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Role of the ubiquitin‐proteasome pathway on proteolytic activity in postmortem proteolysis and tenderisation of sheep skeletal muscle
Author(s) -
Liu Yue,
Du Manting,
Li Xin,
Chen Li,
Shen Qingwu,
Tian Jianwen,
Zhang Dequan
Publication year - 2016
Publication title -
international journal of food science and technology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.831
H-Index - 96
eISSN - 1365-2621
pISSN - 0950-5423
DOI - 10.1111/ijfs.13214
Subject(s) - myofibril , proteasome , sarcomere , ubiquitin , proteolysis , protein degradation , skeletal muscle , microbiology and biotechnology , chemistry , biochemistry , biology , anatomy , myocyte , enzyme , gene
Summary The objective of this study was to investigate the effects of ubiquitin‐proteasome pathway on meat tenderisation. The sheep muscle longissimus lumborum was injected with or without PYR ‐41 (inhibitor of ubiquitination) or MG ‐132 (inhibitor of proteasome). Muscle samples were collected at 6, 15, 24 and 48 h after injection. Myofibrillar protein degradation, muscle ultrastructure and sarcomere length were determined. Results showed that inhibition of proteasome or ubiquitination affected sarcomere length at 48 h after treatments. Destruction of muscle ultrastructure in both treatments was reduced when compared to control. Inhibition of proteasome produced different fragments of myofibrillar proteins in comparison with control at 48 h. In conclusion, ubiquitin‐proteasome plays a role in postmortem proteolysis and might contribute to meat tenderisation.