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
1School of Food Science and Technology, Dalian Polytechnic University, Dalian, 116034 China.
National Engineering Research Center of Seafood, Dalian, 116034 China.
Food Sci Biotechnol. 2016 Dec 31;25(6):1529-1535. doi: 10.1007/s10068-016-0237-x. eCollection 2016.
The proteolysis in muscle tissues of sea cucumber (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 -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.
对海参肌肉组织中的蛋白水解作用（sjMTs）进行了表征。sjMTs中的蛋白质主要是肌球蛋白重链（MHCs）、副肌球蛋白（Pm）和肌动蛋白（Ac），其分子量分别约为200、98和42 kDa。基于SDS-PAGE分析和对释放的三氯乙酸（TCA）可溶性肽的定量，sjMTs中肌肉蛋白在pH 5和50°C时易于降解。MHCs的蛋白水解作用大多被半胱氨酸蛋白酶抑制剂抑制，包括环氧琥珀酰-L-亮氨酰-氨基（4-胍基）丁烷（E-64）和抗蛋白酶（AP）。E-64和AP完全抑制了Pm和Ac的降解，而碘乙酸显示出部分抑制作用。这些结果表明，sjMTs的蛋白水解作用主要归因于半胱氨酸蛋白酶。避免将组织置于40-50°C和微酸性条件下以及抑制半胱氨酸蛋白酶有助于减少海参自溶。
