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Kinetic resolution of racemic 5,6-epoxy-bicyclo[2.2.1]heptane-2-one using genetically engineered Saccharomyces cerevisiae

Carlquist, Magnus LU ; Olsson, Cecilia LU ; Bergdahl, Basti LU ; van Niel, Ed LU ; Gorwa-Grauslund, Marie-Francoise LU and Frejd, Torbjörn LU (2009) In Journal of Molecular Catalysis B: Enzymatic 58(2). p.98-102
Abstract
(+)-5,6-Epoxy-bicyclo[2.2.1]heptane-2-one, (+)-1, and endo-(−)-5,6-epoxy-bicyclo[2.2.1]heptane-2-ol,

endo-(−)-2, were obtained by kinetic resolution of rac-1 by asymmetric bioreduction catalyzed by whole

cells of a genetically engineered Saccharomyces cerevisiae yeast strain. The strain, TMB4100, had 1% phosphoglucose

isomerase (PGI) activity and overexpressed a specific short-chain dehydrogenase, encoded

by the gene YMR226c. The whole cell biocatalystwas demonstrated to be significantly inactivated within

24 h, thus restricting the reaction to lowconcentration. Despite this, the resolution method could be used

to produce optically pure (+)-1 and endo-(−)-2 from the racemic mixture at 5... (More)
(+)-5,6-Epoxy-bicyclo[2.2.1]heptane-2-one, (+)-1, and endo-(−)-5,6-epoxy-bicyclo[2.2.1]heptane-2-ol,

endo-(−)-2, were obtained by kinetic resolution of rac-1 by asymmetric bioreduction catalyzed by whole

cells of a genetically engineered Saccharomyces cerevisiae yeast strain. The strain, TMB4100, had 1% phosphoglucose

isomerase (PGI) activity and overexpressed a specific short-chain dehydrogenase, encoded

by the gene YMR226c. The whole cell biocatalystwas demonstrated to be significantly inactivated within

24 h, thus restricting the reaction to lowconcentration. Despite this, the resolution method could be used

to produce optically pure (+)-1 and endo-(−)-2 from the racemic mixture at 5 g/L substrate. At optimal

conditions, 1 g of rac-1 was kinetically resolved to give (+)-1 in 95% ee and 28% yield and endo-(−)-2 in

74% ee, 80% de and 45% yield. (Less)
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author
; ; ; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Baker's yeast, Saccharomyces cerevisiae, epoxide, racemic epoxy ketone, bioreduction, asymmetric carbonyl reduction, kinetic resolution, enantiomeric ratio, kinetic model
in
Journal of Molecular Catalysis B: Enzymatic
volume
58
issue
2
pages
98 - 102
publisher
Elsevier
external identifiers
  • wos:000265584200016
  • scopus:63249094069
ISSN
1873-3158
DOI
10.1016/j.molcatb.2008.11.014
language
English
LU publication?
yes
additional info
The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Organic chemistry (S/LTH) (011001240), Applied Microbiology (LTH) (011001021)
id
36655255-b4d0-4dc4-909f-121e3fea6465 (old id 1393850)
date added to LUP
2016-04-04 10:18:57
date last changed
2021-08-04 03:18:11
@article{36655255-b4d0-4dc4-909f-121e3fea6465,
  abstract     = {(+)-5,6-Epoxy-bicyclo[2.2.1]heptane-2-one, (+)-1, and endo-(−)-5,6-epoxy-bicyclo[2.2.1]heptane-2-ol,<br/><br>
endo-(−)-2, were obtained by kinetic resolution of rac-1 by asymmetric bioreduction catalyzed by whole<br/><br>
cells of a genetically engineered Saccharomyces cerevisiae yeast strain. The strain, TMB4100, had 1% phosphoglucose<br/><br>
isomerase (PGI) activity and overexpressed a specific short-chain dehydrogenase, encoded<br/><br>
by the gene YMR226c. The whole cell biocatalystwas demonstrated to be significantly inactivated within<br/><br>
24 h, thus restricting the reaction to lowconcentration. Despite this, the resolution method could be used<br/><br>
to produce optically pure (+)-1 and endo-(−)-2 from the racemic mixture at 5 g/L substrate. At optimal<br/><br>
conditions, 1 g of rac-1 was kinetically resolved to give (+)-1 in 95% ee and 28% yield and endo-(−)-2 in<br/><br>
74% ee, 80% de and 45% yield.},
  author       = {Carlquist, Magnus and Olsson, Cecilia and Bergdahl, Basti and van Niel, Ed and Gorwa-Grauslund, Marie-Francoise and Frejd, Torbjörn},
  issn         = {1873-3158},
  language     = {eng},
  number       = {2},
  pages        = {98--102},
  publisher    = {Elsevier},
  series       = {Journal of Molecular Catalysis B: Enzymatic},
  title        = {Kinetic resolution of racemic 5,6-epoxy-bicyclo[2.2.1]heptane-2-one using genetically engineered Saccharomyces cerevisiae},
  url          = {https://lup.lub.lu.se/search/files/5510305/1393853.pdf},
  doi          = {10.1016/j.molcatb.2008.11.014},
  volume       = {58},
  year         = {2009},
}