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

Abstract

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.

Effects of proteases on textural softening and changes in physical property of harpiosquillid mantis shrimp (Harpiosquilla raphidea) during the iced storage

“…This was related to pasty texture of the abdomen of HMS, in which ultimate protein degradation took place (Sriket et al ., 2011; Temdee et al ., 2021). Furthermore, denaturation of muscle protein could occur and induce the aggregation of proteins, thus lowering hydrophilic domain to bind with water (Chen et al ., 2022; Qian et al ., 2023; Zhang et al ., 2023b).…”

The Effects of Four Different Thawing Methods on Quality Indicators of Amphioctopus neglectus

“…During the thawing process, the oxidation of sulfhydryl groups triggers the creation of disulfide bonds, resulting in the cross-linking, linking, and aggregation of protein molecules. Consequently, this brings about alterations in the spatial configuration of MP [48,49]. The activity of Ca 2+ -ATPase can reflect the degree of denaturation and integrity of the myosin head, which contains the binding sites of Ca 2+ -ATPase activity, and thawing can lead to a varying degree of reduction in Ca 2+ -ATPase activity [46].…”

“…During the thawing process, the oxidation of sulfhydryl groups triggers the creation of disulfide bonds, resulting in the cross-linking, linking, and aggregation of protein molecules. Consequently, this brings about alterations in the spatial configuration of MP [48,49].…”

Insight into the evolution of textural properties and juiciness of ready‐to‐eat chicken breasts upon different thermal sterilization: From the perspective of protein degradation

“…Myofibrillar proteins (MP), which make up the highest percentage of muscle proteins, confer textural and functional properties to muscle food, such as water-holding capacity (WHC) and gel-forming abilities (Zhang et al, 2023). Heating within the range of 60-70 C induces denaturation and structural unfolding of myofibrillar proteins, which then aggregate to form a three-dimensional network gel structure that effectively retains moisture.…”