Efficient control of acrylamide in French fries by an extraordinarily active and thermo-stable l-asparaginase: A lab-scale study. (30th October 2021) - Wang, Yiming
Highlights: An active and thermostable l -ASNase from Palaeococcus ferrophilus was reported. The l -ASNase retained over 70% relative activity after incubation at 80 °C for 2 h. The condition of enzyme treatment for acrylamide (AA) inhibition was optimized. The enzyme remained a good stability after three months of storage at 4 °C. The AA content in the enzyme-treated French Fries was significantly reduced. Abstract: 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 °C and retained more than 70% relative activity after incubation at 80 °C for 2 h. Compared to untreated French fries, the AA content in the enzyme-treated (10 U/mL, 85 °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 °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.