Collagen peptides and methods of making, conditioning agents, cosmetics

By using lipase and alkaline protease combined with sodium alginate and carboxymethyl chitosan to form a "microcell" structure during the collagen peptide extraction process, the problem of low active peptide content in traditional methods is solved, and highly active peptides are prepared efficiently, which are suitable for conditioning agents and cosmetics.

CN122303361APending Publication Date: 2026-06-30BEIJING QINGYAN BOSHI HEALTH MANAGEMENT CO LTD

Patent Information

Authority / Receiving Office
CN · China
Patent Type
Applications(China)
Current Assignee / Owner
BEIJING QINGYAN BOSHI HEALTH MANAGEMENT CO LTD
Filing Date
2026-04-27
Publication Date
2026-06-30

AI Technical Summary

Technical Problem

Traditional collagen peptide extraction processes often result in low activity, wide molecular weight distribution, and low content of active peptides, leading to cumbersome, inefficient, and costly post-processing, making them unsuitable for industrial production.

Method used

Animal-derived tissues are treated with lipase and alkaline protease, and combined with sodium alginate and carboxymethyl chitosan to form a "micro-cell" structure. The enzymatic hydrolysate is encapsulated by charge interaction, achieving a highly efficient and stable enzymatic hydrolysis process and increasing the content of active peptides.

Benefits of technology

This method increases the content of active peptides in collagen peptides and improves enzymatic hydrolysis efficiency, resulting in the preparation of high-content active peptides suitable for conditioning agents and cosmetics, with excellent efficacy.

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Abstract

This invention discloses a collagen peptide and its preparation method, as well as conditioning agents and cosmetics. The method involves sequentially treating animal-derived tissue with lipase and alkaline protease. During alkaline protease treatment, sodium alginate and carboxymethyl chitosan in a mass ratio of (0.1-0.3):(0.05-0.1) are added to the system to form a "micro-compartment" further encapsulating the enzymatic hydrolysate for continued hydrolysis. Then, enzyme inactivation and solid-liquid separation are performed, and the clear liquid is collected and freeze-dried to prepare the collagen peptide. This preparation method efficiently extracts collagen peptides with high dipeptide content from animal-derived tissues, thereby improving the cell proliferation and migration activity of the collagen peptides. It has excellent barrier repair activity and can be widely used in conditioning agents and cosmetics.
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