resisting early saccharification product ketoamine and late saccharification product dicarbonyl compounds, better ability of scavenging free radicals and resisting elastase, and can be used for preparing the skin-care product. Moreover, synthesis of melanin in B16-F10 cells can be reduced, and the compound is expected to become a novel functional biological raw material to be applied to the fields of pharmaceutical compositions or skin care products and the like.

The invention relates to screening and application of a Candida antarctica lipase B mutant. Specifically, the Candida antarctica lipase B mutant provided by the invention is obtained by carrying out rational design and directed evolution combined strategy mutation on the basis of a wild Candida antarctica lipase B gene sequence, and the amino acid sequence of the mutant is shown as SEQ ID NO.3. The invention also relates to a preparation method of the Candida antarctica lipase B mutant. The mutant has higher enzyme activity and thermal stability, the hydrolytic catalytic activity of the mutant is improved to 2.1 times of the original hydrolytic catalytic activity, and the half-life period of the mutant enzyme at 50 DEG C is prolonged by 4 times. On the basis, pichia pastoris is used as a host to express the mutant, and a strain with hydrolytic activity improved by 52% is obtained through high resistance screening. The lipase is prepared into an immobilized enzyme to be used in a synthetic reaction of chlorogenic acid derivatives, the highest conversion rate of chlorogenic acid reaches 74% in 24 hours, and the immobilized enzyme has a good industrial application prospect.

The invention provides a Pichia megaterium BA1251 and a method for producing polyhydroxyalkanoate (PHA) by utilizing the Pichia megaterium BA1251 through semi-solid shallow tray fermentation. The Pichia megaterium BA1251 has the advantages that the Pichia megaterium BA1251 can be used for producing the polyhydroxyalkanoate (PHA) by the aid of the Pichia megaterium BA1251; the dry weight of zymophyte produced by the semi-solid fermentation method can reach 100g / kg, and the semi-solid fermentation method has the advantages of high yield, short period, low cost, less waste and environmental friendliness.

The invention belongs to the technical field of biological detection, and discloses a kit and a method for quantitatively detecting residual quantity of host cell protein of pichia pastoris in order to solve the problems of limit of quantitation and low detection sensitivity of an existing detection method. According to the present invention, the empty plasmid without the recombinant human serum albumin gene is introduced into the pichia pastoris, and purification is performed by combining the Protein A chromatographic column and the host cell protein coupling affinity column, such that the prepared polyclonal antibody can be effectively used for the quantitative detection of the residual amount of the pichia pastoris host cell protein in the biological product; the kit formed by the polyclonal antibody has good accuracy and repeatability on the quantitative detection of the host cell protein residues in the pichia pastoris source biological products, the quantification limit is 0.2 ng / mL, and the kit provided by the invention can meet the quantitative detection of the host cell protein residues in all the pichia pastoris source biological products.

The invention discloses a pichia pastoris engineering bacterium for synthesizing bakuchiol from de novo by converting methanol as well as construction and application of the pichia pastoris engineering bacterium. A heterologous p-coumaric acid synthesis pathway is introduced to neutral sites of different chromosomes of pichia pastoris, a high-yield p-coumaric acid strain is obtained through gene knockout, overexpression or heterologous expression of tyrosine and phenylalanine synthesis pathway key genes of a shikimic acid pathway, a heterologous bakuchiol biosynthesis pathway is introduced on the basis, and a high-yield p-coumaric acid strain is obtained. After overexpression of bakuchiol synthetase, endogenous overexpression or heterologous expression of MVA pathway key genes and exogenous acetyl coenzyme A supply pathway genes, methanol concentration optimization and bacterial strain His4 gene supplementation, the yield of bakuchiol is effectively increased to 91.2 mg / L and is increased by 59.8 times compared with that of an initial bacterial strain, and the yield of bakuchiol in a 15L fermentation tank reaches 692.8 mg / L. The method has the characteristics of high conversion efficiency, low production cost, convenience in preparation, wide industrial application prospect and the like.

The invention discloses a method for inducing plant disease resistance by using a hydrolase active mutant of xyloglucan specific glucanase XEG1. A pichia pastoris eukaryotic expression system is utilized to obtain the purified hydrolase activity mutant XEG1E136D protein of the phytophthora sojae core pathogenic factor xyloglucan specific glucanase XEG1, and the hydrolase activity mutant XEG1E136D protein does not have the hydrolase activity of plant cell walls and can activate the systemic resistance of plants. The XEG1E136D is overexpressed into a biocontrol bacterium trichoderma harzianum by utilizing an agrobacterium-mediated fungal transformation optimization system, and the XEG1E136D is proved to be capable of secreting XEG1E136D protein to the outside of cells and activating the broad-spectrum systemic resistance of plants. The XEG1E136D protein expressed by the trichoderma harzianum can be used as a plant vaccine to improve the prevention and treatment effect, and the trichoderma harzianum XEG1E136D protein has a wide application prospect in the field of plant disease prevention and treatment.

The invention belongs to the technical field of gene engineering, and relates to a method for efficiently integrating a target gene into a pichia pastoris genome in a multi-copy manner, which comprises the following steps: S1, constructing a pPIC9K recombinant plasmid containing a single-copy target gene or a pPICZ alpha Amut + recombinant plasmid containing a multi-copy target gene; s2, constructing and integrating a pichia pastoris strain containing the multi-copy target gene by utilizing the pPIC9K recombinant plasmid containing the single-copy target gene or the pPICZ alpha Amut + recombinant plasmid containing the multi-copy target gene; and S3, electrically transforming the recombinant plasmid constructed in the S1 into the pichia pastoris strain integrated with the multi-copy target gene constructed in the S2, and carrying out resistance screening. According to the invention, the contradiction between copy number and screening pressure in the traditional gene integration technology is broken through, and an engineering bacterium construction scheme with higher economical efficiency and stability is provided for industrial production of recombinant protein with high expression quantity.

The invention discloses an antibacterial peptide PPI45 / PPI47 as well as a preparation method and application of the antibacterial peptide PPI45 / PPI47. According to the invention, fungal defensin Plectasin is used as a template, and the self-assembled antibacterial peptide PPI45 / PPI47 is designed. The expression of the self-assembled antibacterial peptide PPI45 / PPI47 in pichia pastoris is realized by optimizing the gene sequence of the antibacterial peptide and constructing a specific expression vector, a perfect purification system is established, large-scale production can be realized, and the self-assembled antibacterial peptide PPI45 / PPI47 can be applied to the fields of antibacterial drug development, hydrogel wound treatment and the like, and has wide application value and market prospect.

The invention relates to recombinant pichia pastoris for high expression of porcine pancreatic phospholipase A2 and application of the recombinant pichia pastoris, and belongs to the technical field of genetic engineering. According to the method disclosed by the invention, a vacuole sorting receptor Vps10 is knocked out by utilizing a CRISPR-Cas9 system, a CPY sorting way between a trans-golgi apparatus and a vacuole is interrupted, and ppPLA2 degradation is reduced; then, in order to relieve unfolded protein response in the endoplasmic reticulum, molecular chaperones are introduced into the genome, and synthesis of ppPLA2 is enhanced; the expression intensity of the ppPLA2 is improved by increasing the gene copy number of the ppPLA2; and finally, high-density fermentation is performed in a 3-L bioreactor, so that high-efficiency expression of the ppPLA2 in the pichia pastoris is realized.

The invention discloses a pichia pastoris high-secretion strain screening system and a use method thereof. According to the system, pichia pastoris is used as a host, and the core structure of the system is as follows: an AOX1 promoter, an alpha-factor signal peptide, a target protein-P2A peptide, an alpha-factor signal peptide, a Gamilus fluorescent protein-G4S connecting peptide-Gcw21 anchoring sequence-AOX1 terminator. The use method comprises the steps of vector construction, conversion of enzyme digestion recovery products, clone strain selection and activation, fermentation, inducible expression and screening, and product collection to finally obtain the strain with high yield of target protein. Through integration of bicistronic design, P2A peptide self-cleavage and cell surface display technologies, efficient screening of target protein high-secretion type strains is realized.

The invention discloses a recombinant VII type collagen as well as a preparation method and application thereof. The recombinant VII type collagen is obtained by repeating a short amino acid sequence GLPGAKGEKGAP for a plurality of times. The secretion yield of the recombinant VII type collagen in a commercial pichia pastoris expression system can be up to about 17.3 g / L, the extracellular secreted protein is basically not degraded in the fermentation process, the purity can reach 90% or above through simple ultrafiltration and decoloration, and industrial mass production can be achieved; and the recombinant VII type collagen has better biological activities of promoting autophagy, improving an endoplasmic reticulum stress state, promoting collagen secretion and inhibiting matrix metalloproteinase from degrading collagen, and shows good tightening and anti-wrinkle effects.

The invention discloses a method for biological high-density synthesis of retinaldehyde and a synthetic strain thereof. The synthetic strain is obtained by expressing ATP citrate lyase ACL, acetyl-CoA synthase ACS, choline kinase CK, inositol polyphosphate kinase IPK and vitreoscilla hemoglobin VHb in host bacteria. Wherein the host bacterium is a pichia pastoris gene modified bacterial strain PP-B2C. The retinaldehyde production performance of the recombinant strain is verified on the basis of a precursor supply pathway, an IUP pathway and a dissolved oxygen level, and the retinaldehyde production capacity of the pichia pastoris is further improved. The construction method of the recombinant pichia pastoris is simple, the synthesis of retinaldehyde can be better promoted, and the retinaldehyde can be efficiently synthesized by the engineering strain by utilizing glucose and methanol through amplification fermentation of a 5L fermentation tank, so that the recombinant pichia pastoris is beneficial to industrial production.

The invention belongs to the field of gene engineering. In particular to high-stability recombinant XVII type collagen as well as a preparation method and application thereof. The recombinant XVII type collagen is obtained by repeating an amino acid sequence (as shown in SEQ ID NO.1) from a natural human XVII type collagen peptide for 2-5 times. The recombinant XVII type collagen can also be secreted and expressed in a pichia pastoris expression system, the preparation method is simple, and the high-yield recombinant XVII type collagen can be obtained at low cost. The cell proliferation, migration and adhesion promoting activities of the recombinant XVII type collagen are obviously superior to those of commercially available XVII type collagen, a triple helix structure can be formed at room temperature, a 1% aqueous solution has high-temperature stability and moist heat sterilization stability, and the recombinant XVII type collagen can be widely applied to the fields of cosmetics and medical instruments.

The invention belongs to the technical field of biology, and particularly discloses a high-density fermentation method and application of recombinant spider silk protein, and the high-density fermentation method comprises the following steps: firstly, transforming an expression vector carrying spider silk protein genes into modified pichia pastoris cells to obtain a strain; the activated strain is subjected to expanding culture, high-density fermentation culture and purification, and recombinant spider silk protein is obtained; wherein the transformation means of the pichia pastoris cell is to integrate Vitreoscilla hemoglobin Vhb gene into the pichia pastoris cell by utilizing a gene recombination technology, and the expression of the Vitreoscilla hemoglobin Vhb gene is improved by carrying out metabolic engineering transformation on the pichia pastoris cell for expression and optimizing the regulation and control of staged fermentation parameters, so that the expression efficiency of the Vitreoscilla hemoglobin Vhb gene is improved. The problems that in existing recombinant protein fermentation, oxygen dependence is high, product degradation is serious, purity is low, and large-scale stability is poor are solved, the yield and purity of recombinant spider silk protein are guaranteed, and large-scale production of the recombinant spider silk protein is facilitated.

The invention discloses an indirect ELISA (enzyme-linked immuno sorbent assay) detection method of a porcine epidemic diarrhea virus antibody SIgA, and belongs to the technical field of animal antibody detection. In order to solve the problems of limited detection range and single immune evaluation dimension of a porcine epidemic diarrhea virus detection method in the prior art, the invention provides an indirect ELISA detection method of a porcine epidemic diarrhea virus antibody SIgA, and the detection method adopts a pichia pastoris eukaryotic secretion platform to prepare a high-activity PEDV S1 antigen; meanwhile, a secreting type IgA antibody is used as a detection target; the method has the advantages of high detection sensitivity, low background noise, better variant compatibility and practical popularization value, and provides a clinical and industrial-level solution for maternal immunity monitoring, piglet passive protection evaluation and vaccine immunity strategy optimization.

The invention belongs to the technical field of gene detection of cross fusion of biology and a new generation of information technology, and particularly relates to a method for detecting residual DNA of multiple host cells based on digital PCR (Polymerase Chain Reaction). The invention discloses a multiplex digital PCR quantitative detection primer pair and a probe group for detecting residual DNA of CHO cells, Vero cells, pichia pastoris, escherichia coli and NS0 cells for the first time. By utilizing the method, not only can the residual DNA of five host cells be simultaneously subjected to single or multiple detection in a single reaction, but also non-specific amplification, signal interference and detection limitation of the residual DNA of the host cells in the qPCR detection process can be solved friendly, and meanwhile, the original concentration of a sample is absolutely quantified by the method; the method does not depend on the establishment of a standard curve, reduces the influence caused by a standard product, and is superior to the prior art.

The invention provides recombinant III-type collagen and application thereof, and relates to the technical field of genetic engineering. According to the invention, the yield of the collagen is improved by optimizing the nucleotide sequence of the target gene and optimizing the culture conditions of pichia pastoris, so that the collagen is efficiently expressed in engineering bacteria. The recombinant engineering bacterium shows strong potential in the aspect of improving the yield of protein with high economic value, and is suitable for large-scale industrial production. The recombinant III-type collagen is high in expression quantity, simple in preparation process and suitable for preparation of biological materials for medical cosmetology, wound repair and the like, and has a wide application prospect.

The invention discloses recombinant human VII type collagen as well as a preparation method and application thereof, and belongs to the technical field of biochemical engineering. The recombinant human VII type collagen comprises a plurality of amino acid residue repetitive units shown as SEQ ID NO.1. Compared with natural VII type collagen, the recombinant human VII type collagen obtained by repeating the repetitive units for multiple times has the advantages that the molecular weight is smaller, the sequence is more easily and efficiently secreted and expressed in a pichia pastoris system after optimization, and the recombinant human VII type collagen can be used for preparing the recombinant human VII type collagen. The method has the characteristics of high yield, low cost, simplicity in operation and easiness in large-scale production. Meanwhile, the anti-oxidation activity is excellent, the skin moisturizing and repairing capacity and the wound healing capacity are promoted, due to the fact that the collagen is derived from human collagen, the risks of allergy and rejection reaction can be remarkably reduced, and the safety is extremely high. Therefore, the recombinant collagen can be used as a core active component to be widely applied to the fields of cosmetics, medicines and the like, and has a good application prospect.

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 present application relates to the field of gene editing technology, bioengineering and application of microbial fermentation, and discloses a Pichia pastoris high-efficiency gene editing system, a construction method thereof and application in a high-yield cordycepin engineering strain.The construction of the Pichia pastoris CRISPR-Cas9 gene editing system mainly includes the following steps: the histidine HIS4 nutritional deficiency back complementation is used to realize the resistance-free assembly of KhCas9; the sgRNA-tRNA array and the IIS type restriction endonuclease combination are used to simplify the gene editing operation and realize the simultaneous and high-efficiency editing of multiple genes; and the Brex27 domain is fused with KhCas9 to strengthen the homologous recombination efficiency. By using the gene editing system, through the optimization of methanol assimilation, 3'-AMP and adenosine precursor supply, ATP / NADPH energy supply and the like, the construction of a cordycepin engineering strain without resistance gene residues is realized for the first time, the gene editing efficiency of Pichia pastoris is greatly improved, and a powerful tool is provided for the industrialized production of cordycepin.

The invention discloses a fuzzy intelligent control method and device for a pichia pastoris fermentation process. The fuzzy intelligent control method comprises the following steps: (1) integrating an online sensor in a bioreactor and monitoring state parameters of fermentation liquor in real time; (2) inputting the monitored parameters into a central control system, and processing the parameters through a fuzzy intelligent control algorithm; and (3) according to an output instruction of the fuzzy intelligent control algorithm, cooperatively regulating and controlling fermentation operation parameters in real time. According to the method disclosed by the invention, a fuzzy intelligent control algorithm is developed by monitoring dissolved oxygen, relative concentration of dissolved carbon dioxide, methanol concentration and pH in fermentation liquor in the fermentation process in real time, so that the fermentation process is accurately regulated and controlled by multi-parameter coordination, and the method is applied to process regulation and control of pichia pastoris fermentation expression recombinant protein. The expression quantity and the production efficiency of the recombinant albumin can be remarkably improved, the production period is shortened, and the method is suitable for industrial large-scale production.

The invention discloses recombinant poria cocos chitin endonuclease as well as a gene, a preparation method and application thereof. The nucleotide sequence of the gene is shown as SEQ ID NO.1 in a sequence table. According to the nucleotide sequence as shown in SEQ ID NO.1, high-level recombinant secretory expression of target protein in pichia pastoris host bacteria can be realized by taking pichia pastoris inducible expression plasmid pPICZ alpha A as a carrier. Under a shake flask fermentation condition, the average secretory expression quantity can reach 300.3 mg / L. The recombinant enzyme obtained by nickel ion affinity chromatography purification not only can effectively hydrolyze colloidal chitin to generate chitosan oligosaccharide (COS), but also can directly degrade chitin-containing raw materials such as shrimps, crabs and the like to generate COS. In addition, the enzyme also shows the activity of hydrolyzing polysaccharides such as cellulose, pectin, agar and the like, and has important potential values in the fields of functional chitosan oligosaccharide preparation, biological energy production, medicine development, feed, environmental protection, agricultural application and the like.

This patent application discloses a recombinant human type II collagen, its preparation method, and its uses. The recombinant human type II collagen of this patent application is a truncated protein of natural human type II collagen, and its amino acid sequence is shown in SEQ ID No: 1. The recombinant human type II collagen of this invention can be expressed in commercial expression systems such as the commercial Pichia pastoris expression system with high expression yields. Furthermore, its tested biological activities (promoting cell proliferation and wound healing) are significantly superior to those of natural human type II collagen, and also significantly superior to other stages of natural human type II collagen.

The invention discloses a high-biological-activity human-derived I-type collagen variant, a composite material based on the high-biological-activity human-derived I-type collagen variant and a preparation method. According to the invention, the COL109 fragment which can be efficiently secreted and expressed in pichia pastoris and has a triple helix structure is obtained through screening; an adhesion domain (GPP) 10 is further fused to improve the mechanical strength, and a variant COL109 (GPP) 10 is obtained; and finally, compounding with polycaprolactone (PCL) according to an optimized ratio (1: 1) to obtain the composite material with high biological activity (promoting osteogenic differentiation and wound healing) and excellent mechanical properties. The material is suitable for bone tissue engineering scaffolds, skin regeneration dressings and the like.

The application discloses a kind of multi-effect repair type collagen and its application in the technical field of synthetic biology, the application selects transdermal peptide TD-1, the coding gene of the transmembrane region of human XVII type collagen, extracellular sixteenth non-collagen region and extracellular fifteenth collagen region and His tag is connected in series, and gene sequence is optimized by pichia pastoris codon selection preference, then obtains T-COL17R3 by construction and expression. Through efficacy experiment, it is verified that T-COL17R3 compared with similar products on sale, not only excellent transdermal performance, also has more optimal ability of promoting cell proliferation, migration, anti early glycation product ketone amine and anti late glycation product dicarbonyl compound, better free radical scavenging ability and anti-elastase ability, and can reduce the synthesis of melanin in B16-F10 cell, therefore, T-COL17R3 has excellent application potential in the development of drug composition or skin care product with repair, anti-wrinkle firming or whitening effect.