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从船蛆分离出的一种新型细菌的胞外内切葡聚糖酶活性

Extracellular endoglucanase activity by a novel bacterium isolated from marine shipworm.

作者信息

Griffin H L, Freer S N, Greene R V

出版信息

Biochem Biophys Res Commun. 1987 Apr 14;144(1):143-51. doi: 10.1016/s0006-291x(87)80487-4.

DOI:10.1016/s0006-291x(87)80487-4
PMID:3579899
Abstract

An extracellular enzyme preparation from shipworm bacterium cultures dramatically increased reducing sugar content of carboxymethylcellulose (CMC3), but did not solubilize sugar from particulate cellulose. The preparation degraded cellodextrins larger than cellotriose (G3). Only interior cellodextrin chain linkages were cleaved and the center-most bond of cellohexaose (G6) was preferentially cleaved. Activity maxima were observed at 60 degrees C and between pH 5.0 and 7.0. The activity was resistant to protease treatment and little loss of activity was observed after 14 d at 25 degrees C.

摘要

船蛆细菌培养物的一种胞外酶制剂显著提高了羧甲基纤维素(CMC3)的还原糖含量,但不能使颗粒状纤维素中的糖溶解。该制剂能降解大于纤维三糖(G3)的纤维糊精。仅内部纤维糊精链连接被切断,纤维六糖(G6)的最中间键被优先切断。在60摄氏度以及pH值5.0至7.0之间观察到活性最大值。该活性对蛋白酶处理具有抗性,在25摄氏度下放置14天后活性几乎没有损失。

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Appl Environ Microbiol. 1993 May;59(5):1259-63. doi: 10.1128/aem.59.5.1259-1263.1993.
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Production of an endoglucanase by the shipworm bacterium, Teredinobacter turnirae.
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J Ind Microbiol Biotechnol. 2004 Jan;31(1):41-7. doi: 10.1007/s10295-004-0113-1. Epub 2004 Jan 24.