Deciphering the thick filaments assembly behavior of myosin as affected by enzymatic deamidation

Enzymatic deamidation is a promising approach in enhancing the solubility of myofibrillar proteins (MPs) in water paving the way of tailor manufacturing muscle protein-based beverages. This work aimed to clarify the solubilization mechanism by deciphering myosin thick filaments assembly as affected by protein-glutaminase deamidation. With the extension of deamidation, filamentous structures in MPs shortened continuously. Dynamic monitoring of quartz crystal microbalance-dissipated showed the adsorption capacity of the deaminated MPs was reduced from 3.66 ng/cm² to 2.03 ng/cm², indicating that the ability to assemble myosin thick filaments was significantly weakened. By simulating the surface charge, it was found that deamidation may neutralize the positive charged clusters distanced at 14-29 nm from rod C-terminus. Since this region confers myosin electrostatic property to initiate staggered dimerization, deamidation in this region, which severely affected the electrostatic balance between residues, impaired ordered thick filament growing and elongating, thus promoting the solubilization of MPs in water.