Open AccessIn Silico Designing of an Industrially Sustainable Carbonic Anhydrase Using Molecular Dynamics Simulation
Author(s) -
Sachin Kumar Bharatiy,
Mousumi Hazra,
Manish Paul,
Swati Mohapatra,
Deviprasad Samantaray,
Ramesh Chandra Dubey,
Shourjya Sanyal,
Saurav Datta,
Saugata Hazra
Publication year - 2016
Publication title -
acs omega
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.779
H-Index - 40
ISSN - 2470-1343
DOI - 10.1021/acsomega.6b00041
Subject(s) - in silico , molecular dynamics , thermophile , chemistry , carbonic anhydrase , enzyme , mesophile , protein engineering , stability (learning theory) , computational biology , directed evolution , biochemistry , mutant , biochemical engineering , bacteria , biology , gene , computational chemistry , genetics , computer science , engineering , machine learning
Carbonic anhydrase (CA) is a family of metalloenzymes that has the potential to sequestrate carbon dioxide (CO 2 ) 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 ( Sulfurihydrogenibium 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.