Add time:08/04/2019         Source:sciencedirect.com

This study aimed to establish the influence of protein oxidation on the ability of magnesium pyrophosphate (PP) to dissociate actomyosin. Actomyosin isolated from pork muscle then suspended in 0.1 M NaCl at pH 6.2 was oxidatively stressed with 10 μM FeCl3/0.1 mM ascorbate/1 mM H2O2 for 6 or 12 h at 4 °C. Protein oxidation was evidenced by the loss of myosin and actin, the concomitant formation of disulphide-cross-linked polymers, and elevated myosin ATPase activity. The intrinsic viscosity of oxidized actomyosin had a weaker response to PP-Mg2+ than that of non-oxidized actomyosin, indicating the suppression of actomyosin dissociation. Moreover, oxidized actomyosin solutions were devoid of small particles (<10 nm) and the stressed actomyosin exhibited weaker binding of PP-Mg2+ than non-oxidized, which further suggested a reduced myosin–PP interaction and subsequent dissociation of the actomyosin complexes.

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