Lijuan Chen1, Xin Li1, Na Ni1, Yue Liu1, Li Chen1, Zhenyu Wang1, Qingwu W Shen1, Dequan Zhang1,2. 1. Institute of Agro-Products Processing Science and Technology, Chinese Academy of Agricultural Sciences/Key Laboratory of Agro-Products Processing, Ministry of Agriculture, Beijing 100193, People's Republic of China. 2. Synergetic Innovation Center of Food Safety and Nutrition, Beijing 100193, People's Republic of China.
Abstract
BACKGROUND: Tenderness is one of the most important quality attributes especially for beef and lamb. As protein phosphorylation and dephosphorylation regulate glycolysis, muscle contraction and turnover of proteins within living cells, it may contribute to the conversion of muscle to meat. The changes of myofibrillar protein phosphorylation in post-mortem ovine muscle with different levels of tenderness were investigated in this study. RESULTS: The protein phosphorylation level (P/T ratio) of the tender group increased from 0.5 to 12 h post mortem and then decreased. The P/T ratio of tough group increased during 24 h post mortem, increasing faster from 0.5 to 4 h post mortem than from 4 to 24 h post mortem.The global phosphorylation level of tough meat was significantly higher than tender meat at 4, 12 and 24 h post mortem (P < 0.05). Protein identification revealed that most of the phosphoproteins were proteins with sarcomeric function; the others were involved in glycometabolism, stress response, etc. The phosphorylation levels of myofibrillar proteins, e.g. myosin light chain 2 and actin, were significantly different among groups of different tenderness and at different post-mortem time points (P < 0.05). CONCLUSION: Protein phosphorylation may influence meat rigor mortis through contractile machinery and glycolysis, which in turn affect meat tenderness.
BACKGROUND: Tenderness is one of the most important quality attributes especially for beef and lamb. As protein phosphorylation and dephosphorylation regulate glycolysis, muscle contraction and turnover of proteins within living cells, it may contribute to the conversion of muscle to meat. The changes of myofibrillar protein phosphorylation in post-mortem ovine muscle with different levels of tenderness were investigated in this study. RESULTS: The protein phosphorylation level (P/T ratio) of the tender group increased from 0.5 to 12 h post mortem and then decreased. The P/T ratio of tough group increased during 24 h post mortem, increasing faster from 0.5 to 4 h post mortem than from 4 to 24 h post mortem.The global phosphorylation level of tough meat was significantly higher than tender meat at 4, 12 and 24 h post mortem (P < 0.05). Protein identification revealed that most of the phosphoproteins were proteins with sarcomeric function; the others were involved in glycometabolism, stress response, etc. The phosphorylation levels of myofibrillar proteins, e.g. myosin light chain 2 and actin, were significantly different among groups of different tenderness and at different post-mortem time points (P < 0.05). CONCLUSION: Protein phosphorylation may influence meat rigor mortis through contractile machinery and glycolysis, which in turn affect meat tenderness.
Authors: Rafael Torres de Souza Rodrigues; Mario Luiz Chizzotti; Camilo Elber Vital; Maria Cristina Baracat-Pereira; Edvaldo Barros; Karina Costa Busato; Rafael Aparecido Gomes; Márcio Machado Ladeira; Taiane da Silva Martins Journal: PLoS One Date: 2017-01-19 Impact factor: 3.240
Authors: Eileen Armstrong; Andres Iriarte; Paula Nicolini; Jorge De Los Santos; Javier Ithurralde; Alejandro Bielli; Gianni Bianchi; Francisco Peñagaricano Journal: PLoS One Date: 2018-07-24 Impact factor: 3.240