Structural characteristics comparison of β-glucosidase enzyme in insects

Beta-glucosidase (βglu) is widespread in all plants, animals, fungi and bacteria. βglu catalyzes the hydrolysis of β-1,4 bonds to terminal non-reducing residues in beta-D-glucosides and oligosaccharides, with release of glucose. Thus these enzymes are named based on the released monosaccharides. In current research, the bioinformatics analysis of βglu was performed in thirteen different insect species from different families. The primary and secondary structural analyses of thirteen species of insects were investigated by ProtParam and SOPMA tools. TMHMM and SignalP server were used to identify transmembrane domains and signal peptide in each species, respectively. The number of amino acids, isoelectric point, molecular weight, instability index, GRAVY and aliphatic index were identified in each sample and compared with each other. According to the results, none of the species had transmembrane domain but Trachymyrmex cornetzi. Also signal peptide just was observed in Acyrthosiphon pisum, Bombyx mori and Cephus cinctus. Based on the structural analysis, there are a lot of similarities among βglu protein in different insect species; however there were some differences among some insects. The obtained data provides background of digestive enzyme studies like βglu and their structural identification in insects.