| dc.contributor.author | Lund, Ingvild | |
| dc.contributor.author | Bøckmann, Pål Lønnegraff | |
| dc.contributor.author | Jacobsen, Elisabeth Egholm | |
| dc.date.accessioned | 2016-11-23T10:45:43Z | |
| dc.date.accessioned | 2021-11-17T09:25:50Z | |
| dc.date.available | 2016-11-23T10:45:43Z | |
| dc.date.available | 2021-11-17T09:25:50Z | |
| dc.date.issued | 2016 | |
| dc.identifier.citation | Tetrahedron 2016, 72:7288-7299 | en_US |
| dc.identifier.issn | 1464-5416 | |
| dc.identifier.uri | https://hdl.handle.net/11250/2830017 | |
| dc.description.abstract | Both enantiomers of 4-(3-chloro-2-hydroxypropoxy)phenyl)acetamide has been synthesized in 98.5–99% enantiomeric excess by use of lipase B from Candida antarctica as catalyst. The R-alcohol is a building block for the cardioselective β-blocker (S)-atenolol ((S)-2-(4-(2-hydroxy-3-(isopropylamino)propoxy)phenyl)acetamide. Performing kinetic resolutions of 3-chloro-1-phenoxy-2-propanol and 3-bromo-1-phenoxy-2-propanol with vinyl butanoate as acyl donor and the same CALB enzyme, but a different preparation, showed higher E-values than previously reported. | en_US |
| dc.language.iso | eng | en_US |
| dc.publisher | Elsevier | en_US |
| dc.title | Highly enantioselective CALB-catalyzed kinetic resolution ofbuilding blocks for β-blocker atenolol | en_US |
| dc.type | Journal article | en_US |
| dc.date.updated | 2016-11-23T10:45:43Z | |
| dc.description.version | publishedVersion | en_US |
| dc.rights.holder | This article will not be available due to copyright restrictions by Elsevier | en_US |
| dc.source.pagenumber | 7288-7299 | en_US |
| dc.source.volume | 72 | en_US |
| dc.source.journal | Tetrahedron | en_US |
| dc.identifier.doi | 10.1016/j.tet.2016.02.018 | |
| dc.identifier.cristin | 1352086 | |
