Food and Fermentation Industries >

2025 , Vol. 51 >Issue 23: 227 - 234

DOI: https://doi.org/10.13995/j.cnki.11-1802/ts.042303

Separation, purification, and structure-activity relationship analysis of tyrosinase inhibitory peptides derived from yak bone collagen protein

  • LI Xuan ,
  • XIE Sha ,
  • LU Haili ,
  • FENG Yaowen ,
  • TANG Lijun ,
  • SUN Dong ,
  • HAO Gang
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  • 1(College of Food and Biotechnology, Sichuan Vocational and Technical College, Suining 629000, China)
    2(College of Pharmacy and Food, Southwest Minzu University, Chengdu 610041, China)

Received date: 2025-02-06

  Revised date: 2025-04-02

  Online published: 2025-12-25

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Abstract

In this study, yak bone collagen was used as the raw material to prepare collagen peptides with tyrosinase inhibitory activity (YBCP).Using tyrosinase inhibition rate (TIA) as the primary indicator, the collagen polypeptides were separated and purified through ultrafiltration, DA201 macroporous adsorption resin, Sephadex G-50, and G-15 gel chromatography, followed by analysis of their structure-activity relationships.The results showed that the fraction <3 kDa (F3) obtained via ultrafiltration exhibited relatively higher TIA.After further purification of F3 using DA201 macroporous adsorption resin, the resulting fraction (peak 1) showed only a 2.50% increase in inhibition rate compared to the unpurified F3.Subsequent purification of F3 via Sephadex G-50 coupled with G-15 yielded a highly active component, YBCP-2-2, which achieved a TIA of 49.07% at a concentration of 10 mg/mL.Amino acid composition analysis revealed that YBCP-2-2 contained a high proportion of antioxidant amino acids (63.45% of total protein), and the content of tyrosinase inhibitory (TI) activity-related amino acids significantly increased to 44.40% compared to YBCP.These amino acids were found to enhance the TIA of the collagen peptides.Additionally, 75.54% of YBCP-2-2 consisted of low-molecular-mass components (<500 Da, corresponding to 2-4 peptides), indicating a strong correlation between TIA and the molecular mass distribution of the collagen peptides.

Key words： collagen peptide; isolation and purification; tyrosinase inhibition; dextran gel

Cite this article

LI Xuan , XIE Sha , LU Haili , FENG Yaowen , TANG Lijun , SUN Dong , HAO Gang . Separation, purification, and structure-activity relationship analysis of tyrosinase inhibitory peptides derived from yak bone collagen protein[J]. Food and Fermentation Industries, 2025 , 51(23) : 227 -234 . DOI: 10.13995/j.cnki.11-1802/ts.042303

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