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Echinobase
ECB-ART-46623
Food Sci Biotechnol 2016 Jan 01;256:1529-1535. doi: 10.1007/s10068-016-0237-x.
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Characterization of proteolysis in muscle tissues of sea cucumber Stichopus japonicus.

Zhao CC , Yang Y , Wu HT , Zhu ZM , Tang Y , Yu CP , Sun N , Lv Q , Han JR , Li AT , Yan JN , Cha Y .


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.

PubMed ID: 30263441
PMC ID: PMC6049250
Article link: Food Sci Biotechnol


Genes referenced: LOC100887844 LOC590297 LOC594261 LOC752081 LOC756768

References [+] :
Chen, Protease activity in post-mortem red swamp crayfish (Procambarus clarkii) muscle stored in modified atmosphere packaging. 2008, Pubmed