2 research outputs found
In Silico Designing of an Industrially Sustainable Carbonic Anhydrase Using Molecular Dynamics Simulation
Carbonic
anhydrase (CA) is a family of metalloenzymes that has
the potential to sequestrate carbon dioxide (CO<sub>2</sub>) from
the environment and reduce pollution. The goal of this study is to
apply protein engineering to develop a modified CA enzyme that has
both higher stability and activity and hence could be used for industrial
purposes. In the current study, we have developed an in silico method
to understand the molecular basis behind the stability of CA. We have
performed comparative molecular dynamics simulation of two homologous
α-CA, one of thermophilic origin (<i>Sulfurihydrogenibium</i> sp.) and its mesophilic counterpart (Neisseria gonorrhoeae), for 100 ns each at 300, 350, 400, and 500 K. Comparing the trajectories
of two proteins using different stability-determining factors, we
have designed a highly thermostable version of mesophilic α-CA
by introducing three mutations (S44R, S139E, and K168R). The designed
mutant α-CA maintains conformational stability at high temperatures.
This study shows the potential to develop industrially stable variants
of enzymes while maintaining high activity