Biochemical changes ofCoregonus peledmyofibrillar proteins isolates as affected by HRGS oxidation system

• DOI: 10.1111/jfbc.12710
• Publication Date: 2018-10-25T02:35:05Z
• Authors: Xiaorong Deng; Yongdong Lei; Juan Liu; Jian Zhang; Junwei Qin
• Keywords: Lipid Oxidation; Myofibril

The objective of the study was to research effect protein oxidation on biochemical properties Coregonus peled muscle proteins. Myofibrillar proteins (MP) prepared from C. back oxidized using a hydroxyl radical-generating system (HRGS: 0.1 mM FeCl3 , ascorbic acid (Asc) and 1-20 H2 O2 ). In HRGS oxidizing system, carbonyls, dityrosine content, surface hydrophobicity MP (p < 0.05) increased with increasing concentration time, while total sulfhydryl, free amino groups Ca-ATPase activity decreased 0.05). sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) pattern reflected formation polymers degradation. results indicate that levels alterations have influence quality protein. PRACTICAL APPLICATIONS: Protein plays major role in meat deterioration peled, which always leads change physical chemical properties. this study, isolates as affected by proposed. Such modification loss groups, shift isoelectric point protein, solubility functionality. Additionally, carbonyls been found be potentially toxic humans, relevant measurement those cause health problems after oral administration. So such modifications are technological nutritional relevance.