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

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

doi:10.1039/b604984b

Cited by 119 publications

(69 citation statements)

References 20 publications

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“…The first industrially important products such as environment-friendly PVC stabilizers and solubilizers on the basis of epoxidized soybean oil have successfully been produced via this chemo-enzymatic method [13]. Further work has also proven the general feasibility of this approach for the epoxidation of cyclic monoterpenes [4,5,8,14].…”

Section: Introductionmentioning

confidence: 91%

Lipase-mediated Epoxidation of the Cyclic Monoterpene Limonene to Limonene Oxide and Limonene Dioxide

Wiemann

Faltl²,

Sieber³

2012

Zeitschrift Für Naturforschung B

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Limonene is an industrially interesting monoterpene that accumulates in bulk quantities as byproduct of the fruit juice industry. The corresponding epoxides are versatile synthetic intermediates and additives for the chemical industry. Due to a number of disadvantages of classical chemical epoxidation including serious safety issues and unwanted side-reactions, we here used a mild lipasecatalyzed chemo-enzymatic epoxidation system, with either free or different immobilized forms of Candida antarctica lipase B. Full limonene conversion (> 98 %) was easily achieved at 40 • C within less than 24 h. The enzymatic activities in the formation of limonene monoxide significantly varied from either 1 -3.4 U/mg biocatalyst at r. t. or from 1.7 -4.9 U/mg biocatalyst at 40 • C. For the first time we showed that it is possible to generate high amounts of limonene dioxide (∼ 30 % with CalB on carrier 350 at 40 • C) using this mild lipase-mediated epoxidation method. Enzyme activities and limonene dioxide yields strongly depend on the nature of the selected enzyme carrier, the immobilization method and the reaction temperature.

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Section: Introductionmentioning

confidence: 91%

Lipase-mediated Epoxidation of the Cyclic Monoterpene Limonene to Limonene Oxide and Limonene Dioxide

Wiemann

Faltl²,

Sieber³

2012

Zeitschrift Für Naturforschung B

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“…102,103,116 Some potential alternatives to hydrogen peroxide as an oxidant were also investigated. For example, Ankudey et al 120 proposed the use of urea hydrogen peroxide and suggest that this oxidant would limit the deactivation of the lipase in comparison with what was observed with hydrogen peroxide. However, these observations were not confirmed by Törnvall et al 119 who did not observe any significant differences between those two oxidants in terms of enzyme deactivation effect.…”

Section: Ii2 Factors Governing the Efficiency Of Lipase-catalyzed Epmentioning

confidence: 99%

The use of lipases as biocatalysts for the epoxidation of fatty acids and phenolic compounds

et al. 2014

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Lipases are versatile enzymes that can be used for various kinds of biocatalyzed reactions. Owing to their selectivity and their mild reaction conditions, they can be often considered as more interesting than classical chemical catalysts. Besides their application in oil and fat processes, these enzymes have proved to be very attractive for other lipase-catalyzed reactions. This review discusses the latest results where lipases are used for the epoxidation of lipid substrates (namely fatty acids and their derivatives) and phenolic compounds. This chemo-enzymatic process involves a two step synthesis where the biocatalyst acts as a perhydrolase to produce peracids, which then act as catalysts to epoxidize double bonds. Various factors govern the efficiency of the reaction in terms of kinetics, yields and enzyme stability.These parameters are evaluated and discussed herein. (Résumé d'auteur

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“…For example, alkene epoxidation based on the chemo-enzymatic perhydrolysis of carboxylic acids and esters has been optimized using Novozyme 435 (immobilized lipase B from Candida antarctica) and the complex urea-hydrogen peroxide [202]. Urea-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.…”

Section: Keeping Hydrogen Peroxide Concentration At Low Levelsmentioning

confidence: 99%

Hydrogen Peroxide in Biocatalysis. A Dangerous Liaison

Hernández

Berenguer-Murcia²,

Rodrigues³

et al. 2012

COC

137

107

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Hydrogen peroxide is a substrate or side-product in many enzyme-catalyzed reactions. For example, it is a side-product of oxidases, resulting from the re-oxidation of FAD with molecular oxygen, and it is a substrate for peroxidases and other enzymes. However, hydrogen peroxide is able to chemically modify the peptide core of the enzymes it interacts with, and also to produce the oxidation of some cofactors and prostetic groups (e.g., the hemo group). Thus, the development of strategies that may permit to increase the stability of enzymes in the presence of this deleterious reagent is an interesting target. This enhancement in enzyme stability has been attempted following almost all available strategies: site-directed mutagenesis (eliminating the most reactive moieties), medium engineering (using stabilizers), immobilization and chemical modification (trying to generate hydrophobic environments surrounding the enzyme, to confer higher rigidity to the protein or to generate oxidation-resistant groups), or the use of systems capable of decomposing hydrogen peroxide under very mild conditions. If hydrogen peroxide is just a side-product, its immediate removal has been reported to be the best solution. In some cases, when hydrogen peroxide is the substrate and its decomposition is not a sensible solution, researchers coupled one enzyme generating hydrogen peroxide "in situ" to the target enzyme resulting in a continuous supply of this reagent at low concentrations thus preventing enzyme inactivation.This review will focus on the general role of hydrogen peroxide in biocatalysis, the main mechanisms of enzyme inactivation produced by this reactive and the different strategies used to prevent enzyme inactivation caused by this "dangerous liaison". Outlook

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

Cited by 119 publications

References 20 publications

Lipase-mediated Epoxidation of the Cyclic Monoterpene Limonene to Limonene Oxide and Limonene Dioxide

Lipase-mediated Epoxidation of the Cyclic Monoterpene Limonene to Limonene Oxide and Limonene Dioxide

The use of lipases as biocatalysts for the epoxidation of fatty acids and phenolic compounds

Hydrogen Peroxide in Biocatalysis. A Dangerous Liaison

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