Purification and biochemical characteristics of beta-glucosidase from Aspergillus awamori K-1

• Published in: Biotechnology, biotechnological equipment Vol. 16; no. 1; pp. 83 - 90
• Main Authors: Petrova, S, Andreev, A, Bakalova, N, Benadova, R, Kolev, D. (University of Sofia "St. Kliment Ohridski", Sofia (Bulgaria))
• Format: Journal Article
• Language: English
• Published: Taylor & Francis 2002
• Subjects: ACTIVIDAD ENZIMATICA; ACTIVITE ENZYMATIQUE; ASPERGILLUS AWAMORI; BETA GLUCOSIDASA; BETA GLUCOSIDASE; BIOCHEMISTRY; BIOCHIMIE; BIOQUIMICA; ENZYME ACTIVITY; PURIFICACION; PURIFICATION
• ISSN: 1310-2818; 1314-3530
• DOI: 10.1080/13102818.2002.10819160

An extracellular β-glucosidase (β-D-glucoside glucohydrolase, EC 3.2.1.21) produced by Aspergillus awamori K-1 was purified to electrophoretic homogeneity. The purified enzyme, which had a glycoprotein nature, was a monomer with a relative molecular mass of 116 kDa and pI= 5.8. The β-glucosidase was the most active against aryl-β-glucosides and cellobiose. In addition, the enzyme was able to catalyze the hydrolysis of β-1→2 and β-1 →6-linked diglucosides. The apparent K m and V values for p-nitrophenyl-β-D-gluco-pyranoside were calculated to be 0.8 mM and 5.29 μmol.min −1 respectively. Maximal β- glucosidase activity occurred at 60 °C and pH 5.0. This enzyme was competitively inhibited by β-D-glucose with K 1 value of 13.15 mM.