α-Amylase is used in many industrial processes to breakdown carbohydrates into simple sugars that can be further manipulated and/or utilized. Certain bacteria derived α-amylase enzymes are known to maintain native protein folding conformation under extreme temperature conditions. Bacillus licheniformis α-amylase (BLA), bacillus amyloliquefaciens α-amylase (BAA), and Bacillus stearothermophilus α-amylase (BSA) are bacteria based amylase enzymes that are structurally similar but have differences in melting point. In order to investigate the structural factors that contribute to the differing thermal stability of these α-amylases, we used classical molecular dynamics simulations (MD) to model each enzyme. We simulated the protein dynamics at physiological and increased temperatures and saved the resulting trajectories. We present the analysis of the structural variations between enzymes at increasing temperatures to elucidate the unfolding patterns and contributing enzyme structural elements.

Investigating the thermal-stability of bacteria based alpha-amylases with molecular dynamics

255th National Meeting (2018)

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