Please use this identifier to cite or link to this item:
https://doi.org/10.1002/elsc.200700052
DC Field | Value | |
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dc.title | Enhanced asymmetric reduction of ethyl 3-oxobutyrate by baker's yeast via substrate feeding and enzyme inhibition | |
dc.contributor.author | Fow, K.-L. | |
dc.contributor.author | Poon, L.C.H. | |
dc.contributor.author | Sim, S.T. | |
dc.contributor.author | Chuah, G.K. | |
dc.contributor.author | Jaenicke, S. | |
dc.date.accessioned | 2014-06-23T05:38:49Z | |
dc.date.available | 2014-06-23T05:38:49Z | |
dc.date.issued | 2008-08 | |
dc.identifier.citation | Fow, K.-L., Poon, L.C.H., Sim, S.T., Chuah, G.K., Jaenicke, S. (2008-08). Enhanced asymmetric reduction of ethyl 3-oxobutyrate by baker's yeast via substrate feeding and enzyme inhibition. Engineering in Life Sciences 8 (4) : 372-380. ScholarBank@NUS Repository. https://doi.org/10.1002/elsc.200700052 | |
dc.identifier.issn | 16180240 | |
dc.identifier.uri | http://scholarbank.nus.edu.sg/handle/10635/76120 | |
dc.description.abstract | The moderate enantioselectivity of wild form baker's yeast can be considerably increased either by using continuous feeding to maintain a low substrate concentration throughout the reaction, or by the selective inhibition of competing enzymatic pathways. The reduction of ethyl 3-oxobutyrate to ethyl (S)-3-hydroxy-butyrate was used as a model reaction. With the substrate feeding method, the enantioselectivity could be increased from 75% to as high as 98%. The increased selectivity originates from the much higher substrate binding constant of the (R)-specific enzymes, so that these enzymes remain essentially inactive if a low concentration of ethyl 3-oxobutyrate is maintained in the bioreactor. Alternatively, the enantioselectivity of baker's yeast can be improved by selectively blocking competing enzymatic pathways. It was found that vinyl acetate is a selective inhibitor for the (R)-specific enzymes. Ethyl (S)-3-hydroxybutyrate with an enantiomeric excess of 98% was obtained by pre-incubation of baker's yeast in 100 mM of vinyl acetate solution for 1 h. These results suggest that by selecting appropriate process conditions, natural baker's yeast can be a competitive biocatalyst for the large-scale production of chiral secondary alcohols. © 2008 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim. | |
dc.description.uri | http://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1002/elsc.200700052 | |
dc.source | Scopus | |
dc.subject | (S)-3-hydroxybutyrate | |
dc.subject | Asymmetric synthesis | |
dc.subject | Baker's yeast | |
dc.subject | Enzyme inhibitor | |
dc.type | Article | |
dc.contributor.department | CHEMISTRY | |
dc.description.doi | 10.1002/elsc.200700052 | |
dc.description.sourcetitle | Engineering in Life Sciences | |
dc.description.volume | 8 | |
dc.description.issue | 4 | |
dc.description.page | 372-380 | |
dc.description.coden | ELSNA | |
dc.identifier.isiut | 000259045800002 | |
Appears in Collections: | Staff Publications |
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