Oxidation of trans- and cis-1,2-cyclohexanediol by Gluconobacter oxydans - Preparation of (R)- and (S)-2-hydroxycyclohexanone
(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.
(Less)
- author
- Adlercreutz, Patrick LU
- organization
- publishing date
- 1989-03-01
- 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}}, }