Purification and biochemical characterization of a transglucosilating beta-glucosidase of Stachybotrys strain (original) (raw)

Applied microbiology and biotechnology, 2007

Abstract

The filamentous fungus Stachybotrys sp has been shown to possess a rich beta-glucosidase system composed of five beta-glucosidases. One of them was already purified to homogeneity and characterized. In this work, a second beta-glucosidase was purified and characterized. The filamentous fungal A19 strain was fed-batch cultivated on cellulose, and its extracellular cellulases (mainly beta-glucosidases) were analyzed. The purified enzyme is a monomeric protein of 78 kDa molecular weight and exhibits optimal activity at pH 6.0 and at 50 degrees C. The kinetic parameters, K (m) and V (max), on para-nitro-phenyl-beta-D: -glucopyranosid (p-NPG) as a substrate were, respectively, 1.846 +/- 0.11 mM and 211 +/- 0.08 micromol min(-1) ml(-1). One interesting feature of this enzyme is its high stability in a wide range of pH from 4 to 10. Besides its aryl beta-glucosidase activity towards salicin, methylumbellypheryl-beta-D: -glucoside (MU-Glc), and p-NPG, it showed a true beta-glucosidase activ...

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