Abstract
Oxidation extent of myofibrillar protein (MP) from silver carp (Hypophthalmichthys molitrix) was affected by the content and type of lipid peroxidation (LPO) products. Oxidized linoleic acid (OLA) was selected as a main representative of lipid peroxidation to investigate the effects of oxidative modification of LPO products on MP structure. Structural changes of the oxidized myofibrillar protein were evaluated by the contents of carbonyl and total sulfhydryls, surface hydrophobicity, SDS-PAGE and Fourier transform infrared spectroscopy. Heating procedure was also applied for further evaluation of gelling properties. The results from SDS-PAGE indicated that aggregation and denaturation of myosin occurred in the oxidized system. The presence of OLA intensified oxidation-initiated loss of a-helix conformation as well as tertiary structure of MP. With the addition of OLA concentration less than 3 mM, a remarkably enhanced gelling capacity of MP was observed. While the excessive covalent bond (OLA > 5 mM) could lead to the breakage of protein-protein bonds, causing the collapse of the gel structure. The gelation procedure induced by OLA involved simultaneous protein oxidation and internal cross-linking.
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Acknowledgments
We acknowledge the financial support by Jiangsu Province (China) “Collaborative Innovation Center for Food Safety and Quality Control”Industry Development Program, and Jiangsu Province (China) Infrastructure Project (Contract No. BM2014051) which have enabled us to carry out this study.
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Wang, L., Zhang, M., Fang, Z. et al. Influence of Linoleic Acid-Induced Oxidative Modification on Gel Properties of Myofibrillar Protein from Silver Carp (Hypophthalmichthys molitrix) Muscle. Food Biophysics 11, 266–274 (2016). https://doi.org/10.1007/s11483-016-9438-3
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DOI: https://doi.org/10.1007/s11483-016-9438-3