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首页> 外文期刊>Journal of bacteriology >Mode of Action of Pectic Enzymes II. Further Purification of Exopolygalacturonate Lyase and Pectinesterase from Clostridium multifermentans
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Mode of Action of Pectic Enzymes II. Further Purification of Exopolygalacturonate Lyase and Pectinesterase from Clostridium multifermentans

机译:果胶酶的作用方式II。从多发酵梭菌中进一步纯化外半乳糖醛酸裂合酶和果胶酯酶

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摘要

Exopolygalacturonate lyase and pectinesterase from Clostridium multifermentans were purified 156-fold and 178-fold, respectively, by gel filtration chromatography on Sephadex G-200. The activities of both enzymes coincided in a single protein peak. Profiles of the two activities also coincided in diethylaminoethyl-cellulose chromatography and zonal centrifugation. These studies indicated that the esterase and the lyase were either complexed or similar molecular species. The former seems more probable because of the relatively high molecular weight. Both activities were most stable at pH 6.0. The esterase was inactivated rapidly at pH 5 or 7. Lyase preparations were freed of pectinesterase activity by heating for 30 min at 38 C and pH 7.0.
机译:在琼脂糖凝胶G-200上通过凝胶过滤色谱分别纯化了多发酵菌中的外半乳糖醛酸裂合酶和果胶酯酶,分别纯化了156倍和178倍。两种酶的活性在单个蛋白质峰中重合。在二乙氨基乙基纤维素色谱法和分区离心中,这两种活性的概况也一致。这些研究表明酯酶和裂解酶是复合的或相似的分子种类。由于分子量较高,前者似乎更有可能。两种活性在 p H 6.0时最稳定。酯酶在 p H 5或7处迅速失活。在38°C和 p H 7.0加热30分钟,裂解酶制剂没有果胶酯酶活性。

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