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Soy protein isolate (SPI) was oxidized by peroxyl radicals derived from 2,2′-azobis (2-amidinopropane) dihydrochloride (AAPH) and the structural and emulsifying properties of oxidized SPI were evaluated. Increasing extent of oxidation resulted in gradual carbonyl group generation, free sulfhydryl group degradation and dityrosine formation. Moderate oxidization could generate soluble protein aggregates...
The development of cold-set protein-stabilized emulsion gels has attracted increasing interests, due to their potential to be applied as a kind of release-controlled carriers, especially for labile lipid-soluble bioactive compounds. This work aimed to elucidate the importance of changing oil volume fraction (ø=0.2–0.6) for the formation and properties of cold-set soy protein isolate (SPI)-stabilized...
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