Covalent immobilization of glucoisomerase on glutaraldehyde-activated bagasse cellulose for fructose syrup production from sago-starch-derived glucose

Abstract

Sago starch holds promise for fructose syrup production as a non-cane sweetener alternative through optimized isomerization processes. A critical challenge in this production system is improving catalytic effectiveness and operational efficiency. Therefore, this study aimed to optimize glucoisomerase immobilization by determining the optimal enzyme concentration and evaluating enzyme reusability for fructose production. This study addresses the challenge by immobilizing glucoisomerase via covalent binding to glutaraldehyde-activated bagasse cellulose, thereby enhancing enzyme stability and enabling repeated use. We evaluated the optimal free enzyme concentration for immobilization, determined enzyme loading on the activated bagasse support, and assessed reusability performance in the isomerization of sago-starch-derived glucose. Optimal immobilization was achieved with a free enzyme concentration of 0.75% (w/v), yielding the highest immobilization effectiveness (51.07% enzyme retention). Under these conditions, an immobilized enzyme concentration of 0.08% (80 U/g) produced 21.94% fructose from an initial 50% glucose, corresponding to a 43.89% degree of conversion. The immobilized glucoisomerase retained effective catalytic activity for up to seven cycles, demonstrating stable conversion performance. These results highlight the potential of the immobilized enzyme system for enhanced process efficiency and repeated use, indicating its potential for industrial-scale production of fructose syrup. These findings confirm that covalent immobilization on glutaraldehyde-activated bagasse cellulose provides an effective and sustainable strategy for improving fructose syrup production from sago starch via glucose isomerization.

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