Partial Purification and Characterization of Armillaria melleaβ-Glucosidase

Abstract

A β-glucosidase from Armillaria mellea, an edible mushroom collected from Hıdırnebi High Plateau (Trabzon, Turkey), was partially purified 41.1-fold by using ion-exchange chromatography and it was biochemically characterized. The enzyme exhibited maximum activity at pH 4.0 and 50°C when p-nitrophenyl-β-D-glucopyranoside was used as a substrate. K_m and V_max values were calculated as 0.3 mM and 3.6 U/mg protein, respectively. A. mellea β-glucosidase was quite stable in the range of pH 3.0–6.0 and 8.0 after 24 h of incubation at 4°C. It was determined that the enzyme was extremely stable in the range of 20–50°C after 1 h incubation. It was also determined that some metal ions and chemicals affected the enzyme activity in different ratios.

Keywords:

• Armillaria mellea
• Mushroom
• β-Glucosidase
• Ion-exchange chromatography
• Characterization

ACKNOWLEDGEMENTS

The authors wish to thank KTU-BAP (Project number 2009.111.02.7) for financial support and Associate Professor Dr. Dursun Yagiz (Selçuk University, Education Faculty, Konya, Turkey) for identifying the mushroom.