Mutational Analysis Of Resveratrol-Cleaving Dioxygenase Towards Enhancement Of Vanillin Synthesis

To create better enzyme for enhanced yield of industrial products is a challenging task in protein engineering. It requires lots of resources to manipulate or mutate enzymes experimentally. Computational biology helps in studying the mutational effects on enzymes' structure and stability. The enzyme selected for our study is a Resveratrol-cleaving Dioxygenase that convert resveratrol to vanillin. Using comprehensive computational investigation, we studied the catalytic activity of Resveratrol-cleaving Dioxygenase at the molecular level. We introduced site directed mutations to create mutants of the Resveratrol-cleaving Dioxygenase and studied its interactions with resveratrol by Molecular docking and Molecular dynamics simulations. Here, by investigating the interactions between the mutant Resveratrol-cleaving Dioxygenase and the substrate allow us to highlight the improved performance of mutants over the wild type Resveratrol-cleaving Dioxygenase. It was observed that mutant1 is as stable as wild type of enzyme and has a better affinity toward substrate as the formation of hydrogen bond has increased as compared to wild type. Hence we propose that mutant1 if created in lab could provide better yield.