Interaction of myofibrillar and preheated soy proteins

Soy protein isolate (SPI) was preheated at 90 degreesC and 95 degreesC for 3 min to obtain preheated samples, SPI 90 and SPI 95, respectively.,The preheat treatment increased protein, hydrophobicity and decreased the aggregation of 11S acidic and basic subunits. The 7S and 11S soy proteins exhibited a decreased thermal stability when mixed with pork niyofibrillar protein isolate (MPI). The presence of preheated SPI accelerated the disappearance of myosin heavy chain in the gelling process. Incorporation of preheated SPI significantly increased the MPI gel elasticity and hardness while native SPI showed negative effects.