Isolation and properties of beta-glucosidase from Ruminococcus albus.
An enzyme active against p-nitrophenyl-beta-D-glucoside was purified from logarithmic-phase cells of Ruminococcus albus cultivated in a medium containing ball-milled cellulose. The purification yielded homogeneous enzyme after an approximately 520-fold increase in specific activity and a 9% yield. The enzyme was identified as a beta-glucosidase because it can hydrolyze cellobiose and cellooligosaccharides to glucose from the nonreducing ends.
D002413:Cations, Divalent; D002475:Cellobiose / Q000378:metabolism; D004789:Enzyme Activation; D005947:Glucose / Q000378:metabolism; D005959:Glucosidases / Q000378:metabolism*; D005960:Glucosides / Q000378:metabolism; D007700:Kinetics; D008970:Molecular Weight; D010459:Peptococcaceae / Q000201:enzymology*; D001617:beta-Glucosidase / Q000302:isolation & purification / Q000378:metabolism*
D002413:Cations, Divalent; D005960:Glucosides; D002475:Cellobiose; C025193:4-nitrophenyl beta-D-glucoside; C034170:4-nitrophenyl beta-cellobioside; D005959:Glucosidases; D001617:beta-Glucosidase; D005947:Glucose