In-silico identification of lysine residue for α-Amylase immobilization on dialdehyde cellulose.

Enzymes are the precious gift of nature to humans. The wise utilization of enzymes may reduce energy needs of humans and the Immobilization technique can help a lot in this regard. This aspect overcomes limitations of the enzymes, therefore providing an opportunity to explore enzymatic chemistry further. In the present context, it is quite cumbersome & costly to identify the amino acid of enzymes involved in the covalent mode of Immobilization. In the present study, molecular modeling techniques were used to do this difficult task. The present work used molecular modeling methods to extract information about the immobilization of α-Amylase (E.C.3.2.1.1) on Dialdehyde Cellulose. The Lysine residue is the most probable residue to interact with Dialdehyde Cellulose. In the present work, a total of 23 lysine residues were used to study covalent binding behavior with α-Amylase. It was found that if Lys142 is involved in binding with Dialdehyde Cellulose then binding affinity (−6.1 & −5.9 kcal mol−1), as well as the involvement of amino acids of both free α-Amylase and Lys142 immobilized α-Amylase with the starch substrate, were found to be similar. The technique reported here is used for the identification of amino acid residue for the Immobilization of enzymes. [Display omitted] • Molecular modeling techniques were used to identify residue involved in bonding. • Docking & visualization software were used in the present study. • Studies were carried out using the concept of stepwise exclusion of individual lysine residue. • Lys142 was involved for immobilization of α-Amylase on Dialdehyde Cellulose. [ABSTRACT FROM AUTHOR]