State Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu 214122, China.
State Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu 214122, China.
Food Chem. 2021 Oct 30;360:130046. doi: 10.1016/j.foodchem.2021.130046. Epub 2021 May 11.
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.
丙烯酰胺(AA)作为一种潜在的致癌物质,广泛存在于油炸淀粉类食品中,引发了国际健康警报。l-天冬酰胺酶(l-ASNase,EC 3.5.1.1)可以通过水解其前体 l-天冬酰胺来有效抑制 AA。在这里,首次鉴定出一种来自古生球菌的新型重组 l-ASNase。纯化后的酶在 pH8.5 和 95°C 下表现出最高的活性,在 80°C 孵育 2 小时后保留超过 70%的相对活性。与未经处理的法式炸薯条相比,用酶处理(10 U/mL,85°C,15 分钟)的法式炸薯条中的 AA 含量显著降低了 79%。值得注意的是,l-ASNase 在 4°C 下储存三个月后仍保持初始活性的 98%以上,表明其具有良好的储存稳定性。这些结果表明,来自古生球菌的 l-ASNase 可以成为食品工业中控制 AA 的理想候选酶,特别是在高温烫漂条件下。