# Pigskin Collagen-Derived Antifreeze Peptides as Clean-Label Cryoprotectants: Inhibition of Ice Recrystallization and Suppression of Oxidative Deterioration in Heme-Rich Pork Sausages

**Authors:** Wentao Xuan, Huiqin Wang, Guanzhen Gao, Jianwu Zhou, Xiaomei Xie, Zhixin Lin, Qiren Chen, Yixin Chen, Qiuhui Zeng, Daohuang Xu, Pingfan Rao, Leiwen Xiang

PMC · DOI: 10.3390/foods15050925 · Foods · 2026-03-06

## TL;DR

This study shows that antifreeze peptides from pigskin collagen can protect frozen pork sausages by reducing ice damage and slowing down spoilage.

## Contribution

The novel use of pigskin collagen-derived peptides as clean-label cryoprotectants in heme-rich meat products is demonstrated.

## Key findings

- APPs reduced thawing and cooking losses in pork sausages compared to controls and commercial phosphates.
- APPs stabilized water structure in sausages, limiting free water formation and preserving texture.
- APPs suppressed oxidative damage by maintaining protein integrity in heme-rich meat.

## Abstract

Frozen red meat products face dual challenges: structural damage from ice recrystallization and subsequent oxidative deterioration driven by endogenous pro-oxidants in heme-rich matrices. This study investigated the efficacy of pigskin collagen-derived antifreeze peptides (APPs) as clean-label cryoprotectants in pork sausages. In vitro characterization confirmed distinct thermal hysteresis (0.51 °C) and potent ice recrystallization inhibition. In the sausage system, 6% APPs overcame ionic screening effects, reducing thawing loss to 4.87% (vs. 7.51% in control) and cooking loss to 14.59%, significantly outperforming commercial phosphates in moisture retention. Low-field NMR revealed that APPs stabilized the actomyosin hydration shell, maintaining the immobilized water proportion (P21) at 93.67% (vs. 88.50% in control) and inhibiting conversion of immobilized water into free water. Furthermore, APPs suppressed oxidative deterioration, limiting protein carbonyl content to 3.08 nmol/mg (vs. 3.71 nmol/mg in control), supporting a “physical–chemical cascade” mechanism whereby superior microstructural preservation mitigates downstream oxidative deterioration. Despite a trade-off in textural resilience (0.37 vs. 0.44), APPs function as specialized “Ice-Structure Stabilizers” offering a robust clean-label strategy for preserving heme-rich meat products.

## Linked entities

- **Proteins:** Act5C (Actin 5C)
- **Chemicals:** phosphates (PubChem CID 1061)

## Full-text entities

- **Chemicals:** water (MESH:D014867), Heme (MESH:D006418), Ice (MESH:D007053), phosphates (MESH:D010710)

## Full text

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## Figures

5 figures with captions in the complete paper: https://tomesphere.com/paper/PMC12985152/full.md

## References

43 references — full list in the complete paper: https://tomesphere.com/paper/PMC12985152/full.md

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Source: https://tomesphere.com/paper/PMC12985152