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Interaction of Myofibrillar and Preheated Soy Proteins
Author(s) -
Feng J.,
Xiong Y.L.
Publication year - 2002
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.2002.tb08827.x
Subject(s) - myofibril , soy protein , chemistry , myosin , protein aggregation , food science , chromatography , thermal stability , biochemistry , organic chemistry
Soy protein isolate (SPI) was preheated at 90 °C and 95 °C 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 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.