Baeyer-Villiger oxidation with peracid generated in situ by CaLB-CLEA catalyzed perhydrolysis
(2013) In Journal of Molecular Catalysis B: Enzymatic 89. p.67-72- Abstract
- Candida antarctica lipase B, immobilized as cross linked enzyme aggregates (CLEAs) was used to mediate the Baeyer-Villiger oxidation of cyclohexanone to epsilon-caprolactone, and the reaction was compared with the one using Novozym (R) 435 as catalyst. The conversion was dependent on the initial concentration of cyclohexanone, and was about 90% after 48 h at concentrations of up to 0.25 M but was decreased at higher concentrations. Caprolactone concentrations up to 0.6 M had no effect on the reaction efficiency. Among the cyclic ketones tested, the highest degree of conversion was achieved for cyclopentanone (88%) and the lowest for cyclooctanone (about 2%). The effect of methyl substitution and position of substitution on the cycloketone... (More)
- Candida antarctica lipase B, immobilized as cross linked enzyme aggregates (CLEAs) was used to mediate the Baeyer-Villiger oxidation of cyclohexanone to epsilon-caprolactone, and the reaction was compared with the one using Novozym (R) 435 as catalyst. The conversion was dependent on the initial concentration of cyclohexanone, and was about 90% after 48 h at concentrations of up to 0.25 M but was decreased at higher concentrations. Caprolactone concentrations up to 0.6 M had no effect on the reaction efficiency. Among the cyclic ketones tested, the highest degree of conversion was achieved for cyclopentanone (88%) and the lowest for cyclooctanone (about 2%). The effect of methyl substitution and position of substitution on the cycloketone was studied using methylcyclohexanone and it has shown to influence the conversion efficiency. Both hydrogen peroxide and the reaction by-product acetic acid had a deleterious effect on the stability of the biocatalyst. (C) 2012 Elsevier B.V. All rights reserved. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/3669846
- author
- Chávez, Georgina LU ; Hatti-Kaul, Rajni LU ; Sheldon, Roger A. and Mamo, Gashaw LU
- organization
- publishing date
- 2013
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- Lipase, CLEAs, Baeyer-Villiger oxidation, epsilon-Caprolactone
- in
- Journal of Molecular Catalysis B: Enzymatic
- volume
- 89
- pages
- 67 - 72
- publisher
- Elsevier
- external identifiers
-
- wos:000315552300011
- scopus:84872977574
- ISSN
- 1873-3158
- DOI
- 10.1016/j.molcatb.2012.12.007
- language
- English
- LU publication?
- yes
- id
- 0809f698-973e-48fe-a727-7eefea5fb383 (old id 3669846)
- date added to LUP
- 2016-04-01 10:57:01
- date last changed
- 2022-03-05 00:20:30
@article{0809f698-973e-48fe-a727-7eefea5fb383,
abstract = {{Candida antarctica lipase B, immobilized as cross linked enzyme aggregates (CLEAs) was used to mediate the Baeyer-Villiger oxidation of cyclohexanone to epsilon-caprolactone, and the reaction was compared with the one using Novozym (R) 435 as catalyst. The conversion was dependent on the initial concentration of cyclohexanone, and was about 90% after 48 h at concentrations of up to 0.25 M but was decreased at higher concentrations. Caprolactone concentrations up to 0.6 M had no effect on the reaction efficiency. Among the cyclic ketones tested, the highest degree of conversion was achieved for cyclopentanone (88%) and the lowest for cyclooctanone (about 2%). The effect of methyl substitution and position of substitution on the cycloketone was studied using methylcyclohexanone and it has shown to influence the conversion efficiency. Both hydrogen peroxide and the reaction by-product acetic acid had a deleterious effect on the stability of the biocatalyst. (C) 2012 Elsevier B.V. All rights reserved.}},
author = {{Chávez, Georgina and Hatti-Kaul, Rajni and Sheldon, Roger A. and Mamo, Gashaw}},
issn = {{1873-3158}},
keywords = {{Lipase; CLEAs; Baeyer-Villiger oxidation; epsilon-Caprolactone}},
language = {{eng}},
pages = {{67--72}},
publisher = {{Elsevier}},
series = {{Journal of Molecular Catalysis B: Enzymatic}},
title = {{Baeyer-Villiger oxidation with peracid generated in situ by CaLB-CLEA catalyzed perhydrolysis}},
url = {{http://dx.doi.org/10.1016/j.molcatb.2012.12.007}},
doi = {{10.1016/j.molcatb.2012.12.007}},
volume = {{89}},
year = {{2013}},
}