Lipase-mediated epoxidation utilizing urea–hydrogen peroxide in ethyl acetate

Emanuel G. Ankudey, Horacio F. Olivo, Tonya L. Peeples

Research output: Contribution to journalArticle

98 Scopus citations

Abstract

A green method for alkene epoxidation based on the chemo-enzymatic perhydrolysis of carboxylic acids and esters has been optimized using Novozyme 435, the immobilized form of Candida antarctica lipase B, and the complex urea–hydrogen peroxide (UHP). UHP, an anhydrous form of hydrogen peroxide, has the potential of releasing hydrogen peroxide in a controlled manner and thus avoids the need to add the aqueous hydrogen peroxide slowly to the reaction mixture. The absence of water in the reaction media was also beneficial, because it minimized undesired reactions of the oxidized products. A minimum amount of enzyme was necessary to show the catalytic effect. On recycling, the enzyme maintained its activity up to six rounds of epoxidations. A range of alkenes was epoxidized by this method providing yields ranging from 75 to 100 percent.

Original languageEnglish (US)
Pages (from-to)923-926
Number of pages4
JournalGreen Chemistry
Volume8
Issue number10
DOIs
StatePublished - Oct 1 2006

All Science Journal Classification (ASJC) codes

  • Environmental Chemistry
  • Pollution

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