Interaction between liposome and myofibrillar protein in surimi: Effect on gel structure and digestive characteristics

Abstract

This study investigated the effects of the interaction between liposomes and myofibrillar protein (MP) on tilapia surimi. The strong interaction between liposomes and MP was primarily mediated through hydrogen bonding and hydrophobic interaction. Liposomes caused the unfolding of MP structure, resulting in the decrease of α-helix content and transformation of spatial structure. Notably, the appropriate ratio of liposomes improved the gel properties of tilapia surimi. The water distribution, microstructure, and texture characteristics further confirmed that liposomes strengthened the structure of surimi gel through non-covalent bonds. However, excessive liposomes (1.0 %) weakened gel characteristics and texture. Moreover, the proper ratio of liposomes enhanced the stability of surimi gels during digestion, reducing protein digestibility from 66.0 % to 54.8 %. Curcumin-loaded liposomes in gel matrix notably delayed digestion and improved bioavailability. This delay in digestion was attributed to the ability of liposomes to decrease the interaction between MP and digestive enzymes. This study provides new insight into the application of liposomes in protein-rich food matrixes.

Keywords: Hydrogen bond; Liposome; Myofibrillar protein.