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

Autor:	Horacio F. Olivo, Emanuel G. Ankudey, Tonya L. Peeples
Rok vydání:	2006
Předmět:	chemistry.chemical_classification Aqueous solution biology Chemistry Ethyl acetate biology.organism_classification Pollution Peroxide chemistry.chemical_compound Enzyme Anhydrous biology.protein Environmental Chemistry Organic chemistry Candida antarctica Lipase Hydrogen peroxide
Zdroj:	Green Chem.. 8:923-926
ISSN:	1463-9270 1463-9262
Popis:	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.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::b83c8c45ab22c925416475bb56d8b183 https://doi.org/10.1039/b604984b Zobrazit plný text záznamu