Regulating the gel structure and digestive function of myofibrillar protein: The distinct roles of pre-hydrated curdlan and β-glucan

This study investigated the effects of pre-hydrated curdlan (CT) and β-glucan (BT) (0.2–1.0 %) on the gel structure, digestion, and rheological properties of myofibrillar protein (MP). Both CT and BT significantly reduced MP digestibility, with CT showing a stronger effect (14.04 % reduction at 1.0 % addition). Hydrogen bonds and hydrophobic interactions were key in stabilizing MP-polysaccharide gels, as confirmed by molecular simulations. CT and BT addition led to smaller particle sizes, more stable zeta potential, and increased α-helix content while reducing random coil structures. Additionally, CT had a greater impact on the tertiary structure of MP. Rheological analysis revealed enhanced gel viscoelasticity in a dose-dependent manner, with CT being more effective. After digestion, gel structures became looser but retained certain features, especially in MP-CT gels. These findings highlight the distinct roles of CT and BT in regulating gel structure and digestion of MP, offering insights for improving meat product functionality.