Zhang Lingying, Zhang Yanna, Wang Yue, Chen Xing
State Key Laboratory of Food Science and Resources, Jiangnan University, Wuxi, Jiangsu, 214122, China.
School of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu, 214122, China.
Curr Res Food Sci. 2023 Oct 5;7:100611. doi: 10.1016/j.crfs.2023.100611. eCollection 2023.
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.
肌原纤维蛋白（MP）的热可逆凝胶可通过使用蛋白质谷氨酰胺酶（PG）进行精细脱酰胺化策略来制备，这项工作旨在揭示MP的热可逆凝胶化与卷曲螺旋（CC）之间的联系。酶促脱酰胺作用使肌原纤维细丝断裂并引发结构重组，从而形成小尺寸聚集体。肌球蛋白尾部CC结构的卷曲和解离是PG脱酰胺化MP（DMP）在可逆凝胶化动态演变中的基本结构基础。用三氟乙醇（TFE）特异性抑制CC组装后，DMP的热可逆凝胶能力受损，这证实了具有温度响应的CC动态组装在DMP的热可逆凝胶化中起关键作用。这些发现可能拓宽天然CC可逆凝胶化的分子基础，并推动新型肌肉蛋白产品开发的进展。
