Scientia Agricultura Sinica ›› 2016, Vol. 49 ›› Issue (7): 1360-1370.doi: 10.3864/j.issn.0578-1752.2016.07.012

• STORAGE·FRESH-KEEPING·PROCESSING • Previous Articles     Next Articles

Protein Phosphorylation on the Function of Myofibrillar Proteins in Mutton Muscle

CHEN Li-juan, LI Xin, LI Zheng, LI Pei-di, LI Zhong-wen, ZHANG De-quan   

  1. Institute of Food Science and Technology, Chinese Academy of Agricultural Sciences/Key Laboratory of Agro-Products Processing, Ministry of Agriculture, Beijing 100193
  • Received:2015-08-07 Online:2016-04-01 Published:2016-04-01

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Abstract: 【Objective】The aim of this study was to analyze the effect of the phosphorylation level which was improved by activating the activity of protein kinase on myofibrillar proteins’ degradation and contraction.【Method】Improve the activity of protein kinases by adding protein kinase A activator Forskolin and protein kinase C activator PMA, followed by the increasing of the phosphorylation level of myofirillar proteins in mutton muscle. By comparing the myofibrillar fragmentation index (MFI), the degree of myofibrillar degradation, the sarcomere length, and other indicators between activator groups and control group to determine the effect of protein phosphorylation levels on lamb muscle contraction and degradation. 【Result】The activity of protein kinases in the PMA group (PKC activated group) were higher than the control group after 1 hour, 2 hour, and 4 hour incubation (P＜0.05). The activity of protein kinases in the Forskolin group (PKA activated group) were higher than in the control group after 1 hour and 4 hour incubation (P＜0.05). The highest activity of the protein kinases appeared after 1 hour incubation. PMA and Forskolin can improve the phosphorylation level of titin, myosin binding protein C, tropomyosin, myosin light chain 2, and a protein of 25 kDa by activating the protein kinases, but the phosphorylation level of myosin heavy chain and actin had no changes. The degradation degree of the PMA group and the Forskolin group were lower than the control group, and the sarcomere length of the PMA group and the Forskolin group was shorter than the control group. 【Conclusion】 On the one hand, the improvement of the myofirillar proteins phosphorylation level can reduce the degree of myofibrillar degradation, while on the other hand, the improvement of the myofirillar proteins phosphorylation level may enhance the force of muscle contraction through the effect on myosin light chain 2, may accelerate the contraction of filament through the effect on adjacent tropomyosin, and finally influence the rigor mortis and tenderization.

Key words: mutton, protein phosphorylation, myofibrillar proteins, muscle contraction, protein degradation

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