Jump to Main Content
Characterization of proteolysis in muscle tissues of sea cucumber Stichopus japonicus
- Zhao, Chen-Chen, Yang, Yang, Wu, Hai-Tao, Zhu, Zhi-Mo, Tang, Yue, Yu, Cui-Ping, Sun, Na, Lv, Qiang, Han, Jia-Run, Li, Ao-Ting, Yan, Jia-Nan, Cha, Yue
- Food science and biotechnology 2016 v.25 no.6 pp. 1529-1535
- Apostichopus japonicus, actin, autolysis, butanes, cysteine proteinase inhibitors, cysteine proteinases, iodoacetic acid, molecular weight, muscle protein, muscle tissues, myosin heavy chains, pH, peptides, polyacrylamide gel electrophoresis, proteolysis, trichloroacetic acid
- The proteolysis in muscle tissues of sea cucumber Stichopus japonicus (sjMTs) was characterized. The proteins from sjMTs were primarily myosin heavy chains (MHCs), paramyosin (Pm), and actin (Ac) having a molecular mass of approximately 200, 98, and 42 kDa, respectively. Based on SDS-PAGE analysis and quantification of trichloroacetic acid (TCA)-soluble peptides released, degradation of muscle proteins from sjMTs was favorable at pH 5 and 50°C. Proteolysis of MHCs was mostly inhibited by cysteine protease inhibitors, including trans-epoxysuccinyl-L-leucyl-amido (4-guanidino) butane (E-64) and antipain (AP). E-64 and AP completely inhibited the degradation of Pm and Ac, while iodoacetic acid showed a partially inhibitory effect. These results indicated that the proteolysis of sjMTs was mainly attributed to cysteine proteases. Avoidance of setting the tissues at 40–50°C and slightly acidic condition and inhibition of cysteine proteases are helpful for decreasing sea cucumber autolysis.