Interaction of Myofibrillar and Preheated Soy Proteins |
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| Authors: | J Feng YL Xiong |
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| Affiliation: | Authors Feng and Xiong are with the Food Science Section, Dept. of Animal Sciences, Univ. of Kentucky, Lexington, KY 40546. Direct inquiries to author Xiong (E-mail: ). |
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| Abstract: | ABSTRACT: Soy protein isolate (SPI) was preheated at 90 °C and 95 °C for 3 min to obtain preheated samples, SPI90 and SPI95, 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 myofibrillar 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. |
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| Keywords: | soy protein isolate heat treatment myosin protein-protein interaction gelation |
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