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. ferrophilusl-ASNase could be a great candidate in controlling AA in the food industry, especially at high blanching temperature.
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