Influence of oxidation on myofibrillar proteins degradation from bovine via μ-calpain

Development of microbial spoilage and lipid and protein oxidation in rabbit meat

“…In their study on the influence of oxidation on bovine myofibrillar proteins degradation, Xue, Huang, Huang & Zhou (2013) showed that increased protein oxidation enhanced the degradation of myosin heavy chain (MHC) but had little influence on the degradation of actin. Martinaud et al (1997) had earlier demonstrated that oxidation of myosin occurs naturally in meat during ageing.…”

“…Decker et al (1993) observed high molecular weight polymers produced by disulphide linkages mainly being derived from myosin and actin. Elsewhere, SDS-PAGE patterns have previously shown a decrease of band size and intensity of MHC after exposure to oxidant (Xue et al, 2013;Morzel et al, 2006). Ooizumi and Xiong (2004) indicated that the initial oxidation of chicken myofibrils induced changes in myosin, particularly intermolecular cross-linking of myosin heavy chain and modifications of thiol groups at the myosin ATPase active site.…”

“…Ooizumi and Xiong (2004) indicated that the initial oxidation of chicken myofibrils induced changes in myosin, particularly intermolecular cross-linking of myosin heavy chain and modifications of thiol groups at the myosin ATPase active site. Highly oxidative conditions cause cross-linking, polymerisation and aggregate formation in MHC through disulfide bonds, bityrosine and carbonyl (Xue et al, 2013;Morzel et al, 2006). Myofibrillar protein cross-linking in the form of binding and entrapping relating to the physical structures could affect meat tenderness (Huff-Lonergan and Lonergan, 2005).…”

“…The current study showed that actin was not affected by postmortem storage at 4 o C. The bands remained relatively stable after d 14 (Figure 1). Elsewhere, actin bands have also been found to be relatively stable even under oxidative conditions of µ-calpain (Xue et al, 2013) and chemical-induced oxidation (Morzel et al, 2006). Gil et al (2006) indicated that actin is degraded very little or not at all during meat ageing at 0-5 °C, even after 56 days and could only undergo substantial degradation at temperatures higher than 25 °C.…”

Effects of High Oxygen Packaging on Tenderness and Water Holding Capacity of Pork Through Protein Oxidation

“…However, the 80 KDa of μ-calpain contains an active cysteine residue at position 115 of catalytic domain II whereas cysteine is highly susceptible to oxidation and is easy to be inactivated through disulfide bond formation during protein oxidative modifications (Lametsch et al 2008;Zhang et al 2013b). Oxidation of proteins has been shown to change their functional properties and thereby concomitant oxidation of calpain and of their myofibrillar substrates can perform how those proteases and proteins act in the control of postmortem aging (Zhang et al 2013b;Rowe et al 2004;Xue et al 2012). To our knowledge, the effects of protein oxidation under HiOx on calpain activation, protein proteolysis, and then meat texture quality of pork are rather poorly studied.…”