Production, immobilization and characterization of beta-glucosidase for application in cellulose degradation from a novel Aspergillus versicolor.

Beta-glucosidase (EC 3.2.1.21) catalyzes the hydrolysis of cellobiose and cellooligosaccharides containing (1 → 4)-beta-glycosidic bonds to glucose, which is crucial in cellulosic ethanol production. In this study, Aspergillus versicolor, a novel highly productive beta-glucosidase strain, was first isolated from Camptotheca acuminata seeds. The highest beta-glucosidase activity with 812.86 U/mL was obtained by using the response surface methodology, and a 14.4-fold has increased compared to the control. The beta-glucosidase was then purified to homogeneity with recovery yield and specific activity of 25.98% and 499.15 U/mg, respectively. To enhance its stability and recyclability, the purified beta-glucosidase was first immobilized onto magnetic MnO by electrostatic adsorption. The immobilized materials were characterized by FR-IT, TEM and FE-SEM. Compared with the free beta-glucosidase, the immobilized enzyme exhibited enhanced thermal stability (1.5-fold raise in half-life at 50 °C), and reusability (holding over 60% activity after eight cycles), besides, the optimum pH has increased to 6.0. Substrate specificity research suggested that the enzyme had high hydrolytic activity on cellobiose. It also had a hydrolysis effect on (1 → 3) and (1 → 6)-beta-glycosidic linkages. Application trials in cellulose hydrolysis revealed that the immobilized enzyme was comparatively more effective. Our results suggested this novel immobilized beta-glucosidase makes a promising alternative for the cellulosic ethanol production.