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

B.A.C. As, van; Dah-Kee Chan; P.J.J. Kivit; A.R.A. Palmans; E.W. Meijer

doi:10.1016/j.tetasy.2007.03.016

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

B.A.C. As, van
, Dah-Kee Chan
, P.J.J. Kivit
, A.R.A. Palmans
, E.W. Meijer

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

13 Citations (Scopus)

3 Downloads (Pure)

Abstract

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%).

Original language	English
Pages (from-to)	787-790
Journal	Tetrahedron
Volume	18
Issue number	6
DOIs	https://doi.org/10.1016/j.tetasy.2007.03.016
Publication status	Published - 2007

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title = "Convenient double-enzymatic synthesis of both enantiomers of 6-methyl-ε-caprolactone",

abstract = "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\%).",

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year = "2007",

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language = "English",

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journal = "Tetrahedron",

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TY - JOUR

T1 - Convenient double-enzymatic synthesis of both enantiomers of 6-methyl-ε-caprolactone

AU - As, van, B.A.C.

AU - Chan, Dah-Kee

AU - Kivit, P.J.J.

AU - Palmans, A.R.A.

AU - Meijer, E.W.

PY - 2007

Y1 - 2007

N2 - 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%).

AB - 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%).

U2 - 10.1016/j.tetasy.2007.03.016

DO - 10.1016/j.tetasy.2007.03.016

M3 - Article

SN - 0040-4020

VL - 18

SP - 787

EP - 790

JO - Tetrahedron

JF - Tetrahedron

IS - 6

ER -

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

Abstract

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