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Chemical, Physical, and Gel‐forming Properties of Oxidized Myofibrils and Whey‐ and Soy‐protein Isolates
Author(s) -
Liu G.,
Xiong Y.L.,
Butterfield D.A.
Publication year - 2000
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.1365-2621.2000.tb13592.x
Subject(s) - myofibril , soy protein , whey protein isolate , chemistry , whey protein , polymerization , myosin , thermal stability , biochemistry , chromatography , food science , organic chemistry , polymer
Myofibrils, oxidized with FeCl 3 /H 2 O 2 /ascorbate, exhibited an increase in carbonyls and amines, SH→SS conversion, peptide scission, myosin polymerization, and a decrease in thermal stability and gel‐formation ability. Amino‐acid side chains of whey‐protein isolates (WPI) and soy‐protein isolates (SPI) were also modified during oxidation, but the thermal stability of WPI or SPI was not significantly altered. Oxidation increased elasticity of SPI gel but not that of WPI gel. Similarly, oxidation promoted interactions of myofibrils with SPI but not with WPI, resulting in > 30% increases in elasticity of the myofibril/SPI composite gel over its nonoxidized control. Hence, in processed meats where oxidation occurs, the presence of soy proteins may enhance the functionality of myofibrillar proteins.