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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
.
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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.
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