# Enzymatic Production of Collagen Oligopeptides from Porcine Skin and Their Structure–Activity Relationships in Anti-Aging and Skin-Whitening Effect

**Authors:** Ying-Yan Liang, Hua-Bin Jiang, Sun-Qiang Xu, Li Chen, Zhuo-Han Cai, Xia Wang, Gui-Can Bi, Jun Xie

PMC · DOI: 10.3390/foods15030507 · Foods · 2026-02-01

## TL;DR

This study explores how collagen peptides from pig skin can help reduce skin aging and darkening by optimizing their production and analyzing their structure and effects.

## Contribution

The study introduces optimized enzymatic conditions for producing collagen oligopeptides with specific structural features linked to anti-aging and skin-whitening effects.

## Key findings

- Optimized hydrolysis produced peptides with 85.77% <1000 Da and 9.68% hydroxyproline.
- PCOPs reduced fibroblast senescence by 39.66% and inhibited melanin synthesis in B16 cells.
- Peptides were mainly from type I collagen, enriched in Pro-Gly motifs and β-sheet structures.

## 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.

## Linked entities

- **Proteins:** COL3A1 (collagen type III alpha 1 chain), LOC103429692 (polyphenol oxidase, chloroplastic-like)
- **Chemicals:** hydrogen peroxide (PubChem CID 784), hydroxyproline (PubChem CID 5810)

## Full-text entities

- **Genes:** TYR (tyrosinase) [NCBI Gene 7299] {aka ATN, CMM8, OCA1, OCA1A, OCAIA, SHEP3}
- **Diseases:** melanoma (MESH:D008545)
- **Chemicals:** melanin (MESH:D008543), Collagen Oligopeptides (-), Gly (MESH:D005998), H2O2 (MESH:D006861), Pro (MESH:D011392), hydroxyproline (MESH:D006909)

## Full text

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## Figures

7 figures with captions in the complete paper: https://tomesphere.com/paper/PMC12896989/full.md

## References

50 references — full list in the complete paper: https://tomesphere.com/paper/PMC12896989/full.md

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Source: https://tomesphere.com/paper/PMC12896989