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. 2016 Dec 31;25(6):1529–1535. doi: 10.1007/s10068-016-0237-x

Characterization of proteolysis in muscle tissues of sea cucumber Stichopus japonicus

Chen-Chen Zhao 1, Yang Yang 1, Hai-Tao Wu 1,2,✉, Zhi-Mo Zhu 1, Yue Tang 1,2, Cui-Ping Yu 1,2, Na Sun 1,2, Qiang Lv 1, Jia-Run Han 1, Ao-Ting Li 1, Jia-Nan Yan 1, Yue Cha 1
PMCID: PMC6049250  PMID: 30263441

Abstract

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.

Keywords: sea cucumber, muscle tissues, autolysis, proteolysis, cysteine protease

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