Efficient control of acrylamide in French fries by an extraordinarily active and thermo-stable L-asparaginase: A lab-scale study

As a potential carcinogen, acrylamide (AA) widely exists in starch-rich foods during frying, triggering international health alerts. L-Asparaginase (L-ASNase, EC 3.5.1.1) could efficiently inhibit the AA by hydrolyzing its precursor L-Asparagine. Here, a novel recombinant L-ASNase from Palaeococcus ferrophilus was identified for the first time. The purified enzyme exhibited its highest activity at pH 8.5 and 95 degrees C and retained more than 70% relative activity after incubation at 80 degrees C for 2 h. Compared to untreated French fries, the AA content in the enzyme-treated (10 U/mL, 85 degrees C, 15 min) French fries was significantly reduced by 79%. Notably, the L-ASNase could remain over 98% of initial activity after three months of storage at 4 degrees C, suggesting good storage stability. These results demonstrated that P. ferrophilus L-ASNase could be a great candidate in controlling AA in the food industry, especially at high blanching temperature.

Automated summary

A novel recombinant L-ASNase from Palaeococcus ferrophilus was found to efficiently inhibit the formation of acrylamide (AA) in starch-rich foods, especially at high temperatures. French fries treated with the enzyme showed a significant reduction in AA content, and the enzyme remained active even after long-term storage, indicating good stability.