Myofibrillar Protein Gelation and Oxidative Stability
Summary
Myofibrillar proteins, chiefly myosin and actin, underpin the texture and functional properties of muscle-derived foods through their capacity to form heat-set gels. Upon heating, these proteins unfold and interact via hydrophobic domains, electrostatic attraction and disulfide bonds to assemble a three-dimensional network that traps water and fat. This gelation process governs key quality attributes such as water-holding capacity, firmness and juiciness in meat products as well as in emerging plant-based analogues. However, exposure to reactive oxygen species during processing and storage can induce oxidative modifications—most notably protein carbonylation and thiol oxidation—that compromise network formation, leading to weakened gels, poor moisture retention and off-flavours. Maintaining oxidative stability is therefore essential to preserve both structural integrity and sensory quality. Advances in understanding the molecular determinants of gel formation and the pathways of oxidative damage have spurred the development of natural antioxidants, novel processing strategies and ingredient designs. These innovations aim to bolster the resilience of protein networks, extend shelf life and improve the nutritional and sensory performance of protein-rich foods across diverse global markets.
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Myofibrillar Protein Gelation and Oxidative Stability publication trend
The graph below shows the total number of articles in myofibrillar protein gelation and oxidative stability across all publications each year (not limited to Nature Index journals).
Technical terms
Myofibrillar proteins: Highly organised structural proteins (mainly myosin and actin) that form muscle fibres and drive gel formation during heating.
Gelation: Heat-induced process in which unfolded proteins form a three-dimensional network, entrapping water and fat to create a gel matrix.
Oxidative stability: Resistance of proteins to structural and functional degradation caused by reactive oxygen species.
Protein carbonylation: Irreversible oxidation of amino acid side chains to carbonyl groups, leading to protein aggregation and functional loss.
Sulfhydryl groups: Thiol (–SH) moieties in cysteine residues crucial for disulfide bond formation and network integrity.
References
- Effects of Gnaphalium affine Extract on the Gel Properties of •OH-Induced Oxidation of Myofibrillar Proteins. Foods (2024).
- Physicochemical Properties and Oxidative Stability of an Emulsion Prepared from (-)-Epigallocatechin-3-Gallate Modified Chicken Wooden Breast Myofibrillar Protein. Antioxidants (2022).
- Dose-Dependent Effect of Hyperoside on the Physicochemical and Gel Properties of Porcine Myofibrillar Proteins at Different NaCl Concentrations under Oxidative Stress. Foods (2023).
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