Convenient double-enzymatic synthesis of both enantiomers of 6-methyl-ε-caprolactone

Both enantiomers of 6-methyl-e-caprolactone (6-MeCL) are obtained in high enantiomeric excess by the combination of an enzymatic ring opening of racemic 6-methyl-e-caprolactone and subsequent enzymatic ring closure. Immobilized Candida antarctica lipase B (Novozym 435) was selected as the biocatalys...

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Main Authors: As, BAC Bart van, Chan, D, Kivit, PJJ, Palmans, ARA Anja, Meijer, EW Bert
Format: Article in Journal/Newspaper
Language:English
Published: 2007
Subjects:
Antarc*
Antarctica
Online Access:http://repository.tue.nl/640887
id ftuniveindhoven:oai:library.tue.nl:640887
record_format openpolar
spelling ftuniveindhoven:oai:library.tue.nl:640887 2023-05-15T13:56:31+02:00 Convenient double-enzymatic synthesis of both enantiomers of 6-methyl-ε-caprolactone As, BAC Bart van Chan, D Kivit, PJJ Palmans, ARA Anja Meijer, EW Bert 2007 application/pdf http://repository.tue.nl/640887 en eng Copyright (c) As, BAC Bart van Copyright (c) Chan, D Copyright (c) Kivit, PJJ Copyright (c) Palmans, ARA Anja Copyright (c) Meijer, EW Bert ISSN:0040-4020 Article / Letter to the editor 2007 ftuniveindhoven 2018-12-26T13:34:47Z Both enantiomers of 6-methyl-e-caprolactone (6-MeCL) are obtained in high enantiomeric excess by the combination of an enzymatic ring opening of racemic 6-methyl-e-caprolactone and subsequent enzymatic ring closure. Immobilized Candida antarctica lipase B (Novozym 435) was selected as the biocatalyst for both the ring-opening and the ring-closing reaction. This route provides ready access to enantiopure (S)-6-MeCL (ee = 99.6%) and (R)-6-MeCL (ee = 98.8%). Article in Journal/Newspaper Antarc* Antarctica Eindhoven University of Technology (TU/e): Research Portal
institution Open Polar
collection Eindhoven University of Technology (TU/e): Research Portal
op_collection_id ftuniveindhoven
language English
description Both enantiomers of 6-methyl-e-caprolactone (6-MeCL) are obtained in high enantiomeric excess by the combination of an enzymatic ring opening of racemic 6-methyl-e-caprolactone and subsequent enzymatic ring closure. Immobilized Candida antarctica lipase B (Novozym 435) was selected as the biocatalyst for both the ring-opening and the ring-closing reaction. This route provides ready access to enantiopure (S)-6-MeCL (ee = 99.6%) and (R)-6-MeCL (ee = 98.8%).
format Article in Journal/Newspaper
author As, BAC Bart van
Chan, D
Kivit, PJJ
Palmans, ARA Anja
Meijer, EW Bert
spellingShingle As, BAC Bart van
Chan, D
Kivit, PJJ
Palmans, ARA Anja
Meijer, EW Bert
Convenient double-enzymatic synthesis of both enantiomers of 6-methyl-ε-caprolactone
author_facet As, BAC Bart van
Chan, D
Kivit, PJJ
Palmans, ARA Anja
Meijer, EW Bert
author_sort As, BAC Bart van
title Convenient double-enzymatic synthesis of both enantiomers of 6-methyl-ε-caprolactone
title_short Convenient double-enzymatic synthesis of both enantiomers of 6-methyl-ε-caprolactone
title_full Convenient double-enzymatic synthesis of both enantiomers of 6-methyl-ε-caprolactone
title_fullStr Convenient double-enzymatic synthesis of both enantiomers of 6-methyl-ε-caprolactone
title_full_unstemmed Convenient double-enzymatic synthesis of both enantiomers of 6-methyl-ε-caprolactone
title_sort convenient double-enzymatic synthesis of both enantiomers of 6-methyl-ε-caprolactone
publishDate 2007
url http://repository.tue.nl/640887
genre Antarc*
Antarctica
genre_facet Antarc*
Antarctica
op_source ISSN:0040-4020
op_rights Copyright (c) As, BAC Bart van
Copyright (c) Chan, D
Copyright (c) Kivit, PJJ
Copyright (c) Palmans, ARA Anja
Copyright (c) Meijer, EW Bert
_version_ 1766264023702044672

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