从产琥珀酸拟杆菌中分离出纤维二糖酶。
Isolation of a Cellodextrinase from Bacteroides succinogenes.
机构信息
Department of Microbiology, University of Guelph, Guelph, Ontario N1G 2W1, Canada.
出版信息
Appl Environ Microbiol. 1987 May;53(5):1034-41. doi: 10.1128/aem.53.5.1034-1041.1987.
Abstract
An enzyme which released the cellobiose group from p-nitrophenyl cellobioside was isolated from the periplasmic space of Bacteroides succinogenes grown on Avicel crystalline cellulose in a continuous cultivation system and separated from endoglucanases by column chromatography. The molecular weight of the enzyme was approximately 40,000, as estimated by gel filtration. The enzyme has an isoelectric point of 4.9. The enzyme exhibited low hydrolytic activity on acid-swollen cellulose and practically no activity on carboxymethyl cellulose, Avicel cellulose, and cellobiose, but it hydrolyzed p-nitrophenyl lactoside and released cellobiose from cellotriose and from higher cello-oligosaccharides. These data demonstrate that the enzyme is a cellodextrinase with an exotype of function.
摘要
从在连续培养系统中以结晶纤维素 Avicel 为底物生长的拟杆菌 succinogenes 的周质空间中分离出一种能够从对硝基苯纤维二糖苷释放纤维二糖单元的酶，并通过柱层析将其与内切葡聚糖酶分离。该酶的分子量约为 40000，通过凝胶过滤估计。该酶的等电点为 4.9。该酶对酸膨胀纤维素表现出低水解活性，对羧甲基纤维素、Avicel 纤维素和纤维二糖几乎没有活性，但它水解对硝基苯乳糖，并从纤维三糖和更高的纤维寡糖中释放纤维二糖。这些数据表明，该酶是一种具有外切型功能的纤维二糖酶。
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