This study examined the impact of pre-acidification induction on the quality attributes and flavor retention of ready-to-cook (RTC) goose meat products. The results demonstrated that pre-acidification could influence the eating qualities of RTC goose meat by effectively regulating the physicochemical properties of goose myofibrillar proteins (MP) including solubility and water-holding capacity. Elevated carbonyl contents indicated an enhanced gel-forming capacity in RTC goose meat during storage, accompanied with reduced total sulfhydryl contents from enhanced protonation pretreatment and augmented lipid oxidation. Structural characterization of MP via sodium dodecyl sulfate-polyacrylamide gel electrophoresis, circular dichroism spectroscopy, and intrinsic fluorescence revealed the formation of a dense protein matrix under highly acidic conditions. Furthermore, the headspace concentration of aldehydes increased by 3.23 times upon enhancing the pre-acidification intensity, resulting in the production of esters and acidic flavor compounds with favorable aromas. Correlation analysis demonstrated the dependence of headspace concentrations of volatile constituents on the acidification-enhanced surface hydrophobicity of MP, attributed to the modified binding sites of proteins after pre-acidification. Current results have indicated both the positive and negative influence of pre-acidulation induction on the eating quality of goose meat products, suggesting the necessity of introducing extra processes to modulate the quality of prefabricated products.
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·H2O2 could form hydrogen bonds with MP, while O3 and NO2‾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.