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dc.contributor.authorJacobsen, Elisabeth Egholm
dc.contributor.authorAnthonsen, Thorleif
dc.contributor.authorEl-Behairy, Mohammed Farrag
dc.contributor.authorSundby, Eirik
dc.contributor.authorAboul-Enein, Mohamed Nabil
dc.contributor.authorAttia, Mohamed Ibrahim
dc.contributor.authorEl-Azzouny, Aida Abd El-Sattar
dc.contributor.authorAmin, Kamilia M.
dc.contributor.authorAbdel-Rehim, Mohamed
dc.date.accessioned2016-11-23T11:16:07Z
dc.date.accessioned2017-02-07T13:39:46Z
dc.date.available2016-11-23T11:16:07Z
dc.date.available2017-02-07T13:39:46Z
dc.date.issued2012
dc.identifier.citationInternational Journal of Chemistry 2012, 4(1):7-13nb_NO
dc.identifier.issn1916-9701
dc.identifier.urihttp://hdl.handle.net/11250/2429815
dc.description.abstractKinetic resolution of rac-Stiripentol, catalysed by lipase A from Candida antarctica by esterification with vinyl butanoate was performed with an E-value of 24. This allowed isolation of (3S)-Stiripentol with an ee of 86 % and the corresponding (3R)-butanoate with an ee of 87 %. Enzymatic hydrolysis of the ester product gave (3R)-Stiripentol with 94 % ee.nb_NO
dc.language.isoengnb_NO
dc.publisherCanadian Center of Science and Education (CCSE)nb_NO
dc.titleLipase Catalysed Kinetic Resolution of Stiripentolnb_NO
dc.typeJournal articlenb_NO
dc.typePeer reviewednb_NO
dc.date.updated2016-11-23T11:16:07Z
dc.source.pagenumber7-13nb_NO
dc.source.volume4nb_NO
dc.source.issue1nb_NO
dc.identifier.doi10.5539/ijc.v4n1p7
dc.identifier.cristin902718
dc.description.localcodeCreative Commons Attribution License 3.0nb_NO


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