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Updated: Feb 14, 2026

An Improved Method for the Preparation of Type I Collagen From Skin
Published on: January 21, 2014
Enzymatic Production of Collagen Oligopeptides from Porcine Skin and Their Structure-Activity Relationships in
Ying-Yan Liang1, Hua-Bin Jiang1,2, Sun-Qiang Xu1
1Key Laboratory of Energy Plants Resource and Utilization, Ministry of Agriculture and Rural Affairs, Guangdong Engineering Technology Research Center for Agricultural and Forestry Biomass, College of Future Biomass, South China Agricultural University, Guangzhou 510642, China.
Abstract:
Collagen-derived peptides are widely studied for their potential roles in skin health and anti-aging. This study applied response surface methodology to optimize the enzymatic hydrolysis of porcine skin-derived collagen oligopeptides (PCOPs) and investigate the associations between peptide characteristics and their cellular effects. The optimized hydrolysis conditions were a solid-to-liquid ratio of 1:2, 52.3 °C, 0.9% enzyme dosage, and pH 7.0. The resulting PCOPs contained 85.77% peptides with molecular weight < 1000 daltons (Da) and 9.68% hydroxyproline. In vitro, 5 mg/mL PCOPs reduced hydrogen peroxide (H2O2)-induced fibroblast senescence by 39.66% and significantly (p < 0.05) reduced tyrosinase activity and melanin synthesis in melanoma cells (B16). Peptidomic profiling identified 52 peptides mainly derived from type I collagen, enriched in Pro-Gly motifs. Circular dichroism analysis indicated that PCOPs primarily consisted of β-sheets (35.3%) and random coils (38.9%). These results suggest that low molecular weight, high hydroxyproline content, Pro-Gly-enriched peptides, and the predominance of β-sheet/random coil structures are associated with the observed cellular effects on fibroblast function and melanogenesis.
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