Research Information System
Food Chemistry, vol.491, 2025 (SCI-Expanded, Scopus)
A recombinant L-asparaginase from Geobacillus kaustophilus was immobilized onto multi-walled carbon nanotubes and silica supports using divinyl sulfone and genipin crosslinkers. The optimal pH was determined to be 8.5 for all enzyme forms, while the optimal temperature was 55 °C for the free enzyme and 60 °C for all immobilized forms. Notably, the catalytic efficiency of GkASNase immobilized on silica via genipin was approximately 3.2-fold higher than that of the free enzyme. GkASNase immobilized on silica support via divinyl sulfone exhibited a 28.9-fold enhancement in thermal stability compared to the free enzyme at 60 °C. The immobilized GkASNase samples retained at least 90 % of their initial activities after 5 reuses. All immobilized GkASNases achieved a 100 % reduction in acrylamide formation after 60 min treatment at 55 °C. These findings indeed highlight the potential of immobilized GkASNase as an efficient and sustainable solution to reduce acrylamide levels in food, particularly in heat-treated starchy foods.