Enhancing the quality attributes of porcine myofibrillar proteins through low-frequency alternating magnetic field-assisted freezing

Abstract

This study explores the potential of low-frequency alternating magnetic field-assisted freezing (LF-MFF) on enhancing the physicochemical stability and gelling performance of porcine myofibrillar proteins (MPs). We observed that LF-MFF markedly reduced oxidative denaturation of MPs compared to refrigerator freezing (RF), thus maintaining higher gel quality. Notably, LF-MFF treatment at 3-4 mT enhanced MPs' solubility, decreased turbidity, and lowered dityrosine content. LF-MFF at 4 mT also effectively minimized MPs' aggregation and degradation. Rheological measurements revealed that the storage modulus (G') and apparent viscosity of MPs treated with 3-4 mT LF-MFF are comparable to those of fresh samples (FS). Furthermore, LF-MFF at 3-4 mT significantly improved the water-holding capacity (WHC), whiteness, gel strength, and textural properties of MPs. The 3-4 mT LF-MFF was particularly effective in enhancing hydrophobic interactions and hydrogen bonding, thereby inhibiting water mobility and protecting microstructure of MPs gels. In summary, LF-MFF, especially at 4 mT, improved the gelation properties of MPs by reducing oxidative denaturation, providing significant insights for its application in the frozen meat industry.

Keywords: Gelling properties; Low-frequency alternating magnetic field-assisted freezing; Microstructure; Myofibrillar proteins; Physicochemical characteristics; Water distribution.