Molecular modeling of cellulose tosylate immobilized α-amylases: An in silico case study through MD simulation and...

The use of enzymes as catalysts in industrial processes has been studied, and they offer more ecologically friendly options for chemical reactions. In the current work, we investigated the potential of molecular modeling to solve the ordinarily difficult problem of identifying the amino acids involved in the covalent mode of immobilization by in silico investigations. The immobilized α-Amylase on Cellulose tosylate (henceforth referred to as Celltos) shows extra peaks of OH and NH₂, CN, SO, C-O-C, and CS. Celltos exhibits distinct ether, imine, and CS peaks, indicating the potential contribution of α-Amylase's hydroxyl, amino, and thiol groups towards immobilization with cellulose's tosylate group. The native amylase was processed for Molecular Dynamics simulation. The simulated amylase was found to be the root mean squarely deviated to 1.16 Å. Autodock Vina, GOLD, SwissDock, and iGemdock generate output averages of 6.164, 6.549, 9.313 & 137.811 and 5.903, 7.656, 9.752 & 132.218 for an unrefined and refined dataset, respectively. The catalytic site intactness values for unrefined and refined SAT9, SAT13, and LAT21 were 83.3 %, 100 %, 100 %, and 8.33 %, 0 %, and 0 %, respectively. Our findings were additionally confirmed by bond distance similarity computations.