Thermophilic enzymes have many potential benefits in industrial production with increased flexibility related to process configurations. A thermostable β-glucosidase from Thermotoga naphthophila RUK-10 was found to possess catalytic activity for cellobiose hydrolysis with a high potential for application in biomass conversion. The aggregation of cellobiose often has an inhibitory effect on cellobiohydrolases and endoglucanases during cellulose hydrolysis. The presence of β-glucosidases has a significant effect on reducing inhibition from hydrolytic products by hydrolysing the intermedia cellobiose. In this study, β-glucosidase TN0602 exhibited a high tolerance to glucose and high thermostability even after a long incubation (>72 h). Additionally, supplementing β-glucosidase TN0602 with microcrystalline cellulose, untreated corn straw and steam-exploded corn straw hydrolysis reactions containing a commercial cellulase led to an increased conversion rate in released glucose compared to hydrolysis without the addition of β-glucosidase (15.82, 30.62 and 35.21%, respectively); the increase of conversion rates were 61.86, 93.50 and 94.55%. It was thus shown that an obvious synergistic effect exists between TN0602 and cellulases for cellulose hydrolysis, suggesting its potential as a component of enzymatic cocktails for the conversion of lignocellulosic biomass to other chemicals.
Keywords: Cellulase; Glucose tolerance; Intermedia inhibition; β-Glucosidase.