Effect of oxidation on the structural and functional properties of myofibrillar in Coregonus peled
Myofibril
Mole
DOI:
10.47836/ifrj.28.5.09
Publication Date:
2022-06-30T12:52:33Z
AUTHORS (5)
ABSTRACT
The effects of the degree oxidation (0.01 mmol/L FeCl3, 0.1 ascorbic acid, 1 - 20 H2O2) principally induced by Fenton systems on structural and functional properties Coregonus peled myofibrillar proteins (MP) was investigated. When levels MP increased, their carbonyl groups increased but sulfhydryl decreased (p < 0.05). SDS-PAGE analysis revealed more cross-linking protein polymerisation in oxidised MP. FTIR suggested that conformational changes results indicated moderate (5 10 improved foaming capacity thus providing better properties; while excessive (≥ 15 led to deterioration due formation large aggregates, therefore, should be avoided application food processing industry.
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