# Modification of Muscle Proteins Induced by Novel Non-Thermal Processing: Theory, Characterization, and Consequences

**Authors:** Yulong Bao, Hao Gou, Wanjun Xu, Longteng Zhang, Yuemei Zhang, Hui Hong, Yi-Ming Zhao

PMC · DOI: 10.3390/foods15050963 · Foods · 2026-03-09

## TL;DR

This review explores how non-thermal processing methods affect muscle proteins in meat and aquatic products, focusing on recent advances and their implications.

## Contribution

The paper provides a comprehensive and up-to-date review of non-thermal processing effects on muscle proteins, emphasizing recent literature.

## Key findings

- Non-thermal processing modifies muscle proteins through oxidation, charge changes, and cross-linking.
- Recent studies highlight the use of advanced characterization methods to analyze these modifications.
- The review outlines how these changes impact meat quality and functional properties.

## Abstract

Muscle-protein modification plays a critical role in determining the quality, functional properties, and nutritional value of meat and aquatic products. Over recent decades, non-thermal processing technologies including irradiation, cold plasma, high-pressure processing, ultrasound, and electromagnetic fields have been widely explored in muscle foods. This review aims to critically examine modifications of food proteins subjected to non-thermal processing, with a focus on literature within the last five years. The review first introduces the type and theory of physicochemical modifications of food proteins, which includes protein oxidation, changes in net charge, cross-linking and aggregation. Subsequently, characterization methods applicable to food proteins are briefly discussed. Finally, the effects of non-thermal processing on muscle proteins are thoroughly discussed. This review will elucidate the intricate mechanisms of protein modification in muscle-based products, providing a theoretical framework to drive the advancement of innovative non-thermal processing technologies.

## Full text

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## Figures

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## References

156 references — full list in the complete paper: https://tomesphere.com/paper/PMC12985131/full.md

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Source: https://tomesphere.com/paper/PMC12985131