57 results about "Collagen product" patented technology

A recombinant humanized collagen and a preparation method therefor. The recombinant humanized type III collagen can be efficiently and stably expressed in three expression systems of yeast, Escherichia coli, and CHO cells, and has the biological activity superior to that of a commercially available collagen product. The recombinant humanized type III collagen has structural characteristics and functional activity similar to those of a natural collagen, and thus has wide application prospects in biomedical materials, tissue engineering products, cosmetics, foods, health care products or drugs, medical instruments, medical cosmetology and the like.

The invention provides humanized recombinant XVII collagen for promoting hair follicle stem cell repair and resisting aging as well as a preparation method and application thereof, and belongs to the technical field of biological medicines. The humanized recombinant XVII type collagen comprises polypeptide derived from the XVII type collagen or repeated protein formed by N times of repeated series connection of the polypeptide serving as a unit, n is an integer from 2 to 4; the polypeptide derived from the XVII type collagen comprises a polypeptide A and / or a polypeptide B; the amino acid sequence of the A polypeptide is as shown in SEQ ID NO: 1; and the amino acid sequence of the B polypeptide is as shown in SEQ ID NO: 2. The humanized recombinant XVII type collagen not only can be massively and stably recombined and expressed, but also has cell adhesion activity, cell proliferation promotion activity, cell migration promotion activity and excellent hair follicle repair and regeneration promotion activity, and has no sensitization side effect. The invention provides a new way for preparing collagen products with rich functions.

The invention relates to the technical field of biochemical engineering and food processing, in particular to a fish collagen extraction process which comprises the following steps: S100, raw material pretreatment; s200, carrying out crushing and enzymolysis pretreatment; s300, carrying out an enzymatic hydrolysis reaction; s400, carrying out solid-liquid separation; s500, carrying out concentration treatment; and S600, drying treatment is carried out. The advanced spectrum analyzer is used for accurately determining the freshness of the fish body, the automatic cutting and ultrasonic cleaning technologies are combined, the quality of raw materials is effectively guaranteed, the enzymolysis reaction conditions are strictly controlled through the high-precision metering pump and the heat exchange system, the enzymolysis efficiency and the product quality are improved, and the production cost is reduced. By adopting a multi-layer composite membrane structure and a specific concentration technology, the efficiency and purity of solid-liquid separation and concentration treatment are remarkably improved, the production process is optimized, the energy consumption and the cost are reduced, pollutants in the production process are effectively removed through application of a plasma cleaning and air purification system, and the product quality is improved. And reliable guarantee is provided for production of high-quality fish collagen products.

The invention relates to a recombinant pichia pastoris genetically engineered bacterium for expressing recombinant full-chain-length humanized collagen as well as a preparation method and application of the recombinant pichia pastoris genetically engineered bacterium, and belongs to the technical field of genetic engineering. The recombinant pichia pastoris genetically engineered bacterium disclosed by the invention expresses recombinant full-chain-length humanized collagen, and a ku70 gene of the recombinant pichia pastoris genetically engineered bacterium is knocked out and knocked into a recombinant 4-proline hydroxylase encoding gene. Recombinant full-chain-length humanized collagen is optimized, a 4-proline hydroxylase gene and a collagen gene are co-expressed in pichia pastoris to obtain hydroxylation modified recombinant collagen, and a corresponding recombinant pichia pastoris genetically engineered bacterium is provided, has proteolytic enzyme A defect and hydroxylation modification capability, and can be used for preparing a recombinant collagen product. The stability of the collagen in the fermentation process is improved. The recombinant full-chain-length humanized collagen provided by the invention is 100% homologous with III-type collagen derived from a human body, so that the immune risk is extremely low, and the biological activity is more perfect.

The invention relates to the technical field of collagen preparation, in particular to a collagen product as well as a preparation method and application thereof. The collagen product prepared by the invention overcomes the problems of poor dissolution effect in cold water, poor fat solubility and poor emulsifying property. The preparation method comprises the following steps: crushing bovine bones, and performing collagen extraction, enzymolysis treatment, glycosylation treatment, fatty acid amidation treatment, polyphenol grafting modification and colloid compounding to obtain the collagen product. During glycosylation treatment, the cold water dissolving effect is improved by adjusting the variety of reducing sugar, the reaction temperature and time and grafting bone peptide molecules to sugar chains, and a flavor substance is generated by the Maillard reaction in the glycosylation treatment, so that the effect of covering the fishy smell of cattle bones is achieved; relevant parameters are adjusted through fatty acid amidation treatment, the bone peptide is endowed with liposolubility and emulsibility, and the solubility and emulsibility of the collagen product are synergistically improved through colloid compounding, optimization of the use amount of various colloids and control of reaction conditions.

The invention relates to the technical field of genetic engineering, in particular to recombinant humanized collagen and a preparation method thereof. The recombinant humanized III-type collagen provided by the invention can be efficiently and stably expressed under three expression systems of yeast, escherichia coli and CHO cells, and has biological activity superior to that of commercially available collagen products. The recombinant humanized III-type collagen disclosed by the invention has structural characteristics and functional activity similar to those of natural collagen, so that the recombinant humanized III-type collagen has wide application prospects in the aspects of biomedical materials, tissue engineering products, cosmetics, foods, health care products or medicines, medical instruments, medical cosmetology and the like.

The present invention relates to an I-type recombinant collagen with high transdermal absorbability, and the use thereof. The human I-type recombinant collagen with high transdermal absorbability of the present invention is composed of multiple repetitions of a short amino acid sequence from natural human I-type collagen as a repeating unit, wherein the short amino acid sequence is as shown in SEQ ID NO: 1, and the number of repetitions is three or more. The human I-type recombinant collagen with high transdermal absorbability of the present invention can be used as a raw material for producing various collagen products, such as an injection, a facial filler, a dressing, cosmetics, a health-care food product, tissue engineering material and a collagen sponge.

The invention provides a preparation method of a hydrolyzed collagen product with surface amphipathicity as well as the product and application thereof, and the preparation method comprises the following steps: (1) taking hydrolyzed collagen enzymatic hydrolysate as a substrate, then preparing a fermentation culture medium with vegetable oil and sugar, and fermenting by adopting candida bumblebee; (2) after fermentation, adding lysozyme into the fermentation liquor for activating treatment, and then sterilizing, centrifuging and filtering; and (3) carrying out freeze-drying treatment on the filtered fermentation liquor to obtain the hydrolyzed collagen product with surface amphipathicity. The hydrolyzed collagen product prepared by the invention not only has low molecular weight and high permeability to skin, but also has water locking and moistening effects on the skin surface due to the amphiphilic sophorolipid on the surface, so that the moisture retention of the skin is better improved, and the product has excellent product characteristics and has wide market prospects.

The invention belongs to the technical field of biology, and particularly relates to recombinant III-type humanized collagen as well as a preparation method and application thereof. On the basis of the III-type human collagen amino acid sequence, the amino acid sequence is designed by means of bioinformatics and the like, so that the recombinant collagen realizes higher expression efficiency and a triple helix structure on the premise of maintaining high biological activity, a section of brand new collagen sequence containing 180 amino acids is designed, the protein molecular weight is small, and the recombinant collagen has the advantages of high expression efficiency, high yield, high yield and the like. The skin permeability is better. Compared with a commercially available collagen product, the recombinant humanized collagen prepared by the technical scheme has better stability, cell proliferation and migration promotion effect and barrier repair capability, so that the recombinant humanized collagen has good practical application value.

The invention discloses an identification method of collagen. A reagent for identification is genipin. The method comprises the following identification steps: I, when the concentration of the collagen is higher than 0.05%, uniformly mixing the genipin solution with the collagen and / or the collagen product solution for reaction and color development, and directly comparing colors for identification; iI, when the concentration of the collagen is lower than 0.05%, after a collagen product solution is extracted, developing by using a genipin solution, and directly comparing colors for identification; and III, when the concentration of the collagen is lower than 0.05%, uniformly mixing the genipin solution and the collagen solution for reaction and color development, and directly comparing colors for identification. According to the identification method, the requirement for the range of the collagen content in collagen raw materials and products is wider, expensive equipment does not need to be used in the identification process, and the identification cost is greatly reduced; the operation process is convenient, the experiment period is short, the identification speed is high, the sensitivity is higher, the stability is good, and the collagen content identification efficiency is improved.

This invention relates to a recombinant type V collagen, its encoding gene, and its applications, belonging to the fields of genetic engineering and protein engineering technology. Based on the amino acid sequence of the α1 chain of human type V collagen, this invention utilizes bioinformatics and other methods to design the amino acid sequence, enabling the recombinant collagen to achieve higher expression efficiency and high stability while maintaining high biological activity. A novel collagen sequence containing 178 amino acids was designed. The nucleotide sequence of this recombinant collagen was optimized using E. coli codon preference to construct a high-expression recombinant strain. The recombinant collagen produced by fermentation of this strain contains no exogenous amino acids such as tags, making it a recombinant humanized type V collagen with good safety. Compared with commercially available type V collagen products, the recombinant type V collagen prepared using the above technical solution has better antioxidant activity and barrier repair capabilities, thus possessing good practical application value.

The invention belongs to the technical field of gene recombination, and particularly relates to a recombinant human III-type triple helix collagen, a recombinant yeast strain for expressing the recombinant human III-type triple helix collagen and a construction method of the recombinant human III-type triple helix collagen. The amino acid sequence of the recombinant human III-type triple-helix collagen is shown as SEQ ID NO. 1, and the recombinant human III-type triple-helix collagen has triple-helix conformation close to a natural biological structure of collagen and has good application value and potential. According to the recombinant yeast strain disclosed by the invention, human-derived III-type collagen and proline hydroxylase are co-expressed in yeast cells without YPS1 protease, and meanwhile, a gene beneficial to vesicle transport and protein folding is transferred, so that hydroxylation of the recombinant collagen can be realized, a natural triple helix conformation is formed, and the recombinant yeast strain can be used for preparing a recombinant collagen product. The degradation problem of the collagen in the expression process can be solved, and the extracellular secretion expression of the triple helix collagen is realized.

The utility model belongs to the technical field of collagen product outer packing, and particularly relates to a carton for collagen product outer packing, which comprises a box cover and a box body which are closed, a storage bin is arranged on one side, close to the box cover, of the box body, a storage piece is arranged in the storage bin, a plurality of storage areas are arranged on the storage piece in a dot matrix mode, and the box cover and the box body are arranged on the box body. A plurality of storage areas are formed in the box body, a collagen product body is inserted into each storage area, the top end of each collagen product body extends to the upper part of the box body, and the storage part comprises partition plates which are sequentially arranged at equal intervals from bottom to top. Therefore, the collagen product bodies are stored in the box body in a dot matrix mode, when the collagen product bodies are taken out, only one collagen product body needs to be pulled out from the top of the box body, the collagen products are conveniently and rapidly taken out, and meanwhile the occupied area of equipment is reduced.

The invention discloses a cross-linked recombinant collagen marker polypeptide and application thereof, and belongs to the technical field of collagen detection. The amino acid sequence of the cross-linked recombinant collagen marker polypeptide is GESGPAGPAGAPGPAGSR. The cross-linked recombinant collagen marker polypeptide has the advantages that the cross-linked recombinant collagen marker polypeptide can be used for The cross-linked recombinant collagen marker polypeptide provided by the invention has strong specificity. The cross-linked recombinant collagen enzymatic hydrolysate is taken as a standard substance, a marker polypeptide is taken as a detection target, and the provided detection method is simple to operate and high in sensitivity, and can be used for quantitative analysis of the cross-linked recombinant collagen; the method can be used for quality control of a crosslinked recombinant collagen product and residual quantity analysis and degradation process evaluation of the crosslinked recombinant collagen product in animal bodies. The cross-linked recombinant collagen marker polypeptide provided by the invention has uniqueness, and a qualitative and quantitative detection method established by taking the marker polypeptide as a marker and a quantitative standard substance has important significance on quality control of a cross-linked recombinant collagen product.

Currently available non-denatured collagen products include powders and capsules that can optionally be incorporated into a final product that does not require heating or acidic conditions, or instead is consumed directly. This has been particularly problematic for administration to non-human mammals, such as pets and livestock, because when added as a dry powder to food or water, the supplements and capsules sink to the bottom of the bowl of food or liquid and remain unconsumed by the mammal, or in the case of capsules, can be difficult, if not impossible, to administer to the mammal.SOLUTION: The present disclosure relates to processed animal foods and / or treats comprising undenatured type II collagen. The undenatured type II collagen is introduced into the animal food and / or treat prior to processing and at least 30% or more of the undenatured collagen remains undenatured after processing of the animal food and / or treat.SELECTED DRAWING: None

The present invention belongs to the technical field of natural active collagen, and specifically relates to a method for detecting the content of active collagen using self-assembly properties. The present invention utilizes the unique self-assembly properties of active collagen with a complete triple helical structure, induces the active collagen to self-assemble into collagen fibers using PBS buffer, and simultaneously uses trypsin to further enzymatically hydrolyze the denatured collagen into small molecules. The precipitated collagen fibers and the denatured polypeptide solution are then separated by ultrafiltration and centrifugation. By detecting the content of collagen in the precipitate, the content of active collagen in the collagen can be simply and quickly quantitatively analyzed. The detection method of the present invention can be used to detect the content of active collagen in various dosage forms of collagen products such as collagen solutions, dressings, sponges, powders, and gel preparations, and has a wide range of applications.

The invention discloses wood frog collagen capable of increasing skin elasticity and resisting aging and a preparation method of the wood frog collagen. The antioxidant wood frog skin collagen product comprises wood frog skin collagen peptide powder, astragalus polysaccharide, centella asiatica extract, sodium hyaluronate, lycium barbarum polysaccharide and green tea extract catechin. The collagen product is rich in various nutritional ingredients, has a relatively excellent antioxidant function, can be used for improving the barrier function of skin to external harmful substances, and can continuously improve the moisture and elasticity of the skin.

The application relates to the technical field of collagen products, and discloses a production method of enzyme-modified pigskin collagen products, which comprises the following steps: step one, pretreatment: after pigskin is cleaned, degreased and cut into pieces, the pigskin is stirred and treated in a composite degreasing agent solution, washed to neutral, and drained; step two, swelling treatment: the pigskin pieces after the pretreatment are placed in an organic acid solution and swelled at 0-15 DEG C for 4-48 hours. The production method of the enzyme-modified pigskin collagen products adopts composite biological enzymes for limited hydrolysis, avoids the damage of strong acid, strong alkali and high-temperature treatment to the triple helix structure of collagen, retains the natural biological activity, controls the molecular weight distribution of the product, significantly improves the water solubility, controls the function and has strong adaptability, different molecular weight sections and different functional characteristics of collagen products can be prepared through the regulation of enzyme types, enzymolysis time and pH value, and the production method meets the customized needs in the fields of daily chemicals, agricultural chemicals, food and the like.

The present application relates to a kind of recombinant human type III collagen and its preparation method and application, belong to the field of bioengineering technology.The amino acid sequence of the recombinant human type III collagen described in the present application is as shown in SEQ ID No.7, is through the directional arrangement of five characteristic triple helix domain and the expansion of polymerization, combined with high-density fermentation process of Pichia pastoris, successfully break through the technical barrier of 4.5g / L target protein concentration.The present application research shows that the recombinant protein at 0.5% concentration not only maintains more than 80% cell viability, more exhibits significant synergistic effect-promote fibroblast migration rate to increase more than 29% compared with blank control group, keratinocyte proliferation rate increases 40.62%, adhesion rate increases 6.53%, provides innovative solution for developing new collagen product with high-efficiency expression and multiple biological activities.

The invention discloses a liquid chromatography-mass spectrometry detection method for recombinant collagen in a collagen product. The detection method is based on liquid chromatography-mass spectrometry, is suitable for qualitative and quantitative detection of recombinant collagen in various collagen products, and is accurate and reliable in detection result. The detection method comprises a pretreatment step, an enzymolysis step, a liquid chromatography-mass spectrometry detection step and a detection result interpretation step. Wherein whether a peak consistent with the retention time of the characteristic polypeptide appears in a detection map of a test sample test solution or not is judged, and whether the test sample test solution contains the specific recombinant collagen or not is judged; and / or according to the proportional relation between the peak area of the peak of the characteristic polypeptide in the detection spectrum of the test sample test solution and the peak area of the peak of the characteristic polypeptide in the detection spectrum of the recombinant collagen raw material standard working solution sample or the characteristic polypeptide standard working solution sample, determining the characteristic polypeptide according to the peak area of the peak of the characteristic polypeptide in the detection spectrum of the recombinant collagen raw material standard working solution sample or the characteristic polypeptide standard working solution sample, and determining the content of the recombinant collagen in the test solution of the test sample.

The present application relates to the technical field of biomaterials and regenerative medicine, and particularly relates to a preparation method of a whole-fish-scale-based bone repair material, comprising the following steps: S1, fish scale fiber preparation: collected fish scales are washed and subjected to decellularization treatment, and then ground into fibrous form; S2, fish scale collagen adhesive preparation: collagen is extracted from the decellularized fish scales by using at least two different extraction methods, the obtained collagen products are mixed, freeze-dried, and then dissolved in deionized water to prepare collagen adhesives with different concentrations; S3, composite material preparation: the collagen adhesive prepared in step S2 is mixed with the fish scale fibers obtained in step S1, and then extruded into a shape; the whole-fish-scale-based bone tissue engineering material can be prepared by combining fish scale collagen and fish scale fibers, the material is not only safer and more reliable in composition, but also allows accurate regulation of the composition, thereby providing more innovative possibilities for the application of fish scale collagen adhesive.

The invention discloses an extraction and separation all-in-one machine and method for preparing collagen products for beauty, and relates to the technical field of extraction and separation.The extraction and separation all-in-one machine comprises a constant-temperature shell, a power rod is arranged in the middle of the upper end of the constant-temperature shell, and an electric push rod is arranged at the upper end of the power rod; and the bottom of the power rod is provided with an extraction mechanism for extracting collagen in the stock solution of the material. The liquid level in the constant-temperature shell is changed by the vertical reciprocating motion of the extraction pipe, so that the pressure of each layer of liquid level is also changed, the dynamic pressure change enables the filter membrane to filter under different hydraulic pressures, the filtering bottleneck under the single pressure condition is avoided, the page turning assembly and the turbulent flow assembly are prevented from extruding raw materials, and the extraction efficiency is improved. The pressure of each layer of liquid level in the constant-temperature shell is changed, and the continuous extrusion action not only contributes to breaking the concentration gradient in a solution, but also promotes the flowing of substances on the surface of a filter membrane, reduces the risk of blockage, and ensures a more thorough filtering effect.

The invention relates to the technical field of collagen-containing products, in particular to collagen membrane cloth as well as a preparation method and application thereof. The invention relates to collagen membrane cloth, which is prepared by taking modified collagen fibers as raw materials, opening, carding and lapping to prepare a fiber web, and then performing spunlace processing, the modified collagen fiber is prepared from a sea cucumber collagen-sea cucumber peptide-plant polyphenol covalent complex, and the plant polyphenol is one or a mixture of two of Chinese herbaceous peony polyphenol and chaenomeles speciosa polyphenol. According to the collagen membrane cloth, collagen is extracted from marine animal tissues, and the collagen membrane cloth has excellent antioxidant, antibacterial, anti-inflammatory and analgesic effects.

The invention belongs to the technical field of natural active collagen, and particularly relates to a method for detecting the content of active collagen by utilizing self-assembly performance. According to the preparation method, the specific self-assembly performance of active collagen with a complete triple-helix structure is utilized, the active collagen is induced to generate self-assembly through a PBS buffer solution to form collagenous fibers, and meanwhile, the denatured collagen is further subjected to enzymolysis into small molecules by using trypsin; then separating the precipitated collagenous fibers from the denatured polypeptide solution through ultrafiltration centrifugation, and simply and rapidly carrying out quantitative analysis on the content of active collagen in the collagen by detecting the content of collagen in the precipitate; the detection method can be used for detecting the content of active collagen in collagen products of various dosage forms such as collagen solutions, dressings, sponges, powder and gel preparations, and is wide in application range.

The invention belongs to the technical field of protein engineering and genetic engineering, and particularly relates to recombinant IV-type collagen as well as a preparation method and application thereof. According to the invention, three high-activity amino acid sequences are screened by taking a human-derived IV-type collagen alpha1 chain as a template, and the nucleotide sequences of the three amino acid sequences are optimized by pichia pastoris codon preference and then are respectively integrated onto a pichia pastoris genome to obtain three recombinant IV-type collagen engineering yeast strains; through shake-flask culture, two engineering yeast strains can be successfully fermented to prepare the recombinant IV type collagen, and are respectively named as IV1-2 and IV1-3. Compared with a commercially available collagen product, the recombinant IV-type collagen prepared by the technical scheme has better oxidation resistance and barrier repair capability, the effect of IV1-3 is better than that of IV1-2, and the recombinant IV-type collagen has good practical application value.

The invention discloses a lactic acid bacteria and yeast co-fermented collagen product, a preparation method and application thereof, the lactic acid bacteria and yeast co-fermented collagen product comprises soluble collagen peptide and metagen generated by lactic acid bacteria and yeast co-fermented collagen, the ratio of the soluble collagen peptide to the metagen is 1: (10-20), the lactic acid bacteria are Lactobacillus casei ZJU2303-RH07, the metagen is a soluble collagen peptide, the soluble collagen peptide is a soluble collagen peptide, the soluble collagen peptide is a soluble collagen peptide, the soluble collagen peptide is a soluble collagen peptide, the soluble collagen peptide is a soluble collagen peptide, the soluble collagen peptide is a soluble collagen peptide, and the soluble collagen peptide is a soluble collagen peptide. The saccharomycetes are saccharomyces cerevisiae ZJU2014-RH05, the preservation number of the saccharomycetes is CGMCC (China General Microbiological Culture Collection Center) 1.19346, the saccharomycetes are Saccharomyces cerevisiae ZJU2014-RH05, and the preservation number of the saccharomycetes is CGMCC 2.6673. The moisture-absorbing and moisture-preserving cosmetic has the advantages of being good in moisture-absorbing and moisture-preserving effect and low in production cost, and has wide market prospects in preparation of cosmetics with moisture-absorbing and moisture-preserving functions.

This invention relates to the fields of microbial fermentation and genetic engineering technology, specifically disclosing a method for preparing human type III collagen fragments. Based on Pichia pastoris, this invention constructs a multidimensional synergistic expression system of "molecular chaperone co-expression - precursor supply - osmotic pressure adaptation regulation," reducing the structural instability of collagen fragments during secretion and post-processing, and constructing an expression system suitable for stable and efficient secretion of collagen fragments. The method described in this invention can achieve efficient extracellular secretory expression of human type III collagen fragments, and the obtained protein has high structural uniformity and stability, with a protein yield of up to 6.55 g / L under 5 L fermenter conditions. The method described in this invention is suitable for the large-scale preparation of human type III collagen fragments and provides a new technical solution for obtaining collagen products with high structural uniformity and good functional activity.

The invention belongs to the technical field of microbial fermentation of collagen, and particularly relates to a microbial fermentation method of collagen. The gelatin is prepared by taking a biological collagen product as a substrate. The method is characterized in that bacillus stearothermophilus and an auxiliary agent are added to carry out fermentation treatment on the substrate in advance, and then enzymolysis is carried out. The main technical contribution of the method lies in providing the application of the bacillus stearothermophilus in collagen proteolysis, the fermentation enzyme activity of the bacillus stearothermophilus is effectively improved by adding auxiliaries, and the prepared gelatin product has good uniformity.

The invention belongs to the technical field of genetic engineering, and particularly provides a recombinant human-like collagen polypeptide and a preparation method and application thereof, the recombinant human-like collagen polypeptide comprises an N-terminal tandem repeat sequence and a C-terminal sequence; the repetitive sequence is as shown in SEQ ID NO. 1; 1, and the C-terminal sequence is as shown in SEQ ID NO. 2. The recombinant human-like collagen polypeptide provided by the invention can correctly express active collagen with a triple helix structure in a prokaryotic expression system, so that the production cost of the active human collagen is greatly reduced, and the production efficiency is improved; compared with natural human I-type collagen, the prepared recombinant human-like collagen polypeptide has better water retention capacity and degradation resistance, and shows a cell migration promoting effect superior to that of a commercially available collagen product in a cell scratch experiment.

The invention relates to the technical field of biological materials and regenerative medicine, in particular to a preparation method of a full-fish-scale-based bone repair material, which comprises the following steps: S1, fish scale fiber preparation: cleaning and decellularizing collected fish scales, and grinding the fish scales into fibers; s2, preparing a fish scale collagen adhesive: extracting collagen from the decellularized fish scales by adopting at least two different extraction methods, mixing the obtained collagen products, freeze-drying, and dissolving in deionized water to prepare collagen adhesives with different concentrations; s3, preparing a composite material: mixing the collagen adhesive prepared in the step S2 with the fish scale fibers obtained in the step S1, and performing extrusion forming; according to the invention, the fish scale collagen is combined with the fish scale fiber, so that the full-fish scale bone tissue engineering material can be prepared, and the material is safer and more reliable in components and allows accurate regulation and control of the components, thereby providing more innovation possibilities for application of the fish scale collagen adhesive.