A Review on Engineering of Organophosphorus Hydrolase (OPH) Enzyme

Document Type: Review Article

Authors

Applied Biotechnology Research Center, Baqiyatallah University of Medical Sciences, Tehran, Iran

Abstract

Organophosphorus chemicals are compounds which have been used as pesticides and insecticides in agriculture. They’re also used as nervous agents and have raised many problems for human and environment. Among the most important methods of decontamination from these compounds are biodegradation methods. Using OPH enzyme in degradation the mentioned compounds is seen as one of the desirable ways, but low activity and specification and low thermostability are among factors significantly decreasing the optimal application of this enzyme. Using methods of protein engineering based on the alteration of specific protein positions in order to improve the activity, specification and thermostability are some common ways used currently. Numerous studies have been done to increase activity and thermostability of OPH enzyme with alteration of some special amino acids the result of which was an increase against different substrates. OPH enzyme active site connected to substrates that consisted of three large, small and releasing packets were one of the goal areas of changing amino acids used by researchers to improve engineered activities. Among other ways of making enzymes more rigid and stable were bending loops by replacing Proline, creating disulfide bonds, ionic bonds by replacing charged amino acids.

Keywords


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