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EnglishMeat quality development is highly influenced by the pH decline caused by the postmortem (PM) glycolysis. Protein phosphorylation is an important mechanism in regulating the activity of glycometabolic enzymes. Here, a gel-based phosphoproteomic study was performed to analyze the protein phosphorylation in sarcoplasmic proteins from three groups of pigs with different pH decline rates from PM 1 to 24 h. Globally, the fast pH decline group had the highest phosphorylation level at PM 1 h, but lowest at 24 h, whereas the slow pH decline group showed the reverse case. The same pattern was also observed in most individual bands in 1-DE. The protein phosphorylation levels of 12 bands were significantly affected by the synergy effects of pH and time (p<0.05). Protein identification revealed that most of the phosphoproteins were glycometabolism-related enzymes, and the others were involved in stress response, phosphocreatine metabolism, and other functions. The phosphorylation of pyruvate kinase and triosephosphate isomerase-1 showed to be related to PM muscle pH decline rate. Our work sheds light on the potential role of protein phosphorylation on regulating meat quality development.
| Titolo: | Gel-based phosphoproteomics analysis of sarcoplasmic proteins in postmortem porcine muscle with pH decline rate and time differences |
| Autore/i: | H. Huang; M. R. Larsen; A. H. Karlsson; L. Pomponio; NANNI COSTA, LEONARDO; R. Lametsch |
| Autore/i Unibo: | |
| Anno: | 2011 |
| Rivista: | |
| Digital Object Identifier (DOI): | http://dx.doi.org/10.1002/pmic.201100173 |
| Abstract: | Meat quality development is highly influenced by the pH decline caused by the postmortem (PM) glycolysis. Protein phosphorylation is an important mechanism in regulating the activity of glycometabolic enzymes. Here, a gel-based phosphoproteomic study was performed to analyze the protein phosphorylation in sarcoplasmic proteins from three groups of pigs with different pH decline rates from PM 1 to 24 h. Globally, the fast pH decline group had the highest phosphorylation level at PM 1 h, but lowest at 24 h, whereas the slow pH decline group showed the reverse case. The same pattern was also observed in most individual bands in 1-DE. The protein phosphorylation levels of 12 bands were significantly affected by the synergy effects of pH and time (p<0.05). Protein identification revealed that most of the phosphoproteins were glycometabolism-related enzymes, and the others were involved in stress response, phosphocreatine metabolism, and other functions. The phosphorylation of pyruvate kinase and triosephosphate isomerase-1 showed to be related to PM muscle pH decline rate. Our work sheds light on the potential role of protein phosphorylation on regulating meat quality development. |
| Data prodotto definitivo in UGOV: | 2013-06-15 15:06:50 |
| Appare nelle tipologie: | 1.01 Articolo in rivista |
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