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Lipase-Catalyzed Kinetic Resolution of Aryltrimethylsilyl Chiral Alcohols
Institute of Chemistry, University of São Paulo, Av. Prof. Lineu Prestes, n°. 748, SP 05508-900, São Paulo, Brazil
* Author to whom correspondence should be addressed.
Received: 27 September 2011; in revised form: 28 October 2011 / Accepted: 17 November 2011 / Published: 23 November 2011
Abstract: Lipase-catalyzed kinetic resolution of aryltrimethylsilyl chiral alcohols through a transesterification reaction was studied. The optimal conditions found for the kinetic resolution of m- and p-aryltrimethylsilyl chiral alcohols, led to excellent results, high conversions (c = 50%), high enantiomeric ratios (E > 200) and enantiomeric excesses for the remaining (S)-alcohol and (R)-acetylated product (>99%). However, kinetic resolution of o-aryltrimethylsilyl chiral alcohols did not occur under the same conditions applied to the other isomers.
Keywords: lipase; aryltrimethylsilyl chiral alcohols; kinetic resolution; transesterification
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MDPI and ACS Style
Palmeira, D.J.; Abreu, J.C.; Andrade, L.H. Lipase-Catalyzed Kinetic Resolution of Aryltrimethylsilyl Chiral Alcohols. Molecules 2011, 16, 9697-9713.
Palmeira DJ, Abreu JC, Andrade LH. Lipase-Catalyzed Kinetic Resolution of Aryltrimethylsilyl Chiral Alcohols. Molecules. 2011; 16(11):9697-9713.
Palmeira, Dayvson J.; Abreu, Juliana C.; Andrade, Leandro H. 2011. "Lipase-Catalyzed Kinetic Resolution of Aryltrimethylsilyl Chiral Alcohols." Molecules 16, no. 11: 9697-9713.