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Oxidation of trans- and cis-1,2-cyclohexanediol by Gluconobacter oxydans - Preparation of (R)- and (S)-2-hydroxycyclohexanone

Adlercreutz, Patrick LU orcid (1989) In Applied Microbiology and Biotechnology 30(3). p.257-263
Abstract

The enzymatic oxidation of 1,2-cyclohexanediol and related substrates by Gluconobacter oxydans (ATCC 621) was investigated. At low pH, membrane-bound enzymes were active and at high pH, NAD-dependent, soluble enzymes showed activity. Whole bacterial cells were used to catalyze some bioconversions. Racemic trans-1,2-cyclohexanediol was oxidized at pH 3.5 to give (R)-2-hydroxycyclohexanone (96% e.e.) and at pH 8.0 the same substrate was oxidized to (S)-2-hydroxycyclohexanone (97% e.e.). The latter conversion was severely inhibited by the reaction product while the former was not significantly product inhibited. (S)-2-hydroxycyclohexanone (97% e.e.) was also prepared from cis-1,2-cyclohexanediol by oxidation with G. oxydans cells at pH 3.5... (More)

The enzymatic oxidation of 1,2-cyclohexanediol and related substrates by Gluconobacter oxydans (ATCC 621) was investigated. At low pH, membrane-bound enzymes were active and at high pH, NAD-dependent, soluble enzymes showed activity. Whole bacterial cells were used to catalyze some bioconversions. Racemic trans-1,2-cyclohexanediol was oxidized at pH 3.5 to give (R)-2-hydroxycyclohexanone (96% e.e.) and at pH 8.0 the same substrate was oxidized to (S)-2-hydroxycyclohexanone (97% e.e.). The latter conversion was severely inhibited by the reaction product while the former was not significantly product inhibited. (S)-2-hydroxycyclohexanone (97% e.e.) was also prepared from cis-1,2-cyclohexanediol by oxidation with G. oxydans cells at pH 3.5 in a reaction which continued to 100% conversion.

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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Applied Microbiology and Biotechnology
volume
30
issue
3
pages
7 pages
publisher
Springer
external identifiers
  • scopus:0000893172
ISSN
0175-7598
DOI
10.1007/BF00256215
language
English
LU publication?
yes
id
ae05495c-72fa-4bed-b76a-637a9d8d8f1a
date added to LUP
2019-06-22 18:56:43
date last changed
2021-01-03 09:31:00
@article{ae05495c-72fa-4bed-b76a-637a9d8d8f1a,
  abstract     = {{<p>The enzymatic oxidation of 1,2-cyclohexanediol and related substrates by Gluconobacter oxydans (ATCC 621) was investigated. At low pH, membrane-bound enzymes were active and at high pH, NAD-dependent, soluble enzymes showed activity. Whole bacterial cells were used to catalyze some bioconversions. Racemic trans-1,2-cyclohexanediol was oxidized at pH 3.5 to give (R)-2-hydroxycyclohexanone (96% e.e.) and at pH 8.0 the same substrate was oxidized to (S)-2-hydroxycyclohexanone (97% e.e.). The latter conversion was severely inhibited by the reaction product while the former was not significantly product inhibited. (S)-2-hydroxycyclohexanone (97% e.e.) was also prepared from cis-1,2-cyclohexanediol by oxidation with G. oxydans cells at pH 3.5 in a reaction which continued to 100% conversion.</p>}},
  author       = {{Adlercreutz, Patrick}},
  issn         = {{0175-7598}},
  language     = {{eng}},
  month        = {{03}},
  number       = {{3}},
  pages        = {{257--263}},
  publisher    = {{Springer}},
  series       = {{Applied Microbiology and Biotechnology}},
  title        = {{Oxidation of trans- and cis-1,2-cyclohexanediol by Gluconobacter oxydans - Preparation of (R)- and (S)-2-hydroxycyclohexanone}},
  url          = {{http://dx.doi.org/10.1007/BF00256215}},
  doi          = {{10.1007/BF00256215}},
  volume       = {{30}},
  year         = {{1989}},
}