Molecular Dynamics Analysis of Glucose Oxidase Stability against Temperature

Abstract

Glucose oxidase (GOD) from local isolated Aspergillus niger IPBCC.08.610 shows a widespread application, specifically as a bioanode in glucose-based biofuel cells. Enzymes with adequate thermal stability are necessary for enhancing product efficiency. Also, evaluating the structural dynamics to improve temperature helps to determine the residue. The molecular dynamics simulation of GOD_IPBCC_1CF3 at temperatures of 300, 400, and 500 K was carried out to analyze important amino acid residues for thermal stability. The results showed that the amino acid residues responsible for thermal stability were dispersed into several essential regions, including D576 at the C terminal, E266-R250, and E38-R237 in the FAD-binding domain E485-R470 in the substrate-binding antiparallel beta system. However, the FAD molecular flexibility against temperature depends on conserve E48 by stabilizing the ribose sugar moiety.