Prediction of the solvent affecting site and the computational design of stable Candida antarctica lipase B in a hydrophilic organic solvent
DC Field | Value | Language |
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dc.contributor.author | Park, Hyun June | - |
dc.contributor.author | Joo, Jeong Chan | - |
dc.contributor.author | Park, Kyungmoon | - |
dc.contributor.author | Kim, Yong Hwan | - |
dc.contributor.author | Yoo, Young Je | - |
dc.date.accessioned | 2021-11-11T04:42:17Z | - |
dc.date.available | 2021-11-11T04:42:17Z | - |
dc.date.created | 2021-11-10 | - |
dc.date.issued | 2013-02-10 | - |
dc.identifier.issn | 0168-1656 | - |
dc.identifier.uri | https://scholarworks.bwise.kr/hongik/handle/2020.sw.hongik/17180 | - |
dc.description.abstract | Enzyme reactions in organic solvent such as for organic synthesis have great industrial potential. However, enzymes lose their stability in hydrophilic organic solvents due to the deformation of the enzyme by the solvent. It is thus important to enhance the stability of enzymes in hydrophilic organic solvents. Previous approaches have not considered on the interaction between enzymes and solvents due to the lack of information. In this study, the structural motions of the enzyme in methanol cosolvent and the interaction between the enzyme surface and the solvent molecule were investigated using molecular dynamics simulation (MD). By analyzing the MD simulation results, the surface residues of Candida antarctica lipase B (CalB) with higher root mean square deviation (RMSD) in a methanol solvent were considered as methanol affecting site and selected for site-directed mutagenesis. The methanol affecting site was computationally redesigned by lowering the RMSD. Among the candidate mutants, the A8T, A92E, N97Q and T245S mutants showed higher organic solvent stability at various methanol concentrations. The rational approach developed in this study could be applied to the stabilization of other industrial enzymes used in organic solvents. (C) 2012 Elsevier B.V. All rights reserved. | - |
dc.language | 영어 | - |
dc.language.iso | en | - |
dc.publisher | ELSEVIER SCIENCE BV | - |
dc.subject | BACILLUS-CIRCULANS XYLANASE | - |
dc.subject | MOLECULAR-DYNAMICS | - |
dc.subject | RATIONAL DESIGN | - |
dc.subject | STABILITY | - |
dc.subject | THERMOSTABILIZATION | - |
dc.subject | SIMULATIONS | - |
dc.subject | HYDRATION | - |
dc.subject | ENZYMES | - |
dc.subject | WATER | - |
dc.title | Prediction of the solvent affecting site and the computational design of stable Candida antarctica lipase B in a hydrophilic organic solvent | - |
dc.type | Article | - |
dc.contributor.affiliatedAuthor | Park, Kyungmoon | - |
dc.identifier.doi | 10.1016/j.jbiotec.2012.11.006 | - |
dc.identifier.scopusid | 2-s2.0-84873856468 | - |
dc.identifier.wosid | 000314800200009 | - |
dc.identifier.bibliographicCitation | JOURNAL OF BIOTECHNOLOGY, v.163, no.3, pp.346 - 352 | - |
dc.relation.isPartOf | JOURNAL OF BIOTECHNOLOGY | - |
dc.citation.title | JOURNAL OF BIOTECHNOLOGY | - |
dc.citation.volume | 163 | - |
dc.citation.number | 3 | - |
dc.citation.startPage | 346 | - |
dc.citation.endPage | 352 | - |
dc.type.rims | ART | - |
dc.type.docType | Article | - |
dc.description.journalClass | 1 | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Biotechnology & Applied Microbiology | - |
dc.relation.journalWebOfScienceCategory | Biotechnology & Applied Microbiology | - |
dc.subject.keywordPlus | BACILLUS-CIRCULANS XYLANASE | - |
dc.subject.keywordPlus | MOLECULAR-DYNAMICS | - |
dc.subject.keywordPlus | RATIONAL DESIGN | - |
dc.subject.keywordPlus | STABILITY | - |
dc.subject.keywordPlus | THERMOSTABILIZATION | - |
dc.subject.keywordPlus | SIMULATIONS | - |
dc.subject.keywordPlus | HYDRATION | - |
dc.subject.keywordPlus | ENZYMES | - |
dc.subject.keywordPlus | WATER | - |
dc.subject.keywordAuthor | Organic solvent stability | - |
dc.subject.keywordAuthor | Candida antarctica lipase B | - |
dc.subject.keywordAuthor | Enzyme engineering | - |
dc.subject.keywordAuthor | Molecular dynamics | - |
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