Title of article
A Review on Engineering of Organophosphorus Hydrolase (OPH) Enzyme
Author/Authors
Farnoosh, Gholamreza Applied Biotechnology Research Center - Baqiyatallah University of Medical Sciences, Tehran Iran , Latifi, Ali Mohammad Applied Biotechnology Research Center - Baqiyatallah University of Medical Sciences, Tehran Iran
Pages
10
From page
1
To page
10
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
Organophosphorus , Protein engineering , Thermostability
Journal title
Astroparticle Physics
Serial Year
2014
Record number
2427180
Link To Document