In Silico Analysis of a GH3 fi-Glucosidase from Microcystis aeruginosa CACIAM 03

Cyanobacteria are rich sources of secondary metabolites and have the potential to be excellent industrial enzyme producers. beta-glucosidases are extensively employed in processing biomass degradation as they mediate the most crucial step of bioconversion of cellobiose (CBI), hence controlling the efficiency and global rate of biomass hydrolysis. However, the production and availability of these enzymes derived from cyanobacteria remains limited. In this study, we evaluated the beta-glucosidase from Microcystis aeruginosa CACIAM 03 (MaBgl3) and its potential for bioconversion of cellulosic biomass by analyzing primary/secondary structures, predicting physicochemical properties, homology modeling, molecular docking, and simulations of molecular dynamics (MD). The results showed that MaBgl3 derives from an N-terminal domain folded as a distorted beta-barrel, which contains the conserved His-Asp catalytic dyad often found in glycosylases of the GH3 family. The molecular docking results showed relevant interactions with Asp81, Ala271 and Arg444 residues that contribute to the binding process during MD simulation. Moreover, the MD simulation of the MaBgl3 was stable, shown by analyzing the root mean square deviation (RMSD) values and observing favorable binding free energy in both complexes. In addition, experimental data suggest that MaBgl3 could be a potential enzyme for cellobiose-hydrolyzing degradation.

Automated summary

In this study, the beta-glucosidase from Microcystis aeruginosa CACIAM 03 (MaBgl3) was evaluated for its potential in cellulosic biomass bioconversion. The results showed that MaBgl3 is a stable enzyme with favorable binding free energy, making it suitable for cellulose hydrolysis.