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嗜热栖热梭菌纤维素结合酶的亲和纯化

Affinity purification of cellulose-binding enzymes of Clostridium stercorarium.

作者信息

Bronnenmeier K, Adelsberger H, Lottspeich F, Staudenbauer W L

机构信息

Lehrstuhl für Mikrobiologie, Technische Universität München, Germany.

出版信息

Bioseparation. 1996 Feb;6(1):41-5.

PMID:8987526
Abstract

Cellulose-affinity chromatography proved to be a fast and efficient purification procedure for exoenzymes of the thermophilic anaerobe Clostridium stercorarium, suitable for the preparation of large amounts of enzymes for technical applications. The cellulose-binding enzymes could be identified as the C. stercorarium; cellulolytic enzymes Avicelase I and Avicelase II characterized previously as endo-1,4-beta-glucanase and exo-1,4-beta-glucanase. A third protein was identified as xylanase A, the major endo-1,4-beta-xylanase of this organism.

摘要

纤维素亲和层析被证明是一种用于嗜热厌氧菌粪堆梭菌外切酶的快速高效纯化方法,适用于制备大量用于技术应用的酶。纤维素结合酶可鉴定为粪堆梭菌的纤维素分解酶纤维二糖水解酶I和纤维二糖水解酶II,先前被表征为内切-1,4-β-葡聚糖酶和外切-1,4-β-葡聚糖酶。第三种蛋白质被鉴定为木聚糖酶A,是该生物体的主要内切-1,4-β-木聚糖酶。

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Affinity purification of cellulose-binding enzymes of Clostridium stercorarium.嗜热栖热梭菌纤维素结合酶的亲和纯化
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The modular cellulase CelZ of the thermophilic bacterium Clostridium stercorarium contains a thermostabilizing domain.嗜热细菌粪堆梭菌的模块化纤维素酶CelZ含有一个热稳定结构域。
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Nucleotide sequence of the Clostridium stercorarium xynA gene encoding xylanase A: identification of catalytic and cellulose binding domains.编码木聚糖酶A的粪堆梭菌xynA基因的核苷酸序列:催化结构域和纤维素结合结构域的鉴定
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CelG from Clostridium cellulolyticum: a multidomain endoglucanase acting efficiently on crystalline cellulose.来自解纤维梭菌的CelG:一种对结晶纤维素具有高效作用的多结构域内切葡聚糖酶。
J Bacteriol. 1997 Nov;179(21):6595-601. doi: 10.1128/jb.179.21.6595-6601.1997.