27 results about "Collagen product" patented technology

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.

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 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 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 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.

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.

FIELD: pharmaceuticals.SUBSTANCE: relates to a formulation in the form of capsules for oral administration, for immediate release of a native collagen product. A formulation in the form of capsules for oral administration, for immediate release of a native collagen product, which is a gelatin capsule containing a central part, the central part contains a native collagen product from fish skins, ascorbic acid and an anti-caking component – calcium stearate, wt.%: native collagen product 83.08, ascorbic acid 14.96, calcium stearate 1.96.EFFECT: intended for oral administration for immediate release of the native collagen product.1 cl

The application relates to the cosmetic technical field, in particular to a retinol microcapsule condensation pearl anti-wrinkle firming triple collagen essence cream and a preparation method thereof. The essence cream provided in the application realizes the balance of retinol slow release stability, mild low stimulation, whole-layer collagen activation and barrier repair performance, and avoids the problems of easy oxidation failure of existing retinol skin care products, relatively high irritability of raw materials, weak transdermal absorption of ordinary collagen products, single anti-aging dimension of single active ingredient, low purification efficiency and insufficient activity of conventional plant extracts. The essence cream provided in the application can be used for facial skin anti-wrinkle firming and daily barrier repair and maintenance, and is suitable for the use requirements of long-acting anti-aging, mild stability maintenance and multi-dimensional skin repair of mature skin and sensitive skin.

A process for the production of a soluble collagen product and an insoluble collagen product from mammalian dermis tissue is described. The tissue may initially be processed to remove the epidermis and adipose tissue and then minced into small pieces. The process includes washing the minced dermis in an enzymatic solution, such as an amylase solution followed by homogenizing the amylased tissue. The soluble and insoluble collagen is then extracted from the homogenized tissue and subsequently separated into distinct soluble and insoluble fractions. The process produces collagen with high Dalton values that can subsequently be combined to produce a mixed composite collagen product. Also, the extracted collagen may be used as an integral composite collagen before separation.

This invention belongs to the field of biotechnology, specifically relating to a recombinant type III humanized collagen, its preparation method, and its uses. Based on the amino acid sequence of type III human collagen, this invention utilizes bioinformatics and other methods to design the amino acid sequence, enabling the recombinant collagen to achieve higher expression efficiency and a triple helix structure while maintaining high biological activity. A novel collagen sequence containing 180 amino acids was designed, resulting in a small molecular weight and better skin penetration. Compared with commercially available collagen products, the recombinant humanized collagen prepared using the above technical solution exhibits better stability, cell proliferation and migration promotion, and barrier repair capabilities, thus possessing significant practical application value.

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

The application belongs to the technical field of bioengineering, and particularly relates to a recombinant humanized collagen III and a coding gene and application thereof. The application adopts advanced AI technology and molecular dynamics simulation to design a new humanized collagen III sequence, so as to ensure that the recombinant humanized collagen III product has high stability and anti-degradation. The new humanized collagen III sequence screened is transferred to a Pichia pastoris strain for recombinant expression, and the prepared recombinant humanized collagen III has the advantages of high stability, high expression and good hydrophilicity. In addition, the recombinant humanized collagen III also has the effects of promoting cell proliferation and cell adhesion.

This invention relates to a recombinant human type XVII collagen, its preparation method, and its applications, belonging to the field of bioengineering technology. The amino acid sequence of the recombinant human type XVII collagen is shown in SEQ ID No. 4. It is formed by constructing recombinant monomers through the directional arrangement of two characteristic triple-helix domains, and then further formed by the tandem connection of eight monomer units. The collagen retains its natural active sites while enhancing its mechanical strength. Combined with high-density fermentation technology using Pichia pastoris, high-expression, high-purity recombinant collagen was successfully obtained. This recombinant protein not only maintains over 85% cell viability at a concentration of 0.5%, but also exhibits multiple biological activities—promoting fibroblast migration rate by over 57%, keratinocyte proliferation rate by 20.97%, and showing significant hair growth effects. This invention provides an innovative solution for developing novel collagen products with both high-efficiency expression and multiple biological activities.

A process for the production of a soluble collagen product and an insoluble collagen product from mammalian dermis tissue is described. The tissue may initially be processed to remove the epidermis and adipose tissue and then minced into small pieces. The process includes washing the minced dermis in an enzymatic solution, such as an amylase solution followed by homogenizing the amylased tissue. The soluble and insoluble collagen is then extracted from the homogenized tissue and subsequently separated into distinct soluble and insoluble fractions. The process produces collagen with high Dalton values that can subsequently be combined to produce a mixed composite collagen product. Also, the extracted collagen may be used as an integral composite collagen before separation.

A method of producing a multifilament collagen fiber bundle involves treating a multifilament support polymer-collagen fiber bundle containing a plurality of collagen monofilaments supported on a support polymer to remove the support polymer from the multifilament support polymer-collagen fiber bundle using a series of liquid media containing a decreasing concentration of the support polymer. The support polymer is more soluble than collagen in a liquid medium, and the gradual removal of the support polymer provides sufficient time for collagen molecules to self-assemble to form fibrils. The resulting multifilament collagen fiber bundle has a D-band structure similar to native collagen, but is offset by 1 / 6 D-band. The multifilament collagen fiber bundle can be cross-linked through ultraviolet rays under the condition of no photoinitiator to form a cross-linked collagen product with excellent tensile strength and Young modulus, and the product is suitable for collagen-based biological materials in the field of tissue repair and regeneration.

This invention provides recombinant humanized collagen, comprising a recombinant humanized type I collagen α1 chain fragment or recombinant humanized type III collagen, wherein the amino acid fragment of the recombinant humanized type I collagen α1 chain fragment is shown in SEQ ID NO: 1; or, the amino acid fragment of the recombinant humanized type III collagen is shown in SEQ ID NO: 2. A method for preparing the recombinant humanized collagen is also disclosed. The preparation process of the method provided by this invention is optimized, particularly by employing a feed strategy during the glycerol-to-methanol transition period to improve protein yield. This invention, through the screening of truncated fragments of recombinant humanized collagen and the optimization of the preparation process, obtains a high-yield, high-purity, and low-endotoxin recombinant humanized collagen product.

The present disclosure provides a cost-effective method for extracting fish scale collagen having a large molecular weight, pertaining to the technical field of fish scale collagen. The present disclosure includes: 1) performing pretreatment, including: repeatedly subjecting fish scales to frozen storage and thawing; 2) performing impurity protein removal, including: removing fish silver from the pretreated fish scales; and soaking the fish scales in sodium chloride solution, followed by cleaning and drying; 3) performing fish scale collagen extraction, including: mixing the dried fish scales with purified water according to a ratio of 1:5 to 1:20, subjecting the mixture to hydrothermal extraction at 40° C. to 100° C. for 1 to 4 hours, performing solid-liquid separation, and collecting the solution as a fish scale collagen extract; and 4) lyophilizing the fish scale collagen extract to obtain a solid fish scale collagen product.

The invention relates to recombinant human XVII type collagen as well as a preparation method and application thereof, and belongs to the technical field of bioengineering. The amino acid sequence of the recombinant human XVII type collagen is shown as SEQ ID No.4, and the recombinant human XVII type collagen is formed by constructing a recombinant monomer through directional arrangement of two characteristic triple helical structural domains and further connecting eight monomer units end to end in series; the collagen not only retains natural active sites, but also enhances the mechanical strength. And the recombinant collagen with high expression quantity and high purity is successfully obtained by combining a pichia pastoris high-density fermentation technology. The recombinant protein not only keeps more than 85% of cell activity at the concentration of 0.5%, but also shows multiple biological activities, the fibroblast migration rate is promoted to be improved by over 57%, the keratinocyte proliferation improvement rate is 20.97%, and the recombinant protein has a remarkable hair growth effect; the invention provides an innovative solution for developing a novel collagen product with efficient expression and multiple biological activities.

The invention relates to recombinant human III-type collagen as well as a preparation method and application thereof, and belongs to the technical field of bioengineering. The amino acid sequence of the recombinant human III-type collagen is shown as SEQ ID No.7, and the technical barrier of 4.5 g / L target protein concentration is successfully broken through by directional arrangement and multimerization expansion of five characteristic triple helical structural domains in combination with a pichia pastoris high-density fermentation process. Researches show that the recombinant protein not only keeps more than 80% of cell activity at the concentration of 0.5%, but also shows remarkable synergistic effects, namely promoting the migration rate of fibroblasts to be increased by more than 29% compared with a blank control group, increasing the proliferation rate of keratinocytes by 40.62%, increasing the adhesion rate by 6.53% and increasing the survival rate of the keratinocytes. An innovative solution is provided for developing a novel collagen product with efficient expression and multiple biological activities.

The invention relates to the technical field of collagen extraction, in particular to an extraction method of pigskin collagen, which comprises the following steps: selecting fresh back pigskin, retaining a corium layer, cutting into slices, rinsing with deionized water for multiple times, air-drying surface moisture, and performing vacuum freeze drying. The method comprises the following steps: crushing pig skin, performing supercritical extraction on the crushed pig skin to remove related cell impurities, further crushing pig dermis powder, performing irradiation sterilization to obtain pretreated powder, adding the pretreated powder into an immobilized pepsin solution for hydrolysis, and after the reaction is finished, removing immobilized enzyme and enzymolysis residues by centrifugation to obtain an enzymolysis product; the method comprises the following steps: taking pigskin as a raw material, diluting with acetic acid, transferring to a dialysis bag, continuously dialyzing for multiple times in deionized water to obtain a pigskin collagen solution, and then carrying out vacuum freeze-drying preservation, the method utilizes the easily available pigskin as the raw material, is low in cost, avoids toxic and volatile organic solvents, strong acids and strong alkalis in the extraction process, and can obtain a high-purity collagen product.

The recombinant humanized collagen provided by the invention comprises a recombinant humanized I-type collagen alpha1 chain fragment or a recombinant humanized III-type collagen, and the amino acid fragment of the recombinant humanized I-type collagen alpha1 chain fragment is as shown in SEQ ID NO: 1; or the amino acid fragment of the recombinant humanized III-type collagen is as shown in SEQ ID NO: 2. The invention also discloses a preparation method of the recombinant humanized collagen, a preparation process is optimized in the preparation method provided by the invention, and particularly, a glycerol-to-methanol transition switching period material supplementing strategy is adopted for material supplementing, so that the yield of the protein is improved. The recombinant humanized collagen product with high yield, high purity and low endotoxin is obtained by screening the truncated fragments of the recombinant humanized collagen and optimizing the preparation process.