Structural and gel property changes in chicken myofibrillar protein induced by argon cold plasma-activated water: With a molecular docking perspective.

This study investigated the effects of plasma-activated water (PAW) generated with argon at discharge times of 0, 4, 8, 12, and 16 min on the gel properties and structures of chicken myofibrillar protein (MP). Under treatments of 8, 12, and 16 min, both the gel strength and water retention capacity of MP significantly improved, with the gel strength (0.53 N) peaking at 16 min and the lowest cooking loss（30.38 %）. As the treatment time increased from 0 to 16 min, the storage modulus also gradually increased. Results from low-field nuclear magnetic resonance indicated a slowing of water proton mobility, with the proportion of bound water rising from 0.26 % (0 min) to 0.52 % at 16 min. Fourier transform infrared spectroscopy, endogenous fluorescence spectroscopy and scanning electron microscopy confirmed PAW's alteration of MP's secondary and tertiary structures and gel microstructure. Additionally, this study explored the influence of argon PAW's primary active species on MP from a molecular docking perspective·HO could form hydrogen bonds with MP, while O and NO‾could interact via both hydrogen bonds and electrostatic interactions. Thus, PAW can alter protein structure and enhance MP's functional properties, providing insights for applying cold plasma in processing chicken gel products.