Quantitative Improvements and Insights into CALB-Catalyzed Resolution of trans- and cis-2-Phenylcyclopropyl Azolides

Yan Ru Yeh; Yi Jia Tzeng; Shau Wei Tsai

doi:10.1002/slct.201800578

Quantitative Improvements and Insights into CALB-Catalyzed Resolution of trans- and cis-2-Phenylcyclopropyl Azolides

Yan Ru Yeh
, Yi Jia Tzeng
, Shau Wei Tsai^*

^*Corresponding author for this work

Department of Chemical and Materials Engineering

Chang Gung University

Research output: Contribution to journal › Journal Article › peer-review

3 Scopus citations

Abstract

With trans-2-phenylcyclopropyl azolides as the model substrate for hydrolytic or alcoholic resolution in methyl tert-butyl ether (MTBE) via Novozym 435 as an immobilized Candida antarctica lipase B (CALB), quantitative improvements of the enzyme activity and enantioselectivity were reported. At the best reaction conditions of 35^oC, leading to k_2RRK_mRR ⁻¹=5.185 L/h⋅g and E_trans=97.2, for hydrolysis of trans-2-phenylcyclopropyl 1,2,4-azolide (trans-2-PCPT), (1R,2R)-2-PCPCA of high optical purity was obtained. Insights into CALB performance via kinetic and thermodynamic analysis for trans- and cis-2-phenylcyclopropyl 1,2,4-triazolide (cis-2-PCPT) were furthermore addressed, showing the prospect of present kinetic resolution process for synthesizing other optically pure 2-arylcyclopropane-1-carboxylic acids.

Original language	English
Pages (from-to)	5353-5360
Number of pages	8
Journal	ChemistrySelect
Volume	3
Issue number	19
DOIs	https://doi.org/10.1002/slct.201800578
State	Published - 24 05 2018

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Publisher Copyright:
© 2018 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim

Keywords

2-phenylcyclopropyl-1-carboxylic acid
CALB
azolide
kinetic and thermodynamic analysis
kinetic resolution

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10.1002/slct.201800578

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title = "Quantitative Improvements and Insights into CALB-Catalyzed Resolution of trans- and cis-2-Phenylcyclopropyl Azolides",

abstract = "With trans-2-phenylcyclopropyl azolides as the model substrate for hydrolytic or alcoholic resolution in methyl tert-butyl ether (MTBE) via Novozym 435 as an immobilized Candida antarctica lipase B (CALB), quantitative improvements of the enzyme activity and enantioselectivity were reported. At the best reaction conditions of 35oC, leading to k2RRKmRR −1=5.185 L/h⋅g and Etrans=97.2, for hydrolysis of trans-2-phenylcyclopropyl 1,2,4-azolide (trans-2-PCPT), (1R,2R)-2-PCPCA of high optical purity was obtained. Insights into CALB performance via kinetic and thermodynamic analysis for trans- and cis-2-phenylcyclopropyl 1,2,4-triazolide (cis-2-PCPT) were furthermore addressed, showing the prospect of present kinetic resolution process for synthesizing other optically pure 2-arylcyclopropane-1-carboxylic acids.",

keywords = "2-phenylcyclopropyl-1-carboxylic acid, CALB, azolide, kinetic and thermodynamic analysis, kinetic resolution",

author = "Yeh, \{Yan Ru\} and Tzeng, \{Yi Jia\} and Tsai, \{Shau Wei\}",

note = "Publisher Copyright: {\textcopyright} 2018 Wiley-VCH Verlag GmbH \& Co. KGaA, Weinheim",

year = "2018",

month = may,

day = "24",

doi = "10.1002/slct.201800578",

language = "英语",

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T1 - Quantitative Improvements and Insights into CALB-Catalyzed Resolution of trans- and cis-2-Phenylcyclopropyl Azolides

AU - Yeh, Yan Ru

AU - Tzeng, Yi Jia

AU - Tsai, Shau Wei

PY - 2018/5/24

Y1 - 2018/5/24

N2 - With trans-2-phenylcyclopropyl azolides as the model substrate for hydrolytic or alcoholic resolution in methyl tert-butyl ether (MTBE) via Novozym 435 as an immobilized Candida antarctica lipase B (CALB), quantitative improvements of the enzyme activity and enantioselectivity were reported. At the best reaction conditions of 35oC, leading to k2RRKmRR −1=5.185 L/h⋅g and Etrans=97.2, for hydrolysis of trans-2-phenylcyclopropyl 1,2,4-azolide (trans-2-PCPT), (1R,2R)-2-PCPCA of high optical purity was obtained. Insights into CALB performance via kinetic and thermodynamic analysis for trans- and cis-2-phenylcyclopropyl 1,2,4-triazolide (cis-2-PCPT) were furthermore addressed, showing the prospect of present kinetic resolution process for synthesizing other optically pure 2-arylcyclopropane-1-carboxylic acids.

AB - With trans-2-phenylcyclopropyl azolides as the model substrate for hydrolytic or alcoholic resolution in methyl tert-butyl ether (MTBE) via Novozym 435 as an immobilized Candida antarctica lipase B (CALB), quantitative improvements of the enzyme activity and enantioselectivity were reported. At the best reaction conditions of 35oC, leading to k2RRKmRR −1=5.185 L/h⋅g and Etrans=97.2, for hydrolysis of trans-2-phenylcyclopropyl 1,2,4-azolide (trans-2-PCPT), (1R,2R)-2-PCPCA of high optical purity was obtained. Insights into CALB performance via kinetic and thermodynamic analysis for trans- and cis-2-phenylcyclopropyl 1,2,4-triazolide (cis-2-PCPT) were furthermore addressed, showing the prospect of present kinetic resolution process for synthesizing other optically pure 2-arylcyclopropane-1-carboxylic acids.

KW - 2-phenylcyclopropyl-1-carboxylic acid

KW - CALB

KW - azolide

KW - kinetic and thermodynamic analysis

KW - kinetic resolution

UR - https://www.scopus.com/pages/publications/85047559623

U2 - 10.1002/slct.201800578

DO - 10.1002/slct.201800578

M3 - 文章

AN - SCOPUS:85047559623

SN - 2365-6549

VL - 3

SP - 5353

EP - 5360

JO - ChemistrySelect

JF - ChemistrySelect

IS - 19

ER -

Quantitative Improvements and Insights into CALB-Catalyzed Resolution of trans- and cis-2-Phenylcyclopropyl Azolides

Abstract

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Keywords

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