Physicochemical and structural changes of myofibrillar proteins in muscle foods during thawing: Occurrence, consequences, evidence, and implications

Myofibrillar protein (MP) endows muscle foods with texture and important functional properties, such as water-holding capacity (WHC) and emulsifying and gel-forming abilities. However, thawing deteriorates the physicochemical and structural properties of MPs, significantly affecting the WHC, texture, flavor, and nutritional value of muscle foods. Thawing-induced physicochemical and structural changes in MPs need further investigation and consideration in the scientific development of muscle foods. In this study, we reviewed the literature for the thawing effects on the physicochemical and structural characters of MPs to identify potential associations between MPs and the quality of muscle-based foods. Physicochemical and structural changes of MPs in muscle foods occur because of physical changes during thawing and microenvironmental changes, including heat transfer and phase transformation, moisture activation and migration, microbial activation, and alterations in pH and ionic strength. These changes are not only essential inducements for changes in spatial conformation, surface hydrophobicity, solubility, Ca²⁺ -ATPase activity, intermolecular interaction, gel properties, and emulsifying properties of MPs but also factors causing MP oxidation, characterized by thiols, carbonyl compounds, free amino groups, dityrosine content, cross-linking, and MP aggregates. Additionally, the WHC, texture, flavor, and nutritional value of muscle foods are closely related to MPs. This review encourages additional work to explore the potential of tempering techniques, as well as the synergistic effects of traditional and innovative thawing technologies, in reducing the oxidation and denaturation of MPs and maintaining the quality of muscle foods.