PROPERTIES OF A GENETICALLY RECONSTRUCTED PREVOTELLA-RUMINICOLA ENDOGLUCANASE

被引：50

作者：

MAGLIONE, G

MATSUSHITA, O

RUSSELL, JB

WILSON, DB

机构：

[1] CORNELL UNIV, DIV BIOL SCI, BIOCHEM MOLEC & CELL BIOL SECT, ITHACA, NY 14853 USA

[2] CORNELL UNIV, DIV BIOL SCI, MICROBIOL SECT, ITHACA, NY 14853 USA

[3] USDA ARS, ITHACA, NY 14853 USA

来源：

APPLIED AND ENVIRONMENTAL MICROBIOLOGY | 1992年 / 58卷 / 11期

关键词：

D O I：

10.1128/AEM.58.11.3593-3597.1992

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

A pUC19-derived plasmid was constructed that coded for a hybrid cellulase with the Thermomonospora fusca E2 cellulose-binding domain at its C terminus joined to the Prevotella ruminicola 40.5-kDa carboxymethyl cellulase (CMCase). The hybrid enzyme was purified and characterized enzymatically. It bound tightly to cellulose, and its specific activities on carboxymethyl cellulose, amorphous cellulose, and ball-milled cellulose were 1.5, 10, and 8 times that of the 40.5-kDa CMCase, respectively. Furthermore, the modified enzyme gave synergism with an exocellulase in the degradation of filter paper, while the 40.5-kDa CMCase did not.

引用

页码：3593 / 3597

页数：5

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