Computational approach for designing thermostable Candida antarctica lipase B by molecular dynamics simulation

Candida antarctica lipase B (CalB) is one of the most useful enzyme for various reactions and bioconversions. Enhancing thermostability of CalB is required for industrial applications. In this study, we propose a computational design strategy to improve the thermostability of CalB. Molecular dynamic...

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Bibliographic Details
Published in:Journal of Biotechnology
Main Authors: Park, Hyun June, Park, Kyungmoon, Kim, Yong Hwan, Yoo, Young Je
Format: Article in Journal/Newspaper
Language:English
Published: ELSEVIER SCIENCE BV 2016
Subjects:
Candida antarctica lipase B
Enzyme rigidity
Molecular dynamics simulation
Thermostability
Antarc*
Antarctica
Online Access:https://scholarworks.unist.ac.kr/handle/201301/20337
http://www.sciencedirect.com/science/article/pii/S0168165614008621
https://doi.org/10.1016/j.jbiotec.2014.09.014
Description
Summary:Candida antarctica lipase B (CalB) is one of the most useful enzyme for various reactions and bioconversions. Enhancing thermostability of CalB is required for industrial applications. In this study, we propose a computational design strategy to improve the thermostability of CalB. Molecular dynamics simulations at various temperatures were used to investigate the common fluctuation sites in CalB, which are considered to be thermally weak points. The RosettaDesign algorithm was used to design the selected residues. The redesigned CalB was simulated to verify both the enhancement of intramolecular interactions and the lowering of the overall root-mean-square deviation (RMSD) values. The A251E mutant designed using this strategy showed a 2.5-fold higher thermostability than the wild-type CalB. This strategy could apply to other industry applicable enzymes. close

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