VISUALIZATION OF THE ADSORPTION OF A BACTERIAL ENDO-BETA-1,4-GLUCANASE AND ITS ISOLATED CELLULOSE-BINDING DOMAIN TO CRYSTALLINE CELLULOSE

被引：52
作者：
GILKES, NR
KILBURN, DG
MILLER, RC
WARREN, RAJ
SUGIYAMA, J
CHANZY, H
HENRISSAT, B
机构：
[1] JOSEPH FOURIER UNIV GRENOBLE, CTR RECH MACROMOLEC VEGETALES, CNRS, BP 53 X, F-38041 GRENOBLE, FRANCE
[2] UNIV BRITISH COLUMBIA, DEPT MICROBIOL, VANCOUVER V6T 1Z3, BC, CANADA
[3] UNIV TOKYO, FAC AGR, DEPT FOREST PROD, BUNKYO KU, TOKYO 113, JAPAN
来源：
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES | 1993年 / 15卷 / 06期
关键词：
ADSORPTION; CELLULASE; COLLOIDAL GOLD LABELING; ELECTRON MICROSCOPY; FLOCCULATION; MICROCRYSTALLINE CELLULOSE;
D O I：
10.1016/0141-8130(93)90052-N
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
Endo-beta-1,4-glucanase A (CenA), a cellulase from the bacterium Cellulomonas fimi, is composed of two domains: a catalytic domain and a cellulose-binding domain. Adsorption of CenA and its isolated cellulose-binding domain (CBD-PT(CenA)) to Valonia cellulose microcrystals was examined by transmission electron microscopy using an antibody sandwich technique (CenA/CBD.PT(CenA)-alphaCenA IgG-protein A-gold conjugate). Adsorption of both CenA and CBD-PT(CenA) occurred along the lengths of the microcrystals, with an apparent preference for certain crystal faces or edges. CenA or CBD.PT(CenA), but not the isolated catalytic domain, were shown to prevent the flocculation of microcrystalline bacterial cellulose. The cellulose-binding domain may assist crystalline cellulose hydrolysis in vitro by promoting substrate dispersion.
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收藏
页码：347 / 351
页数：5
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