Acrylamide mitigation in French fries using native l-asparaginase from Aspergillus oryzae CCT 3940

Abstract The Maillard reaction is responsible for color and flavor formation in fried, roasted and baked foods. However, this reaction can also promote the formation of acrylamide, a potential human carcinogen. The application of l -asparaginase represents a promising method for acrylamide mitigation in heated products by the direct conversion of the precursor l -asparagine to l -aspartic acid and ammonia, which does not lead to additional acrylamide formation. Our research group produced and purified an l -asparaginase from native Aspergillus oryzae CCT 3940 with highly potential for acrylamide mitigation. To verify the enzymatic effectiveness, we compared the native l -asparaginase with the commercial recombinant enzyme. For this purpose, a GC-MS/MS method was developed, optimized and validated for the assessment of acrylamide in French fries. Our results indicate a relationship between the l -asparagine content and acrylamide formation in French fries. The acrylamide concentration of the fried potato treated with the l -asparaginase from A. oryzae CCT 3940 and treated with commercial enzyme reduced 72% and 92%, respectively compared to control sample. Moreover, the l -asparaginase from A. oryzae CCT 3940 showed no l -glutaminase activity, while commercial enzyme promoted a decrease in the l -glutamine content (25%). Our results suggest that l -asparaginase from A. oryzae CCT 3940 may be of great value for acrylamide mitigation.