Hydrogel Formation of Enzymatically Solubilized Corn Bran Feruloylated Arabinoxylan by Laccase-Catalyzed Cross-Linking.

In order to upgrade the potential of cereal bran arabinoxylan for advanced hydrogel applications, a deep understanding of its gelation process is required. This work provides a comprehensive and systematic analysis of the laccase-catalyzed cross-linking of feruloylated arabinoxylan (FAX) to establish a clear link between processing conditions and final hydrogel properties. Endo-1,4-xylanase was used to obtain corn bran FAX rich in ferulic acid moieties, and then we demonstrated that gel formation is driven by the oxidative coupling of these feruloyl monomers into diferulic acid bridges, e.g., 8-5', 5-5', 8--4', and 8-5' benzofuran diferulic acids. A systematic investigation revealed that hydrogel properties were significantly affected by the processing conditions, i.e., FAX concentration, enzyme dosage, reaction pH, and reaction temperature during the enzymatic gel formation catalyzed by laccase. While gel strength peaked at a FAX concentration of 30 mg/mL, an optimal temperature of 25 °C and pH 6 were identified. Notably, we discovered a critical trade-off with enzyme concentration: higher laccase levels accelerated the reaction but compromised the final hydrogel's mechanical strength and water retention. Gelation failed completely at pH ≥ 9 due to laccase inactivation. Meanwhile, scanning electron microscope analysis revealed that the microstructure of the FAX hydrogels was significantly affected by changes in the processing conditions. These findings offer crucial insights for the rational design of FAX-based hydrogels, enabling their tailored fabrication for food industry applications.