Structure prediction and functional analyses of a thermostable lipase obtained from Shewanella putrefaciens

Abstract

Previous experimental studies on thermostable lipase from Shewanella putrefaciens suggested the maximum activity at higher temperatures, but with little information on its conformational profile. In this study, the three-dimensional structure of lipase was predicted and a 60 ns molecular dynamics (MD) simulation was carried out at temperatures ranging from 300 to 400 K to better understand its thermostable nature at the molecular level. MD simulations were performed in order to predict the optimal activity of thermostable lipase. The results suggested strong conformational temperature dependence. The thermostable lipase maintained its bio-active conformation at 350 K during the 60 ns MD simulations.

Keywords:

• lipase
• MD simulations
• thermostability
• structure prediction

Acknowledgements

The authors would like to express their gratitude to the Centre for High Performance Computing, Department of Science and Technology of South Africa, and Henan University of Technology of China.