School of Food and Bioengineering, Xihua University, Chengdu, China.
School of Laboratory Medicine, Chengdu Medical College, Chengdu, China.
J Sci Food Agric. 2018 Oct;98(13):5095-5104. doi: 10.1002/jsfa.9048. Epub 2018 May 17.
Organophosphate and carbamate pesticide residues in food and the environment pose a great threat to human health and have made the easy and rapid detection of these pesticide residues an important task. Discovering new enzyme sources from plants can help reduce the cost of large-scale applications of rapid pesticide detection via enzyme inhibition.
Plant esterase from kidney beans was purified. Kidney bean esterase is identified as a carboxylesterase by substrate and inhibitor specificity tests and mass spectrometry identification. The kidney bean esterase demonstrates optimal catalytic activity at 40 °C, pH 6.5 and an enzyme concentration of 0.30 µg mL . The kidney bean esterase can be inhibited by organophosphate and carbamate pesticides, which can be substituted for acetylcholinesterase. The limit of detection of the purified kidney bean esterase was two- to 20-fold higher than that of the crude one. The method detection limit meets the detection requirement for the maximum residue limits (MRL) in actual samples.
The findings of the present study provide a new source of enzymes for pesticides detection by enzyme inhibition. © 2018 Society of Chemical Industry.
食物和环境中的有机磷和氨基甲酸酯类农药残留对人类健康构成了巨大威胁，因此快速、简便地检测这些农药残留成为一项重要任务。从植物中发现新的酶源有助于降低基于酶抑制作用的大规模快速农药检测的成本。
从菜豆中纯化了植物酯酶。通过底物和抑制剂特异性试验以及质谱鉴定，确定菜豆酯酶为羧酸酯酶。菜豆酯酶在 40°C、pH6.5 和酶浓度为 0.30μg/mL 时表现出最佳的催化活性。菜豆酯酶可被有机磷和氨基甲酸酯类农药抑制，可替代乙酰胆碱酯酶。纯化的菜豆酯酶的检测限比粗提物的检测限高 2 至 20 倍。该方法的检测限满足实际样品中最大残留限量（MRL）的检测要求。
本研究为基于酶抑制作用的农药检测提供了一种新的酶源。 © 2018 英国化学学会。
