Acrylamide is a potent carcinogen and neurotoxin formed by the Maillard reaction when L-asparagine reacts with starch at high temperature. It is formed in food materials mainly deep fried and bakery products. Enzymatic pretreatment of these food products with asparaginase enzyme leads to reduction in acrylamide. However, enzymatic process is quite expensive due to high cost, low catalytic efficiency as well as problem with enzyme reusability. Present work deals with these problems by exploring L-asparaginase from Bacillus aryabhattai. Asparaginase enzyme was immobilized on APTES modified magnetic nanoparticles. It was found to be more than three-fold increase their thermal stability from free enzyme and retained 90% activity after fifth cycle. The immobilized enzyme also showed better affinity towards its substrate. During pretreatment of asparagine in a starch-asparagine food model system and it was clearly demonstrated that asparaginase nanoconjugates had reduced the formation of acrylamide by more than 90% within 30 min.