An endopeptidase (Cudrania protease) with a molecular mass of 76 kDa has been purified from the fruits of Cudrania cochinchinensis (Lour.) Kudo et Masam. The enzyme was stable between pH 6 and 10 at 30°C for 60 min. The enzyme activity was inhibited by diisopropyl fluorophosphate, chymostatin, and aprotinin, but not by EDTA or pepstatin. These results indicated that the enzyme was a serine protease.
从 Cudrania cochinchinensis (Lour.) Kudo et Masam 的果实中纯化出了一种分子质量为 76 kDa 的内肽酶(Cudrania
蛋白酶)。在 30°C 条件下,该酶在 pH 值 6 和 10 之间稳定 60 分钟。该酶的活性受
氟磷酸二异
丙酯、糜
蛋白酶和阿普罗汀的抑制,但不受
乙二胺四乙酸乙二酯(
EDTA)和胃
蛋白酶的抑制。这些结果表明该酶是一种
丝氨酸蛋白酶。