Characterization of Three Extracellular β-Glucosidases Produced by a Fungal Isolate sp. YDJ14 and Their Hydrolyzing Activity for a Flavone Glycoside.

J Microbiol Biotechnol

Department of Pharmacy, and Research Institute of Life Pharmaceutical Sciences, Sunchon National University, Suncheon 57922, Republic of Korea.

Published: May 2018

A cellulolytic fungus, YDJ14, was isolated from compost and identified as an sp. strain. Three extracellular β-glucosidases, BGL-A1, BGL-A2, and BGL-A3, were separated using ultrafiltration, ammonium sulfate fractionation, and High-Q chromatography. The molecular masses of the three enzymes were estimated to be 100, 45, and 40 kDa, respectively, by SDS-PAGE. The optimum pH and temperature of BGL-A3 were 5.0 and 50°C, respectively, whereas the optimum pH and temperature of BGL-A1 and BGL-A2 were identical (4.0 and 60°C, respectively). The half-life of BGL-A3 at 70°C (2.8 min) was shorter than that of BGL-A1 and BGL-A2 (12.1 and 8.8 min, respectively). All three enzymes preferred -nitrophenyl-β--glucopyranoside (NPG) and hardly hydrolyzed cellobiose, suggesting that these enzymes were aryl β-glucosidases. The of BGL-A3 (1.26 mM) for NPG was much higher than that of BGL-A1 and BGL-A2 (0.25 and 0.27 mM, respectively). These results suggested that BGL-A1 and BGL-A2 were similar in their enzymatic properties, whereas BGL-A3 differed from the two enzymes. When tilianin (a flavone glycoside of acacetin) was reacted with the three enzymes, the inhibitory activity for monoamine oxidase, a target in the treatment of neurological disorders, was similar to that shown by acacetin. We conclude that these enzymes may be useful in the hydrolysis of flavone glycosides to improve their inhibitory activities.

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http://dx.doi.org/10.4014/jmb.1802.02051DOI Listing

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