In Silico Approaches to Reveal Structural Insights, Stability and Catalysis of Bacillus-Derived α-Amylases Prior to Advance Lab Experiments

Abstract

[Formula: see text]-amylase is the most widely used Glycoside Hydrolase (GH) in industries for decades. It randomly cleaves the [Formula: see text]-D-(1, 4) glucosidic bonds of [Formula: see text]-polysaccharides (starch and glycogen) to release glucose and short-chain oligosaccharides. Substantial advances have taken place in research related to [Formula: see text]-amylases. However, bioinformatics study needs a little more exploration before conducting wet-lab experiments. We aimed to perform a comparative structure-function relationship study of 10 different Bacillus-derived [Formula: see text]-amylases using several computational biology tools. After aligning all the [Formula: see text]-amylases, 3D structures were made using the SWISS-MODEL. The accuracy and stability of the predicted models were validated via different web servers like Verify-3D, ERRAT, RMSD and ProSA. MolProbity and PROCHECK were used for mapping the residues in the most favored region of the Ramachandran plot. The Ramachandran plot reveals that [Formula: see text] of the amino acid residues of the selected [Formula: see text]-amylase genes lie within the favored region. Our findings suggest that all the [Formula: see text]-amylases were stable as per the validation results we got. The study has revealed clear and concise structural related aspects. This paper will encourage the researchers to include and prioritize in silico work of [Formula: see text]-amylase genes to obtain more accurate outcomes. As the output obtained in this study via in silico tools reveals the structural peculiarity and more about the catalytic domain impression, it highly recommends incorporating such studies for better results. This approach will save efforts, costs and time for researchers.