title: Computational approach for designing thermostable Candida antarctica lipase B by molecular dynamics simulation.
abstract: 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.
authors.affiliation: Bio-Max Institute, Seoul National University, Seoul, Republic of Korea.
authors.forename: Hyun June
authors.initials: HJ
authors.lastname: Park
authors.affiliation: Department of Biological and Chemical Engineering, Hongik University, Chungnam 339-701, Republic of Korea.
authors.forename: Kyungmoon
authors.initials: K
authors.lastname: Park
authors.affiliation: Department of Chemical Engineering, Kwangwoon University, Seoul 139-701, Republic of Korea.
authors.forename: Yong Hwan
authors.initials: YH
authors.lastname: Kim
authors.affiliation: Bio-Max Institute, Seoul National University, Seoul, Republic of Korea; School of Chemical and Biological Engineering, Seoul National University, Seoul 151-744, Republic of Korea. Electronic address: yjyoo@snu.ac.kr.
authors.forename: Young Je
authors.initials: YJ
authors.lastname: Yoo
mesh_terms: D004795:Enzyme Stability; D005656:Fungal Proteins / Q000737:chemistry* / Q000235:genetics; D008049:Lipase / Q000737:chemistry* / Q000235:genetics; D056004:Molecular Dynamics Simulation; D016297:Mutagenesis, Site-Directed; D009154:Mutation; D010843:Pichia / Q000235:genetics; D010957:Plasmids; D013696:Temperature
chemical_list: D005656:Fungal Proteins; D008049:Lipase; C431349:lipase B, Candida antarctica
keywords: Candida antarctica lipase B; Enzyme rigidity; Molecular dynamics simulation; Thermostability