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dc.contributor.authorKoźniewski, Bartłomiej
dc.contributor.authorKamińska, Janina
dc.date.accessioned2015-06-03T11:11:22Z
dc.date.available2015-06-03T11:11:22Z
dc.date.issued2011
dc.identifier.citationBiotechnology and Food Science, 2011 Vol.75 nr 1 s.3-14
dc.identifier.issn2084-0136
dc.identifier.other0000035870
dc.identifier.otherKontynuacja Zeszytów Naukowych Politechniki Łódzkiej, serii Chemia Spożywcza i Biotechnologia.
dc.identifier.urihttp://hdl.handle.net/11652/270
dc.description.abstract(±)-N-Benzoyl-α-methylserine ethyl ester and (±)-4- hydroxymethyl-4-methyl-2-phenyl-1,3-oxazol-5(4H)-one were synthesized and used as substrates for enzyme catalyzed kinetic resolution in organic solvents. Several lipases active for O-acetylation of both compounds were found. The most active enzymes were screened for influence of solvent, acetyl donor type, its concentration, biocatalyst quantity and reaction temperature on resolution rate and enantioselectivity ratio E. For acetylation of (±)-N-benzoyl-α-methylserine ethyl ester with isopropenyl acetate in the presence of Novozym ® 435 the highest enantioselectivity E = 35 was found, yielding at 54% conversion (S)-N-Benzoyl-α-methylserine ethyl ester with 94% ee and (R)-O-acetyl-N-benzoyl-α-methylserine ethyl ester with 82% ee.en_EN
dc.formatapplication/pdf
dc.language.isoenen_EN
dc.publisherWydawnictwo Politechniki Łódzkiejpl_PL
dc.publisherLodz University of Technology. Pressen_EN
dc.relation.ispartofseriesZeszyty Naukowe Politechniki Łódzkiejpl_PL
dc.relation.ispartofseriesBiotechnology and Food Scienceen_EN
dc.titleResolution of α-methylserine dervatives via lipase mediated acetylationen_EN
dc.typeArticleen_EN
dc.typeArtykułpl_PL


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