Engineering organophosphate hydrolase for enhanced biocatalytic performance: A review

The attack of nerve agents and the usage of pesticides bring threats on the safety of human lives and environments. Release of the threats of these compounds, organophosphorus compounds (OPCs), is a long-term challenge. Enzymatic degradation has been widely studied for the detoxification and bioremediation as an efficient and clean approach. Organophosphate hydrolase (OPH) is a promising enzyme to detoxification and bioremediation. However, the catalytic efficiencies of OPH for most OPCs are several orders of magnitude less than the best substrate, implying the existence of large rooms for further improving its biocatalytic efficiency. Meanwhile, it is necessary to enhance the performance of OPH resistance to harsh environments. Many efforts have been made for enhancing the biocatalytic performance of OPH and this review is dedicated to summarize and discuss the progress. The first focus is on the enhancement of OPH stereoselectivity and catalytic efficiency by molecular mutations. Then, improvement in the biocatalytic performance by a series of engineering methods including protein fusion, chemical modification, and immobilization are discussed. Finally, the efforts on broadening the substrate spectrum and designing artificial enzymes for OPCs hydrolysis are described to reveal the potential of OPH for extended applications. The engineering of OPH indicates the ability of OPH to be manipulated and makes it more capable of detoxification of OPCs and bioremediation of their pollutions.

Automated summary

The enzymatic degradation of organophosphorus compounds is an efficient and clean approach for detoxification and bioremediation, but further improvement in catalytic efficiency and resistance is needed. Research has focused on enhancing enzyme performance through molecular mutations and engineering methods, as well as expanding substrate spectrum and designing artificial enzymes for extended applications.