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Heat‐induced Gelation Properties of Salt‐Soluble Muscle Proteins as Affected by Non‐Meat Proteins
Author(s) -
McCORD A.,
SMYTH A.B.,
O'NEILL E.E.
Publication year - 1998
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.1365-2621.1998.tb15789.x
Subject(s) - whey protein isolate , chemistry , whey protein , salt (chemistry) , food science , myosin , muscle protein , biochemistry , biology , skeletal muscle , organic chemistry , endocrinology
Addition of whey protein concentrate (WPC), whey protein isolate (WPI) or soy protein isolate (SPI) to salt‐soluble muscle proteins (SSP) decreased the gel strength. WPI:SSP gels had higher water‐holding capacity than SSP, SSP:WPC or SSP:SPI gels. Myosin heavy chain was a principal contributor to gel network formation in SSP, SSP:WPC, SSP:WPI and SSP:SPI systems. The characteristic fibrous network formed by SSP was the dominant feature of the microstructure of SSP:WPC and SSP:WPI gels. SSP:SPI gels had a more aggregated appearance due to the occurrence of clusters of SPI throughout the gel matrix.