Visualization of the adsorption of a bacterial endo-beta-1,4-glucanase and its isolated cellulose-binding domain to crystalline cellulose.
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.PTCenA) to Valonia cellulose microcrystals was examined by transmission electron microscopy using an antibody sandwich technique (CenA/CBD.PTCenA-alpha CenA IgG-protein A-gold conjugate). Adsorption of both CenA and CBD.PTCenA occurred along the lengths of the microcrystals, with an apparent preference for certain crystal faces or edges. CenA or CBD.PTCenA, 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.
Gilkes
N R
NR
Department of Microbiology, University of British Columbia, Vancouver, Canada.
Kilburn
D G
DG
Miller
R C
RC
Warren
R A
RA
Sugiyama
J
J
Chanzy
H
H
Henrissat
B
B
D000192:Actinomycetales / Q000201:enzymology*; D001419:Bacteria / Q000201:enzymology*; D001665:Binding Sites; D002480:Cellulase / Q000737:chemistry / Q000378:metabolism*; D002482:Cellulose / Q000737:chemistry / Q000378:metabolism*; D003460:Crystallization; D008854:Microscopy, Electron
D002482:Cellulose; D002480:Cellulase