2011
DOI: 10.1016/j.ijms.2010.11.010
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Degradation and oxidation postmortem of myofibrillar proteins in porcine skeleton muscle revealed by high resolution mass spectrometric proteome analysis

Abstract: The rapid pH decline post-mortem causes denaturation (loss of functionality and water holding capacity) (WHC) of many proteins, and high rates of post mOltem muscle glycolysis favor

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Cited by 39 publications
(23 citation statements)
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“…Examples include post-mortem protein degradation [77,78], increased level of oxidation [79,80] and phosphorylation [36,67] of specific muscle proteins during post-mortem storage. Therefore, whether post-mortem changes have a role in reducing the abundance and/or confound the identification of these proteins may require further study.…”
Section: Fig 3 -Number Of Proteins Identified In the Three Crude Framentioning
confidence: 99%
“…Examples include post-mortem protein degradation [77,78], increased level of oxidation [79,80] and phosphorylation [36,67] of specific muscle proteins during post-mortem storage. Therefore, whether post-mortem changes have a role in reducing the abundance and/or confound the identification of these proteins may require further study.…”
Section: Fig 3 -Number Of Proteins Identified In the Three Crude Framentioning
confidence: 99%
“…These modifications include oxidation and phosphorylation on muscle proteins. Recent studies have indeed pointed out that protein oxidation is a significant process associated to post-mortem events [39,40]. In fact, the shift in energy metabolism after slaughter due to the lack of oxygen supply leads to the formation of reactive oxygen species (ROS) that cause oxidative damages to proteins.…”
Section: Protein Degradation and Modificationmentioning
confidence: 99%
“…As muscle tissue is converted into meat, myofibrillar and cytoskeletal proteins, such as desmin, actin, myosin, troponin and tropomyosin, are degraded by calpains (Lametsch and Bendixen, 2001;Lametsch et al, 2002;Lametsch et al, 2003;Lametsch et al, 2004;Morzel et al, 2004;Hwang et al, 2005;Muroya et al, 2007). Other proteins, including cellular defence/stress proteins (such as heat shock proteins (HSP) 70 and 27), and metabolic enzymes (such as creatine kinase, myokinase, pyruvate kinase, glycogen phosphorylase and NADH dehydrogenase) were also found to change in abundance during postmortem storage and therefore also seem to play a role in meat aging (Lametsch et al, 2002;Jia et al, 2006;Jia et al, 2007;Laville et al, 2009;Bjarnadottir et al, 2010;Bernevic et al, 2011). The postmortem accumulation of several enzymes involved in ATP-generating pathways, such as the glycolytic and the tricarboxylic acid cycles, suggests that an increase in aerobic metabolism occurs after slaughter to replenish ATP levels in muscle tissue (Jia et al, 2006).…”
Section: Postmortem Changes In Meat Proteinsmentioning
confidence: 99%
“…Oxidative processes may also contribute to drip loss. Using 2-DE combined with LC-MS/MS, Bernevic et al (2011) analyzed the oxidation profile of porcine muscle tissue at different drip losses. They identified and characterized several oxidative modifications in creatine kinase, actin, and triosephosphate isomerase, representing possible biomarker candidates.…”
Section: Proteomics To Study Effects Of Processing/conservation Treatmentioning
confidence: 99%