中文摘要：

提取并研究了海刺参体壁组织蛋白酶B的酶学性质，结果表明，该酶最适反应pH为5．5，最适反应温度为40℃，在20℃～30℃酶活稳定，金属离子Ca^2＋、Mg^2＋、K^＋、Mn^2＋、Fe^2＋、Cu^2＋和Zn^2＋均能抑制酶活，其中Ca^2＋、Mg^2＋作用微弱，而Zn^2＋可完全抑制酶活；碘乙酸、EDTA对酶具有一定的抑制作用，亮抑酶肽、抗痛素和E-64对酶可完全抑制。DTF和L-半胱氨酸对酶有一定的激活作用。

英文摘要：

Cathepsin B was extracted from body wall of the sea cucumber and studied its enzymatic properties. The enzyme was purified by sulfate ammonium. The optimum pH and temperature were 5.5 and 40 ℃ respectively. The activity was stable at 20 ℃-30 ℃, but unstable when the temperature was higher. Metal cations including Ca^2＋, Mg^2＋, K^＋, Mn^2＋, Fe^2＋, Ca^2＋ and Zn^2＋ could inhibite the cathepsin B in various degree, the former two cations had slightly effect, but the last one could totally inhibite the enzyme. Cathepsin B was partially inhibited by indoacetic acid and EDTA, and was completely inhibited by leupeptin, antipain and E-64. On the contrary, DTT and L-cysteine could increase the activity of the protease.