LAUSR

Abstract In the present work, a novel strategy is developed to immobilize cellulase enzyme. Firstly, biobased hollow polymer particles were prepared from commonly available bio-phenylpropene, trans-anethole (ANE) through a preparation process established earlier by us, then onto which amino-modified Fe3O4 NPs were covalently attached to form biobased magnetic hollow particles (BMHPs). Further, the surface of BMHPs was modified with glutaraldehyde via Schiff base reaction to produce multi-layered magnetic hollow particles (MMHPs). Cellulase (Aspergillus niger) was covalently immobilized on MMHPs also through Schiff base reaction, providing multi-layered magnetic hollow particles containing cellulase (c-MMHPs). An optimum loading amount of cellulase was achieved as 180 mg/g. The c-MMHPs were characterized by SEM, TEM, EDX, VSM, FT-IR, BET and XRD analysis techniques. The immobilized cellulase (c-MMHPs) was used as bio-catalyst towards carboxymethyl cellulose (CMC) and showed impressive catalytic activity and significantly enhanced stability at different pH and temperature conditions. Besides, the adsorption ability and the adsorption kinetic study of c-MMHPs towards BSA and methylene blue dye were also investigated. The maximum adsorption towards BSA and MB was found to be up to 716 and 264 mg/g, respectively. The present work opens up a new strategy to immobilize enzymes, and the created MMHPs constitute a promising platform for immobilizing enzymes and other biomacromolecules.