Enhancing cellulose hydrolysis via cellulase immobilization on zeolitic imidazolate frameworks using physical adsorption

Abstract

This study investigates the immobilization of cellulase on zeolitic imidazolate frameworks (ZIFs) by physical adsoption, speci cally ZIF-8-NH 2 and Fe 3 O 4 @ZIF-8-NH 2 , to enhance enzymatic hydrolysis e ciency. The immobilization process was thoroughly analyzed, including optimization of conditions and characterization of ZIF carriers and immobilized enzymes. The impacts on the catalytic activity of cellulase under various temperatures, pH levels, and storage conditions were examined. Additionally, the reusability of the immobilized enzyme was assessed. Results showed the cellulase immobilized on Fe 3 O 4 @ZIF-8-NH 2 exhibited a high loading capacity of 339.64 mg/g, surpassing previous studies. Its relative enzymatic activity was found to be 71.39 %. Additionally, this immobilized enzyme system demonstrates robust reusability, retaining 68.42 % of its initial activity even after 10 cycles. These ndings underscore the potential of Fe 3 O 4 @ZIF-8-NH 2 as a highly e cient platform for cellulase immobilization, with promising implications for lignocellulosic biore nery.