Thermo-reversible gelation of myofibrillar protein: Relationship between coiled-coil and thermal reversibility

Lingying Zhang; Yanna Zhang; Yue Wang; Xing Chen

doi:10.1016/j.crfs.2023.100611

Thermo-reversible gelation of myofibrillar protein: Relationship between coiled-coil and thermal reversibility

Curr Res Food Sci. 2023 Oct 5:7:100611. doi: 10.1016/j.crfs.2023.100611. eCollection 2023.

Authors

Lingying Zhang^{1

2}, Yanna Zhang^{1

2}, Yue Wang^{1

2}, Xing Chen^{1

2}

Affiliations

¹ State Key Laboratory of Food Science and Resources, Jiangnan University, Wuxi, Jiangsu, 214122, China.
² School of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu, 214122, China.

Abstract

Thermo-reversible gel of myofibrillar protein (MP) can be made by tactics of elaborate deamidation using protein-glutaminase (PG), and this work aimed to disclose the link between thermally reversible gelation of MP and the coiled-coil (CC). Enzymatic deamidation fragmented myofibril filaments and triggered structural reassembly to create small-sized aggregates. The coiling and dissociation of CC structure in the myosin tails is the fundamental structural basis of the PG deamidated MP (DMP) in the dynamic evolution of reversible gelation. After specific inhibition of CC assembly by trifluoroethanol (TFE), the thermo-reversible gel ability of DMP was impaired, which confirmed that the dynamic assembly of CC with temperature response played a key role in the thermo-reversible gelation of DMP. The findings may broaden the molecular basis of natural CC reversible gelation and foster advances for the development of new muscle protein products.

Keywords: Coiled-coil; Myofibrillar protein; Protein glutaminase; Thermo-reversible gel; Trifluoroethanol.