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  • Title: Gelation properties of myofibrillar protein under malondialdehyde-induced oxidative stress.
    Author: Wang L, Zhang M, Fang Z, Bhandari B.
    Journal: J Sci Food Agric; 2017 Jan; 97(1):50-57. PubMed ID: 26916602.
    Abstract:
    BACKGROUND: The structure of myofibrillar protein (MP) can be readily altered by oxidation, leading to the unfolding of MP structure, which further promotes protein-protein interactions, and thus influences the MP gelling properties. The objective of the study was to investigate the effect of malondialdehyde-induced oxidative stress on the gelation properties of myofibrillar protein (MP). Structural changes of the oxidised MPs were evaluated by the contents of carbonyl and total sulfhydryls, surface hydrophobicity, SDS-PAGE and Fourier transform infrared spectroscopy. The oxidative stability of the MP gels as indicated by lipid hydroperoxide was also determined. RESULTS: With the addition of an MDA concentration less than 10 mmol L-1 , the MP gels showed an improved elasticity, gel strength, water holding capacity, and oxidative stability. Nevertheless, higher MDA concentration (25-50 mmol L-1 ) significantly reduced the gel quality, probably due to the formation of excessive covalent bonds in the system. CONCLUSION: Results suggested that protein aggregation occurred in the oxidised system. Myosin was involved in gel formation through non-disulfide covalent bond. © 2016 Society of Chemical Industry.
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