β‐Glucosidase produced by <i>Moniliophthora perniciosa</i>: Characterization and application in the hydrolysis of sugarcane bagasse
Larissa Emanuelle da Silva Almeida, Geise Camila de Araujo Ribeiro, Sandra Aparecida de Assis
Abstract
Abstract β‐Glucosidases (BGLs) belong to the group of enzymes of cellulases and act in the last stage of cellulose degradation, releasing glucose molecules, eliminating the inhibitory effect of cellobiose. This study focused on the production, characterization, and application of BGL from Moniliophthora perniciosa in the hydrolysis of pretreated sugarcane bagasse (3% NaOH + 6% Na 2 SO 3 ), with varying enzymatic loads and reaction times. The enzyme showed an optimum pH of 4.5 and 60°C. It was stable at all temperatures analyzed (50–90°C) and retained about 100% of its activity at 50°C after 60 min of incubation. Among the ions analyzed, BaCl 2 increased BGL activity 9.04 ± 1.41 times. The maximum production of reducing sugars (89.15%) was achieved after 48 h with 10 mg of protein.