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Updated: Feb 3, 2026

A New Screening Method for the Directed Evolution of Thermostable Bacteriolytic Enzymes
Published on: November 7, 2012
Disulfide bridge formation to increase thermostability of DFPase enzyme: A computational study
Mozafar Mohammadi1, Amirhossein Sakhteman2, Sajjad Ahrari3
1Applied Biotechnology Research Centre, Baqiyatallah University of Medical Sciences, Tehran, Iran.
Abstract:
Organophosphate compounds bioremediation by use of organophosphorus degradation enzymes such as DFPase is a developing interest in industry and medicine. The most important problem with the bio-catalytic enzymes is their instability on high temperatures. This work carried out to find suitable locations for introducing disulfide bridges in DFPase enzyme. We employed some computational approaches to design the disulfide bridges and evaluate their roles in the enzyme structural thermostability. According to the in silico results, mutant 6 (V24C, C76) increased the enzyme thermostability relative to wild-type.
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