10 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 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 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.

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.

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.

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.

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.