Integration of α-amylase into covalent organic framework for highly efficient biocatalyst

In recent days covalent organic frameworks (COFs) are engrossed more consideration in numerous fields of application due to their porosity, high ordered arrangement, high surface area, chemical stability and specific binding sites. Herein we demonstrate a COFs, with tunable properties to achieve excellent capability for hosting an enzyme as a biocatalyst. The synthesized COFs have possessed networking morphology, lightweight, flexibility and several functionalities for modulated interaction with α-amylase which offers outstanding loading capacities. The properties of the COFs are thoroughly investigated using SEM, NMR, FTIR, XPS, XRD, TGA and BET. The Km value of the biocomposites indicates the remarkable substrate affinity of the α-amylase towards starch hydrolysis. The accountability of the COFs enhanced the activity efficiency of the enzyme in a different environment and also facilitated for reusability and storage stability. [Display omitted] •COF is synthesized by Schiff-base condensation using aldehyde and amine.•The COFs have several binding sites with flexible network like morphology.•α-amylase immobilized here by physical adsorption with strong interaction.•Immobilized α-amylase shows strong substrate affinity for starch hydrolysis.•Immobilized enzyme exhibits poor leaching and splendid reusability.