Properties of a genetically reconstructed Prevotella ruminicola endoglucanase.
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.
Maglione
G
G
Section of Biochemistry, Molecular and Cell Biology, Cornell University, Ithaca, New York.
Matsushita
O
O
Russell
J B
JB
Wilson
D B
DB
D000192:Actinomycetales / Q000201:enzymology / Q000235:genetics; D001439:Bacteroides / Q000201:enzymology* / Q000235:genetics*; D001483:Base Sequence; D002266:Carboxymethylcellulose Sodium / Q000378:metabolism; D002480:Cellulase / Q000235:genetics*; D002482:Cellulose / Q000378:metabolism; D006026:Glycoside Hydrolases / Q000235:genetics; D008969:Molecular Sequence Data; D011994:Recombinant Proteins; D013379:Substrate Specificity
D011994:Recombinant Proteins; D002482:Cellulose; D006026:Glycoside Hydrolases; D002480:Cellulase; C019826:carboxymethylcellulase; D002266:Carboxymethylcellulose Sodium