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Development of a mixed solvent system for the efficient resolution of (R, S)-2-octanol catalyzed by magnetite-immobilized lipase
Alternative TitleJ. Mol. Catal. B-Enzym.
Liu, Ying1; Guo, Chen1,2; Liu, Chun-Zhao1
2014-03-01
Source PublicationJOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC
ISSN1381-1177
Volume101Issue:1Pages:23-27
AbstractIn order to find a suitable reaction system for the enzymatic resolution of (R, S)-2-octanol, the effects of the molecular structure of the solvent on the enantioselectivity (E) and enzymatic activity of Yarrowia lipolytica lipase (YLL) immobilized onto magnetic nanoparticles were systematically analyzed. Both the E and enzymatic activity of the reaction in an acyclic, structurally linear solvent were higher than those in the corresponding branched chain solvent or cyclic solvent. In a mixed solvent system with acetone and carbon tetrachloride (v/v = 3:7), the immobilized YLL exhibited high enantioselectivity, activity, and reusability. The thermodynamic analysis showed that the enantiomer discrimination was enthalpy-driven at all temperatures tested. These results present new opportunities and challenges for understanding and intensifying the enzymatic resolution process of (R, S)-2-octanol by designing suitable solvent system. (C) 2013 Elsevier B.V. All rights reserved.; In order to find a suitable reaction system for the enzymatic resolution of (R, S)-2-octanol, the effects of the molecular structure of the solvent on the enantioselectivity (E) and enzymatic activity of Yarrowia lipolytica lipase (YLL) immobilized onto magnetic nanoparticles were systematically analyzed. Both the E and enzymatic activity of the reaction in an acyclic, structurally linear solvent were higher than those in the corresponding branched chain solvent or cyclic solvent. In a mixed solvent system with acetone and carbon tetrachloride (v/v = 3:7), the immobilized YLL exhibited high enantioselectivity, activity, and reusability. The thermodynamic analysis showed that the enantiomer discrimination was enthalpy-driven at all temperatures tested. These results present new opportunities and challenges for understanding and intensifying the enzymatic resolution process of (R, S)-2-octanol by designing suitable solvent system. (C) 2013 Elsevier B.V. All rights reserved.
KeywordYarrowia Lipolytica Lipase Resolution 2-octanol Enantioselectivity Magnetite
SubtypeArticle
WOS HeadingsScience & Technology ; Life Sciences & Biomedicine ; Physical Sciences
DOI10.1016/j.molcatb.2013.12.011
URL查看原文
Indexed BySCI
Language英语
WOS KeywordORGANIC-SOLVENTS ; SUBSTRATE-SPECIFICITY ; KINETIC RESOLUTION ; ENANTIOSELECTIVITY ; WATER ; ENZYMES ; MEDIA ; TRANSESTERIFICATION ; BIOCATALYSIS ; PERFORMANCE
WOS Research AreaBiochemistry & Molecular Biology ; Chemistry
WOS SubjectBiochemistry & Molecular Biology ; Chemistry, Physical
WOS IDWOS:000332142400004
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Cited Times:6[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Version出版稿
Identifierhttp://ir.ipe.ac.cn/handle/122111/8072
Collection研究所(批量导入)
Affiliation1.Chinese Acad Sci, Inst Proc Engn, Natl Key Lab Biochem Engn, Beijing 100190, Peoples R China
2.Chinese Acad Sci, Inst Proc Engn, Key Lab Green Proc & Engn, Beijing 100190, Peoples R China
Recommended Citation
GB/T 7714
Liu, Ying,Guo, Chen,Liu, Chun-Zhao. Development of a mixed solvent system for the efficient resolution of (R, S)-2-octanol catalyzed by magnetite-immobilized lipase[J]. JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC,2014,101(1):23-27.
APA Liu, Ying,Guo, Chen,&Liu, Chun-Zhao.(2014).Development of a mixed solvent system for the efficient resolution of (R, S)-2-octanol catalyzed by magnetite-immobilized lipase.JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC,101(1),23-27.
MLA Liu, Ying,et al."Development of a mixed solvent system for the efficient resolution of (R, S)-2-octanol catalyzed by magnetite-immobilized lipase".JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC 101.1(2014):23-27.
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