Immobilization of l-asparaginase on genipin cross-linked chitosan beads shows better acrylamide diminution in cassava chips: Process optimization and characterization.

Glutaraldehyde is the conventionally used cross-linker for the activation and cross-linking of support matrices used in enzyme immobilization. However, the toxic nature of glutaraldehyde makes it unsafe for food applications, propelling the need for nontoxic cross-linkers. Genipin reacts with the primary and secondary amines generating a dark-blue colored pigment and is an attractive alternative to glutaraldehyde as a cross-linker for enzyme immobilization. Apart from its excellent cross-linking properties, genipin possesses added advantages over glutaraldehyde such as proven health benefits, biocompatibility, and biodegradability. The present study explores the application of chitosan beads cross-linked with the natural and nontoxic agent, genipin, for immobilizing l-asparaginase, aimed at its subsequent use in mitigating acrylamide formation in food products. The immobilized l-asparaginase exhibited improved functionalities such as stability, reusability, and reduction in acrylamide formation in deep-fried cassava chips. One of the limitations observed during application in the food process was the mechanical fragility of the chitosan beads during speedy stirring. This can be overcome by increasing the concentration and time of contact of the coagulant bath during the formation of chitosan beads. The drying of the enzyme-bound chitosan beads will also lead to shrinkage and prevent breakage during stirring. This study conclusively demonstrated the applicability of immobilizing l-asparaginase on genipin cross-linked chitosan beads in food-related processes.