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Quantitative Improvements and Insights into CALB‐Catalyzed Resolution of trans ‐ and cis ‐2‐Phenylcyclopropyl Azolides
Author(s) -
Yeh YanRu,
Tzeng YiJia,
Tsai ShauWei
Publication year - 2018
Publication title -
chemistryselect
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.437
H-Index - 34
ISSN - 2365-6549
DOI - 10.1002/slct.201800578
Subject(s) - candida antarctica , kinetic resolution , hydrolysis , chemistry , ether , catalysis , substrate (aquarium) , resolution (logic) , lipase , stereochemistry , enzyme , organic chemistry , medicinal chemistry , enantioselective synthesis , oceanography , artificial intelligence , geology , computer science
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 o C, leading to k 2RR K 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.