Identification of protein markers of muscle fibre type and ageing progress in beef cutaneous trunci and masseter

This study aimed to identify protein markers for fibre type, and extent of post-mortem proteolysis, in bovine cutaneous trunci and masseter, which represent very different muscles types. We applied mass-spectrometry-based proteomic techniques to analysis of muscle fibre type and, examined temporal proteolysis changes with post-mortem ageing. Global proteomic analysis was performed on fresh beef masseter (high type-I fibres) and cutaneous trunci (high type-II fibres). The profile of semi-tryptic peptides, before and after ageing, was analysed to quantify protein degradation extent. Progression of proteolysis in type-I and type-II muscles was indicated by semi-tryptic peptides derived from heat-shock-protein 27, and troponin T fast skeletal muscle, respectively. The content of type I fibres in beef could be estimated using the abundance of myosin light chain-3, and enzymes involved in glycolysis could indicate the content of type-II fibres. These markers could be used in the supply chain to monitor and improve beef quality.

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Publication Details

Journal
Food Chemistry
Published
2025-12-25
DOI
https://doi.org/10.1016/j.foodchem.2025.147747
Primary Topic
Meat and Animal Product Quality
Type
article
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article

Identification of protein markers of muscle fibre type and ageing progress in beef cutaneous trunci and masseter

Robyn Dorothy Warner, Melindee Hastie, Michael G. Leeming, Zhenzhao Li
Food Chemistry
Meat and Animal Product Quality
article

Identification of protein markers of muscle fibre type and ageing progress in beef cutaneous trunci and masseter

Robyn Dorothy Warner, Melindee Hastie, Michael G. Leeming, Zhenzhao Li
article en

Abstract

This study aimed to identify protein markers for fibre type, and extent of post-mortem proteolysis, in bovine cutaneous trunci and masseter, which represent very different muscles types. We applied mass-spectrometry-based proteomic techniques to analysis of muscle fibre type and, examined temporal proteolysis changes with post-mortem ageing. Global proteomic analysis was performed on fresh beef masseter (high type-I fibres) and cutaneous trunci (high type-II fibres). The profile of semi-tryptic peptides, before and after ageing, was analysed to quantify protein degradation extent. Progression of proteolysis in type-I and type-II muscles was indicated by semi-tryptic peptides derived from heat-shock-protein 27, and troponin T fast skeletal muscle, respectively. The content of type I fibres in beef could be estimated using the abundance of myosin light chain-3, and enzymes involved in glycolysis could indicate the content of type-II fibres. These markers could be used in the supply chain to monitor and improve beef quality.

Food ChemistryVol. 503
The University of Melbourne (AU)
Openalex Percentile: Top 36%
Meat and Animal Product Quality
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