Mechanism of CaCl2 modulation of the properties of acyl-modified ovalbumin–myofibrillar protein composite gel

Chicken breast products exhibit a rough texture and poor taste owing to the special fibrous tissue structure of chicken breast. Thus, adapting the taste of processed chicken breast products is pivotal to improving consumer satisfaction. Therefore, we used CaCl2 and acyl-modified ovalbumin (AOVA) in a concerted effort to improve the gelation properties of chicken breast myofibrillar protein (MP). The investigation of molecular interactions and microstructure revealed the mechanism behind the changes in the physicochemical properties of the prepared gel. Molecular docking showed that AOVA enhanced the gel structure of MP through hydrogen bonding and salt bridges. The investigation results indicated that 0.30 mol/L CaCl2 facilitated the unfolding of AOVA-MP molecules, increasing the number of disulphide bonds and hydrophobic interactions, as well as conferring better hardness, springiness, cohesiveness, and chewing properties to the AOVA-MP gel with a denser and more homogeneous gel network structure. This study provides new insights into the quality improvement in chicken breast mince products. © 2024