Characterization of a novel thermostable α-amylase from Calothrix sp. using in silico approaches

Abstract

Cyanobacteria, photoautotrophic microorganisms found in diverse environments, are promising producers of bioactive compounds with industrial applications. Among these, α-Amylases hydrolyze α(1,4) glycosidic bonds in starch, generating fermentable monomers for bioprocesses. This study used computational approaches to identify and characterize potentially thermostable α-Amylases from cyanobacterial sequences from a public database. The protein Amy1 was identified and analyzed through structural modeling, sequence comparison, molecular dynamics simulations, and binding free energy calculations to assess protein-ligand interactions. Molecular dynamics at 27 °C and 50 °C were conducted to evaluate putative enzyme stability, guiding experimental validation of thermostability. These studies were carried out to ensure accuracy for experimental tests, which are important to confirm this thermostable characteristic. These findings highlight cyanobacterial alpha-amylase characteristics as viable alternatives to commercial equivalents and pave the way for future biotechnological applications and large-scale production.