Chemical, Physical, and Gel-forming Properties of Oxidized Myofibrils and Whey- and Soy-protein Isolates

ABSTRACT Myofibrils, oxidized with FeCl3/H2O2/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 isol...

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Bibliographic Details
Published in:Journal of food science 2000-08, Vol.65 (5), p.811-818
Main Authors: Liu, G., Xiong, Y.L., Butterfield, D.A.
Format: Article
Language:English
Subjects:
Animal, plant, fungal and microbial proteins, edible seaweeds and food yeasts
Biological and medical sciences
Food additives
Food industries
Food science
Fundamental and applied biological sciences. Psychology
Meat and meat product industries
myofibrils
protein oxidation
Proteins
soy
Soybeans
whey
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Summary:ABSTRACT Myofibrils, oxidized with FeCl3/H2O2/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.
ISSN:0022-1147
1750-3841
DOI:10.1111/j.1365-2621.2000.tb13592.x