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Phosphorylation of myosin regulatory light chain affects actomyosin dissociation and myosin degradation
Author(s) -
Cao Lichuang,
Hou Chengli,
Shen Qingwu,
Zhang Dequan,
Wang Zhenyu
Publication year - 2019
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.14138
Subject(s) - myosin , phosphorylation , dissociation (chemistry) , myosin light chain kinase , immunoglobulin light chain , biophysics , chemistry , biology , microbiology and biotechnology , biochemistry , antibody , immunology , organic chemistry
Summary This research aimed to investigate the influence of myosin regulatory light chain ( MRLC ) phosphorylation on actomyosin dissociation and myosin degradation in post‐mortem ovine longissimus thoracis ( LT ) muscle with a purpose for strategies to improve meat quality in practice. Data obtained show that the highest actomyosin dissociation occurred at 48 h post‐mortem. Based on the cluster analysis of the actomyosin dissociation degree at 48 h post‐mortem, samples were divided into high, middle and low‐actomyosin dissociation groups. During 0.5–72 h post‐mortem, the phosphorylation level of MRLC significantly decreased ( P < 0.05), while actomyosin dissociation, and degradation of MRLC and myosin heavy chains ( MHC ) significantly increased ( P < 0.05). The level of MRLC phosphorylation was negatively correlated with the degree of actomyosin dissociation ( r = −0.794, P < 0.05), and the degradation of MRLC ( r = −0.764, P < 0.05) and MHC ( r = −0.826, P < 0.05). In conclusion, phosphorylation of MRLC may regulate actomyosin dissociation, as well as degradation of MRLC and MHC .