Improving Catalytic Activity and Thermal Stability of Methyl-Parathion Hydrolase for Degrading the Pesticide of Methyl-Parathion

Pesticides are indispensable in today’s agriculture. Methyl-parathion hydrolase (MPH, E.C.3.1.8.1) could hydrolyze organophosphorus pesticides, including methyl-parathion. MPH rehabilitate soil and water resources contaminated by pesticides. However, natural MPHs generally exhibited a low tolerance to high temperatures catalytic efficiency. In this study, we improved the efficiency toward methyl-parathion thermal stability of from Pseudomonas sp. WBC-3 through saturation mutagenesis fusion with self-assembling amphipathic peptides (SAP). The experimental characterization showed that compared wild-type enzyme, kcat/Km mutant T271S yielded was increased 224.3% MPH. T50 Tm SAP3-MPH an SAP fused at N-terminus were 6.2°C 6.0°C, respectively. Compared SAP3 (SAP3-T271S) 2.1-fold increase without significantly affecting stability. simultaneous improvement would be beneficial for its application degradation detection Furthermore, our study provides potential combination strategy design other enzyme preparations pollutant degradation.