Advanced

Genetically engineered Saccharomyces cerevisiae for kinetic resolution of racemic bicyclo[3.3.1]nonane-2,6-dione

Carlquist, Magnus LU ; Wallentin, Carl-Johan LU ; Wärnmark, Kenneth LU and Gorwa-Grauslund, Marie-Francoise LU (2008) In Tetrahedron: Asymmetry 19(19). p.2293-2295
Abstract
Whole cells of the genetically engineered Saccharomyces cerevisiae strain TMB4100 (1% PGI, YMR226c) were Used as the biocatalyst for the kinetic resolution of racemic bicyclo[3.3.1]nonane-2,6-dione rac-1. The yeast's phosphoglucose isomerase activity was decreased, and the short-chain dehydrogenase/reductase encoded by YMR226c was overexpressed. This reduced the demand for the glucose to regenerate NADPH, while at the same time the reaction rate and selectivity towards (-)-1 became higher. The demand for yeast biomass also decreased, facilitating down-stream processing, which is of considerable importance oil a large scale. With 15 g dry weight/L of the genetically engineered yeast TMB4100 (1% PGI, YMR226c), 40 g/L rac-1 was kinetically... (More)
Whole cells of the genetically engineered Saccharomyces cerevisiae strain TMB4100 (1% PGI, YMR226c) were Used as the biocatalyst for the kinetic resolution of racemic bicyclo[3.3.1]nonane-2,6-dione rac-1. The yeast's phosphoglucose isomerase activity was decreased, and the short-chain dehydrogenase/reductase encoded by YMR226c was overexpressed. This reduced the demand for the glucose to regenerate NADPH, while at the same time the reaction rate and selectivity towards (-)-1 became higher. The demand for yeast biomass also decreased, facilitating down-stream processing, which is of considerable importance oil a large scale. With 15 g dry weight/L of the genetically engineered yeast TMB4100 (1% PGI, YMR226c), 40 g/L rac-1 was kinetically resolved within 24 h producing pure (+)-1 with all enantiomeric excess (ee) of 100% after 75% conversion. This corresponds to a biochemical selectivity constant of E = 10.3 +/- 2.2. Thus, compared with conventional methods which use commercial baker's yeast as a biocatalyst, the reaction system was significantly improved, and Would be superior in a large-scale process. (C) 2008 Elsevier Ltd. All rights reserved. (Less)
Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Tetrahedron: Asymmetry
volume
19
issue
19
pages
2293 - 2295
publisher
Elsevier
external identifiers
  • wos:000261369200011
  • scopus:54849410469
ISSN
0957-4166
DOI
10.1016/j.tetasy.2008.09.024
language
English
LU publication?
yes
id
cd7af1b2-3d8e-48c6-9fd5-d9053203125d (old id 1304349)
date added to LUP
2009-03-23 14:35:44
date last changed
2017-01-01 06:00:20
@article{cd7af1b2-3d8e-48c6-9fd5-d9053203125d,
  abstract     = {Whole cells of the genetically engineered Saccharomyces cerevisiae strain TMB4100 (1% PGI, YMR226c) were Used as the biocatalyst for the kinetic resolution of racemic bicyclo[3.3.1]nonane-2,6-dione rac-1. The yeast's phosphoglucose isomerase activity was decreased, and the short-chain dehydrogenase/reductase encoded by YMR226c was overexpressed. This reduced the demand for the glucose to regenerate NADPH, while at the same time the reaction rate and selectivity towards (-)-1 became higher. The demand for yeast biomass also decreased, facilitating down-stream processing, which is of considerable importance oil a large scale. With 15 g dry weight/L of the genetically engineered yeast TMB4100 (1% PGI, YMR226c), 40 g/L rac-1 was kinetically resolved within 24 h producing pure (+)-1 with all enantiomeric excess (ee) of 100% after 75% conversion. This corresponds to a biochemical selectivity constant of E = 10.3 +/- 2.2. Thus, compared with conventional methods which use commercial baker's yeast as a biocatalyst, the reaction system was significantly improved, and Would be superior in a large-scale process. (C) 2008 Elsevier Ltd. All rights reserved.},
  author       = {Carlquist, Magnus and Wallentin, Carl-Johan and Wärnmark, Kenneth and Gorwa-Grauslund, Marie-Francoise},
  issn         = {0957-4166},
  language     = {eng},
  number       = {19},
  pages        = {2293--2295},
  publisher    = {Elsevier},
  series       = {Tetrahedron: Asymmetry},
  title        = {Genetically engineered Saccharomyces cerevisiae for kinetic resolution of racemic bicyclo[3.3.1]nonane-2,6-dione},
  url          = {http://dx.doi.org/10.1016/j.tetasy.2008.09.024},
  volume       = {19},
  year         = {2008},
}