β-glucanases are industrially significant glycosyl hydrolases which hydrolyze the glycosidic bonds in insoluble or partially soluble β-glucan molecules by acting as exo- and endo-hydrolases. Molecular characterization and structural elucidation are vital for uncovering the structural and functional relationship of β-glucan degrading enzymes. In the present study, full-length gene sequences of exo-β-1,4-glucanase (EXO-14) and endo-β-1,3-glucanase (ENDO-13), isolated from Streptomyces althioticus TBG-MR17 and Streptomyces cinereoruber subsp. cinereoruber TBG-AL13, respectively, were obtained. The primary sequence analysis and sequence based structural analysis were performed in silico. The obtained 1737 bp EXO14 gene and 1293 bp ENDO13 gene encoded 578 and 438 putative amino acids, respectively. The in silico functional domain predictions showed a multi-domain architecture of both enzymes and showed diverse physiochemical properties. The substrate binding analysis through molecular docking delivered the possible architecture of active sites, the tunnel type in EXO-14 prominently cleaves external β-1,4- linkages and open cleft like structure in ENDO-13 has more propensity to cut internal bonds. Overall, the results generate valuable information for continuing the understanding of β-glucanase enzymes especially from Streptomyces spp., and provide significance for upgrading their catalytic properties through enzyme engineering.
Key words: CAZyme families, dbCAN annotation, Superimposition, Molecular docking
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