Purification of the beta-glucosidase from Sclerotinia sclerotiorum.
A beta-glucosidase (EC 3.2.1.21) has been isolated from culture filtrates of the fungus Sclerotinia sclerotiorum. The protein was purified by gel filtration on a column of Bio-Gel P-300 and by ion exchange chromatography on DEAE-Bio-Gel A. The molecular weight, determined by gel filtration, was 240,000. Km values for the enzyme towards p-nitrophenyl-beta-D-glucoside and cellobiose were respectively 0.10 mM and 1.23 mM. The beta-glucosidase activity was found to be strongly associated with a beta-xylosidase (EC 3.2.1.37) activity, suggesting that both activities could be represented in a single protein complex.
D001203:Ascomycota / Q000201:enzymology*; D002475:Cellobiose / Q000378:metabolism; D002850:Chromatography, Gel; D005959:Glucosidases / Q000302:isolation & purification*; D005960:Glucosides / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008970:Molecular Weight; D013696:Temperature; D014995:Xylosidases / Q000378:metabolism; D001617:beta-Glucosidase / Q000302:isolation & purification*
D005960:Glucosides; D002475:Cellobiose; C025193:4-nitrophenyl beta-D-glucoside; D005959:Glucosidases; D014995:Xylosidases; D001617:beta-Glucosidase; C026579:exo-1,4-beta-D-xylosidase