章鱼消化道蛋白酶的分离纯化及性质OA北大核心CSCDCSTPCD
Extraction, Purification and Characterization of Protease from Digestive Tract of Octopus vulgaris
以章鱼加工下脚料消化道为原料，经硫酸铵沉淀、纤维素CM-52阳离子交换层析、DEAE-SephadexA50阴离子交换层析、SDS-PAGE电泳等方法，从中提取纯化出一种蛋白酶电泳纯样品OP-I，并对其性质进行研究。结果表明：该酶分子质量为80．5kD。最适反应温度为55-60℃，pH值为7-9。金属蛋白酶抑制剂（EDTA）可以完全抑制该酶的活性。Mn^2＋、Ca^2＋、Mg^2＋对OP-I有激活作用，酶促动力学研究显示其米氏常数量‰为0．…查看全部>>
An electrophoretically pure protease, named as OP-I, was obtained from the digestive tract of Octopus vulgaris by ammonium sulfate precipitation, cellulose CM-52 cation-exchange chromatography, DEAE-Sephadex A50 anion-exchange chromatography and SDS-PAGE. Its properties were also characterized. The results showed that the molecular weight of the protease was 80.5 kD and its optimal reaction temperature and pH were 55 - 60 ℃and 7 - 9, respectively. OP-I could…查看全部>>
任佩;王莹;金玉兰;朴美子
青岛农业大学食品科学与工程学院,山东青岛266109青岛农业大学食品科学与工程学院,山东青岛266109青岛农业大学化学与药学院,山东青岛266109青岛农业大学食品科学与工程学院,山东青岛266109
轻工纺织
章鱼蛋白酶纯化性质
Octopus vulgarisproteasepurificationcharacterization
《食品科学》 2012 (7)
168-171,4
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