44 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 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 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.

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 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.

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.

The present invention discloses a low-molecular-weight, high-antioxidant-activity fish maw collagen peptide, its preparation method, and application, belonging to the technical field of functional product development. The present invention prepares a fish maw collagen peptide by using ultrasound, microwave, or high hydrostatic pressure-assisted enzymatic hydrolysis, wherein the peptide content with a relative molecular mass between 70 and 500 Da is 72.47% to 77.78%, the hydrophobic amino acid content is 37.30% to 38.66%, the GL content is 0.03 to 0.65 g / 100 g, and the GPA content is 0.6 to 1.8 g / 100. It has strong antioxidant activity and has the effect of enhancing immunity. In addition, it has the advantages of a simple process flow, low cost, mild reaction conditions, and environmental friendliness. The present invention can provide solid theoretical support for improving the economic value of fish by-products, increasing the utilization rate of fish maw collagen products, rationally utilizing resources, and developing new health care and skin care products.

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 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 present application provides a product quality testing method, which relates to the field of product quality testing technology, including: the product life chain of interactive collagen products; combined process and result testing, and the construction of a dual-drive test module; monitoring and returning product data streams, triggering dynamic testing, and performing phased data stream off-axis analysis and evaluation to determine the first test matrix, triggering static testing, performing component content analysis and molecular texture analysis, and predicting denaturation thresholds to determine the second test matrix; performing homology mapping verification on the first test matrix and the second test matrix to generate a product quality test sheet. This application can solve the technical problem in the prior art that the existing collagen product quality testing method cannot comprehensively evaluate the dynamic and static characteristics of the product, resulting in inaccurate product quality test results. By constructing a dual-drive test module, the quality of the collagen product can be comprehensively evaluated, and the accuracy of the product quality test results can be improved.

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.