Identification of S-nitrosylated proteins in postmortem pork muscle using modified biotin switch method coupled with isobaric tags

Meat tenderness: advances in biology, biochemistry, molecular mechanisms and new technologies

“…This suggested a lack of involvement of Calpain-1 in the observed tenderizing effect of HPP. Contrary to these findings, Zhang et al (2018b) reported that pork subjected to HPP treatment (range 0-400 MPa, for 10 min at 20°C and kept at 4°C before treatment) within 2 h of slaughter showed higher MFI, an indication of increased proteolysis. HPP treatment of Calpain-2 and Calpain-1 and calpastatin in saline resulted in a small decrease in the Calpain-1 activity and a substantial decrease in calpastatin activity, suggesting a role for the calpain system in pork tenderization by HPP (Zhang et al, 2018b) which is in contrast to previous findings.…”

“…Contrary to these findings, Zhang et al (2018b) reported that pork subjected to HPP treatment (range 0-400 MPa, for 10 min at 20°C and kept at 4°C before treatment) within 2 h of slaughter showed higher MFI, an indication of increased proteolysis. HPP treatment of Calpain-2 and Calpain-1 and calpastatin in saline resulted in a small decrease in the Calpain-1 activity and a substantial decrease in calpastatin activity, suggesting a role for the calpain system in pork tenderization by HPP (Zhang et al, 2018b) which is in contrast to previous findings. Furthermore, the authors reported that HPP prevented rigor development and thus it appears that mechanical and biochemical factors may explain the tenderizing effects of HPP of pork.…”

“…NO and protein S-nitrosylation are involved in postmortem metabolism which might account for the variation in meat tenderization. A large number of proteins including glycolytic enzymes, antioxidant proteins and enzymes, myofibrillar proteins, Ca 2+ channel components and heat shock proteins were identified to be S-nitrosylated in pork muscle (see Table 1; Liu et al, 2018b). Those proteins were proposed to be involved in biochemical processes including glycolysis and pH decline, calpain autolysis and proteolysis and Ca 2+ release from SR in postmortem muscle (Figure 1).…”

“…A recent meta-analysis of 23 experiments and 216 treatments on high pressure processing (HPP) applied to beef, sheepmeat, pork and chicken showed that the maximum tenderization occurred using 68-80 o C at 100-150 MPa, and significant tenderization also occurred under HPP conditions of 35-60 o C and 100-150 MPa . Recent studies have focused on exploring the mechanism of action for the tenderizing effect of HPP (high hydrostatic pressure) (Morton et al, 2017;Morton, Lee, Pearson, & Bickerstaffe, 2018;Zhang et al, 2018b;. Beef hot-boned within 1 h of slaughter, at a temperature of 30-35°C, treated with HPP (175 MPa, for 2 min) and chilled to -1°C for 1 day, resulted in 60% and 43% lower WBSF in longissimus thoracis and gluteus medius, respectively and better sensory scores compared to controls (Morton et al, 2017).…”

Myoglobin Post-Translational Modifications Influence Color Stability of Beef Longissimus Lumborum

“…PTM can modulate proteins' functionality, localization, turnover, and interactions with other proteins (Seo and Lee, 2004;Rakhit et al, 2014;Müller, 2017). Previous investigations have documented that PTM in calpain (Liu et al, 2016;Du et al, 2019), myofibrillar proteins (Huang et al, 2012;Li et al, 2017), and metabolic enzymes (Anderson et al, 2014;Cruzen et al, 2015;Carlson et al, 2017;Huang et al, 2018;Liu et al, 2018) in skeletal muscles of livestock (cattle, pig, and sheep) influenced meat tenderness and muscle to meat conversion. The aforementioned studies suggested the potential of protein PTM as novel biomarkers for meat quality (Li et al, 2021).…”