Myofibrillar protein can form a thermo‐reversible gel through elaborate deamidation using protein‐glutaminase.

BACKGROUND: Novel thermo‐reversible hydrogels that undergo gelation in feedback to external stimuli have numerous applications in the food, biomedical, and functional materials fields. Muscle myofibrillar protein (MP) has long been known for thermally irreversible gelation. Once the reversible gelation of MP is achieved, its scope for research and application will expand. RESULTS: The work reported here achieved, for the first time, a thermo‐reversible MP gelation by elaborate deamidation using protein glutaminase (PG). The protein concentration and PG reaction time within windows of 1.0–2.5% and 8 h or 12 h were observed to be vital for creating thermo‐reversible gels. The gel strength increased with protein concentration. The gel displayed a perforated lamellar microstructure, which resulted in a high water‐holding capacity. The rheological results revealed the thermo‐reversibility of the gel was robust for up to five cycles of heating and cooling. The thermally reversible gelation is closely related to the reversible assembly between individual α‐helix and helical coiled coil. Hydrophobic interactions proved to be predominantly involved in the formation and stabilization of the gel network structure. CONCLUSION: This work increases the scope of research into the thermo‐responsive behavior of MP‐based gel. It can foster advances in research into the applications of muscle proteins and into the use of PG as a novel ingredient in the food industry. © 2022 Society of Chemical Industry. [ABSTRACT FROM AUTHOR]