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- W2380547503 abstract "Chicken breast myofibrillar protein was oxidized to different extents after 24 h of incubation in hydroxyl radical generation systems(10 μ mol/L FeCl 3, 0.1 mmol/L ascorbic acid, and 0 to 5 mmol/L H 2 O 2) and physico-chemical properties of the different oxidation products and properties of heat-induced gels prepared from them were comparatively investigated. The results showed that carbonyl content steadily increased and thiol group content declined with increasing H 2 O 2 concentration, indicating continuous oxidation of the myofibrillar protein. Heat-induced gel hardness increased significantly as the concentration of H 2 O 2 increased from 0.00 to 0.10 mmol/L while protein solubility and surface hydrophobicity declined. When H 2 O 2 concentration increased up to 5 mmol/L, protein solubility as well as gel hardness and springiness significantly decreased( P 0.05), whereas the converse trend was observed for surface hydrophobicity. These results suggest that mild oxidation could improve the heat-induced gel formation of myofibrillar protein." @default.
- W2380547503 created "2016-06-24" @default.
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- W2380547503 date "2013-01-01" @default.
- W2380547503 modified "2023-09-26" @default.
- W2380547503 title "Effect of Oxidation Degree on Heat-induced Gel Formation and Physico-chemical Properties of Myofibrillar Protein" @default.
- W2380547503 hasPublicationYear "2013" @default.
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