Effect of oxidation on the structural and functional properties of myofibrillar in Coregonus peled

Abstract

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