[Purification and some properties of extracellular beta-glucosidase from Rhizopus japonicus IFO5318].
The beta-glucosidase from Rhizopus japonicus IFO5318 was purified by Ammonium sulfate salting out and column chromatographies with the recovery of 22%. The molecular weight of the enzyme was about 4.0 x 10(5), consisting of four identical subunits; The optimum reaction temperature and pH for the beta-glucosidase were 55 degrees C and pH 5.5, respectively; While the enzyme was sensitive to heat, it could be stable at a wide range of pH. The Km and Vmax values of the enzyme were 0.825 mg.ml-1 and 135.4 mumol.min-1.mg-1, respectively, using p-Nitrophenyl-beta-D-glucopyranoside as a substrate. The beta-glucosidase exhibited strongest hydrolysis effect on cellobiose and some of its activity could be inhibited by SDS, Fe3+ and Hg2+.
Chen
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X
College of Life Sciences, Wuhan University, Wuhan 430072.
Fujio
Y
Y
D008970:Molecular Weight; D012233:Rhizopus / Q000737:chemistry*; D001617:beta-Glucosidase / Q000737:chemistry / Q000302:isolation & purification*
D001617:beta-Glucosidase