Abstract
Kinetic properties of extracellular β-glucosidase from Aspergillus ornatus were determined. The pH and temperature optima for the enzyme were found to be 4.6 and 60°C, respectively. Under these conditions, the enzyme exhibited a Km (p-nitrophenyl-β-glucoside) value of 0.76±0.11 mM. The activation energy for the enzyme was 11.8 kcal/mol. Several divalent metal ions inhibited β-glucosidase activity, some of which showed inhibition of enzyme activity only at higher concentrations. Ag2+ was the most potent inhibitor. A metal chelating agent, EDTA, also inhibited β-glucosidase activity. Except for trehalose, glucose, glucono-δ-lactone, cellobiose, gentiobiose, laminaribiose, maltose and isomaltose inhibited β-glucosidase activity. Glucose was found to be a competitive inhibitor, whereas glucono-δ-lactone and other β-linked disaccharides were noncompetitive (mixed) inhibitors of the enzyme.
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