Collagen structure, and method for producing collagen structure

A collagen and manufacturing method technology, applied in the direction of peptide/protein components, skin care preparations, medical preparations containing active ingredients, etc., can solve the problem of insufficient improvement of gel thermal stability, poor thermal stability, and gel strength Insufficient and other problems, to achieve excellent mechanical strength, avoid deterioration, and excellent thermal stability

Active Publication Date: 2014-11-12
株式会社日皮
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  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

Collagen gel is effective as a cell carrier, medical material, etc., but its thermal stability is poor, and the gel strength may not be sufficient
In the existing cross-linking method of contacting the protein cross-linking agent with the collagen gel, the cross-linking is performed on the surface of the collagen fibers, and the cross-linking agent does not penetrate into the center of the gel, so the thermal stability of the gel not fully improved

Method used

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  • Collagen structure, and method for producing collagen structure
  • Collagen structure, and method for producing collagen structure
  • Collagen structure, and method for producing collagen structure

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0124] (1) Modulation of collagen structure

[0125] The dermis of pigskin is minced with a meat grinder, degreased and washed thoroughly, and the resulting tissue is used as a raw material. Suspend the raw material in an aqueous solubilization solution mixed with pepsin at a final concentration of 5 mg / ml and acetic acid at 50 mM, so that the final concentration of collagen reaches 4.5 (w / v) %, and solubilize overnight at 4° C. deal with. Sodium chloride was added to the enzyme-solubilized collagen solution obtained as above to make the final concentration 5 (w / v)%, salting out was carried out, and the salted out product was recovered by centrifugation. The recovered salted-out product was dispersed in distilled water to make the collagen concentration reach 3 (w / v)%, and hydrochloric acid was added to adjust the pH to 3.0, and dissolved uniformly to form a collagen solution.

[0126] To 2.5 ml of this collagen solution (at 4°C), 47.5 ml of phosphate-buffered saline (pH 7.5...

Embodiment 2

[0156](1) Modulation of collagen structure

[0157] The dermis of pigskin is minced with a meat grinder, degreased and washed thoroughly, and the resulting tissue is used as a raw material. Suspend the raw material in an aqueous solubilization solution mixed with pepsin at a final concentration of 5 mg / ml and acetic acid at 50 mM, so that the final concentration of collagen reaches 4.5 (w / v) %, and solubilize overnight at 4° C. deal with. Sodium chloride was added to the enzyme-solubilized collagen solution obtained as above to make the final concentration 5 (w / v)%, salting out was carried out, and the salted out product was recovered by centrifugation. The recovered salted-out product was dispersed in distilled water to make the collagen concentration reach 3 (w / v)%, and hydrochloric acid was added to adjust the pH to 3.0, and dissolved uniformly to prepare a collagen solution. To 5 ml of this collagen solution (at 4° C.), 95 ml of phosphate-buffered saline (pH 7.5) at 4° C...

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Abstract

Provided is a collagen structure characterized by: comprising collagen fibers of 1 to 5 µm in average diameter; and has a water content of 0 to 15 (w / w)% and a collagen density of 50 to 800 mg / cm 3 . After generating collagen fibers by neutralizing an acidic collagen solution, the resulting solution is subjected to filtration or the like to form crude collagen fibers having a collagen concentration of 12 to 50 (w / v)%. The thus obtained crude collagen fibers are molded into a prescribed shape and then dried, thereby the collagen structure can be produced. Since the collagen structure is produced using, as raw material, collagen fibers that are formed by association of collagen molecules, the collagen structure has excellent cell infiltration property. Further, since the collagen density of the collagen structure is equivalent to that of in vivo collagen tissue, the collagen structure exhibits excellent tissue regeneration capacity when filled into a defective part in vivo. Therefore, the collagen structure can be preferably used as an artificial material for regenerative medicine and the like.

Description

technical field [0001] The present invention relates to a collagen structure including collagen fibers, and a method for producing the collagen structure. Background technique [0002] Collagen is a main protein that forms raw hides, tendons, bones, etc. of fish, pigs, and cattle. Since collagen has high homology among animals, it has low antigenicity, excellent body affinity and tissue adaptability, and has excellent characteristics as a raw material for medical materials. In the case of any abnormality in the body tissue, as an artificial material that can stably supply the transplanted tissue and avoid immune rejection, various components using collagen as a raw material are being developed. [0003] For example, there is a cell-invasive medical material in which denatured collagen having a helical structure content of 0 to 80% is bound or coated on a carrier made of synthetic resin or the like (Patent Document 1). Although collagen has excellent tissue affinity, collag...

Claims

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Application Information

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Patent Type & Authority Applications(China)
IPC IPC(8): A61L27/00A61K8/64A61K38/17A61P7/04A61P17/02A61P19/02A61P35/00A61P37/02A61P43/00
CPCA61L2300/418A61L2300/42A61L2300/414A61K8/65A61K2800/91A61Q19/08A61L27/24A61K8/027A61K2800/412A61K47/42A61K9/7007Y10T428/298A61P17/02A61P19/02A61P27/02A61P35/00A61P37/02A61P43/00A61P7/04A61L31/044A61L31/14A61L2300/80
Inventor 小仓孝之田中启友大场康弘服部俊治
Owner 株式会社日皮
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