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Abstract
Aspergillus unguis NII-08123, a filamentous fungus isolated from soil, was found to produce β-glucosidase (BGL) activity with high glucose tolerance. Cultivation of the fungus in different carbon sources resulted in the secretion of different isoforms of the enzyme. A low molecular weight isoform, which retained ~60 % activity in the presence of 1.5 M glucose, was purified to homogeneity and the purified enzyme exhibited a temperature and pH optima of 60 °C and 6, respectively. The K m and V max of the enzyme were 4.85 mM and 2.95 U/mg, respectively, for 4-nitrophenyl β-d-glucopyranoside. The glucose inhibition constant of the enzyme was 0.8 M, indicating high glucose tolerance, and this is the second-highest glucose tolerance ever reported from the Aspergillus nidulans group. The glucose-tolerant BGL from A. unguis, when supplemented to cellulase preparation from Penicillium, could improve biomass hydrolysis efficiency by 20 % in 12 h compared to the enzyme without additional beta glucosidase supplementation. The beta glucosidase from A. unguis is proposed as a highly potent “blend-in” for biomass saccharifying enzyme preparations.
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