'Watching' lipase-catalyzed acylations using 1H NMR: Competing hydrolysis of vinyl acetate in dry organic solvents

Hedda K. Weber; Hansjörg Weber; Romas J. Kazlauskas

doi:10.1016/S0957-4166(99)00274-8

'Watching' lipase-catalyzed acylations using ¹H NMR: Competing hydrolysis of vinyl acetate in dry organic solvents

Hedda K. Weber, Hansjörg Weber, Romas J. Kazlauskas

Biotechnology Institute

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

56 Scopus citations

Abstract

Lipase-catalyzed acetylations of 1-phenylethanol with vinyl acetate were monitored in situ by ¹H NMR spectroscopy. Surprisingly, even under dry conditions (no added water) the major reaction was hydrolysis of the vinyl acetate, not acetylation of the substrate. Because this competing hydrolysis consumes water and releases acetic acid, the reaction conditions in lipase-catalyzed acylations are not constant, but vary with the reaction time. Addition of a chiral shift reagent reveals the enantiomeric purity of the starting alcohol and allows calculation of the enantiomeric ratio, E, for the reaction.

Original language	English (US)
Pages (from-to)	2635-2638
Number of pages	4
Journal	Tetrahedron Asymmetry
Volume	10
Issue number	14
DOIs	https://doi.org/10.1016/S0957-4166(99)00274-8
State	Published - Jul 16 1999

Bibliographical note

Funding Information:
We thank Dr. Françoise Sauriol (McGill University) for perfect technical support. H. K. Weber thanks the Austrian Science Foundation (FWF) for an Erwin-Schrödinger-Auslandsstipendium as a postdoctoral fellow at McGill University.

Copyright:
Copyright 2015 Elsevier B.V., All rights reserved.

Publisher link

10.1016/S0957-4166(99)00274-8

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title = "'Watching' lipase-catalyzed acylations using 1H NMR: Competing hydrolysis of vinyl acetate in dry organic solvents",

abstract = "Lipase-catalyzed acetylations of 1-phenylethanol with vinyl acetate were monitored in situ by 1H NMR spectroscopy. Surprisingly, even under dry conditions (no added water) the major reaction was hydrolysis of the vinyl acetate, not acetylation of the substrate. Because this competing hydrolysis consumes water and releases acetic acid, the reaction conditions in lipase-catalyzed acylations are not constant, but vary with the reaction time. Addition of a chiral shift reagent reveals the enantiomeric purity of the starting alcohol and allows calculation of the enantiomeric ratio, E, for the reaction.",

author = "Weber, {Hedda K.} and Hansj{\"o}rg Weber and Kazlauskas, {Romas J.}",

note = "Funding Information: We thank Dr. Fran{\c c}oise Sauriol (McGill University) for perfect technical support. H. K. Weber thanks the Austrian Science Foundation (FWF) for an Erwin-Schr{\"o}dinger-Auslandsstipendium as a postdoctoral fellow at McGill University. Copyright: Copyright 2015 Elsevier B.V., All rights reserved.",

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AU - Kazlauskas, Romas J.

N1 - Funding Information: We thank Dr. Françoise Sauriol (McGill University) for perfect technical support. H. K. Weber thanks the Austrian Science Foundation (FWF) for an Erwin-Schrödinger-Auslandsstipendium as a postdoctoral fellow at McGill University. Copyright: Copyright 2015 Elsevier B.V., All rights reserved.

PY - 1999/7/16

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N2 - Lipase-catalyzed acetylations of 1-phenylethanol with vinyl acetate were monitored in situ by 1H NMR spectroscopy. Surprisingly, even under dry conditions (no added water) the major reaction was hydrolysis of the vinyl acetate, not acetylation of the substrate. Because this competing hydrolysis consumes water and releases acetic acid, the reaction conditions in lipase-catalyzed acylations are not constant, but vary with the reaction time. Addition of a chiral shift reagent reveals the enantiomeric purity of the starting alcohol and allows calculation of the enantiomeric ratio, E, for the reaction.

AB - Lipase-catalyzed acetylations of 1-phenylethanol with vinyl acetate were monitored in situ by 1H NMR spectroscopy. Surprisingly, even under dry conditions (no added water) the major reaction was hydrolysis of the vinyl acetate, not acetylation of the substrate. Because this competing hydrolysis consumes water and releases acetic acid, the reaction conditions in lipase-catalyzed acylations are not constant, but vary with the reaction time. Addition of a chiral shift reagent reveals the enantiomeric purity of the starting alcohol and allows calculation of the enantiomeric ratio, E, for the reaction.

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