Improving enzymatic efficiency of β-glucosidases in cellulase system by altering its binding behavior to the insoluble substrate during bioconversion of lignocellulose.

The enzymatic efficiency of β-glucosidases is influenced by their binding behavior onto insoluble substrates (cellulose and lignin) during bioconversion of lignocellulose. This study suggested that the Bgl3 protein (Aspergillus fumigatus) showed strong adsorption affinity to lignin and the Bgl1 protein (Penicillium oxalicum) tended to adsorb to cellulose. It indicated that the various surface properties of the fibronectin type Ш-like domain (FnIII) led to different binding properties of β-glucosidases by investigating their binding mechanism. By engineering β-glucosidases' FnIII domain, Bgl3-1 and Bgl1-3 were constructed, which both showed lower binding capacities to insoluble substrates. As well as for Bgl1-3, its sensitivity to the phenolic component was also eased. Based on that, the reconstructed protein showed high catalytic efficiency during the enzymatic hydrolysis of corn stover by effectively transforming cellobiose to glucose. Thus, this study provided a new strategy to engineer β-glucosidases to enhance their performance in the cellulase system.