Methyl parathion hydrolase (MPH) plays an important role in degrading a range of organophosphorus compounds. In order to display MPH on the cell surface of Escherichia coli strain RosettaBlue™, the Flavin-based fluorescent protein EcFbFP was severed as an auto-anchoring matrix. With net negative charges of EcFbFP supplying the driving forces, fusion protein MPH-EcFbFP through a two-step auto-surface display process was finally verified by (a) inner membrane translocation and (b) anchoring at outer membrane. Cells with surface-displayed MPH obtained activity of 0.12 U/OD600 against substrate methyl parathion. MPH when fused with engineered EcFbFP containing 20 net negative charges exhibited fivefold higher anchoring efficiency and tenfold higher enzymatic catalytic activity of 1.10 U/OD600. The above result showed that MPH was successfully displayed on cell surface and can be used for biodegradation of methyl parathion.

中文翻译：

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基于黄素的荧光蛋白EcFbFP在大肠杆菌中对甲基对硫磷水解酶的自动引导表面展示。

甲基对硫磷水解酶（MPH）在降解一系列有机磷化合物中起重要作用。为了在大肠杆菌菌株RosettaBlue™的细胞表面上显示MPH，将基于黄素的荧光蛋白EcFbFP切断为自锚定基质。随着EcFbFP的净负电荷提供驱动力，融合蛋白MPH-EcFbFP通过两步自动表面显示过程最终通过（a）内膜移位和（b）锚定在外膜上得到了验证。表面显示MPH的细胞对底物甲基对硫磷的活性为0.12 U / OD600。MPH与包含20个净负电荷的工程EcFbFP融合时，其锚固效率和1.10 U / OD600的酶催化活性高出五倍。