Epoxidation and Baeyer–Villiger oxidation using hydrogen peroxide and a lipase dissolved in ionic liquids

Kotlewska, Aleksandra J.; Rantwijk, Fred van; Sheldon, Roger A.; Arends, Isabel W. C. E.

doi:10.1039/c1gc15255f

Cited by 107 publications

(64 citation statements)

References 82 publications

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“…Within this class of enzymes, perhydrolases are able to efficiently catalyze perhydrolysis reactions for the formation of peracids [5,6], but the unusual participation of lipases for global oxidative process has attracted the attention of different research groups in the last decade [5,7,8]. Thus, examples of lipase-mediated epoxidation [9][10][11][12][13][14], Baeyer-Villiger reactions [15][16][17][18][19], perhydrolysis of carboxylic acid and esters [20], sequential Baeyer-Villiger reaction and ring-opening polymerization [21], and also consecutive esterification and Baeyer-Villiger cascade reactions [22] have appeared in the literature, giving access to synthetically useful oxygenated heterocycles through clean and selective transformations under mild reaction conditions.…”

Section: Introductionmentioning

confidence: 99%

Lactonization reactions through hydrolase-catalyzed peracid formation. Use of lipases for chemoenzymatic Baeyer–Villiger oxidations of cyclobutanones

González‐Martínez

Rodríguez‐Mata

Méndez-Sánchez

et al. 2015

Journal of Molecular Catalysis B: Enzymatic

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Abstract:A one-pot chemoenzymatic method has been described for the synthesis of -butyrolactones starting from the corresponding ketones through a Baeyer-Villiger reaction.The approach is based on a lipase-catalyzed perhydrolysis for the formation of peracetic acid, which is the responsible for the ketone oxidation. Optimization studies have been performed in the oxidation of cyclobutanone, finding Candida antarctica lipase type B, ethyl acetate and urea-hydrogen peroxide complex as the best system. The relative ratio of these reagents has also been analyzed in depth. This synthetic approach has been successfully extended to a family of 3-substituted cyclobutanones in high substrate concentration, yielding the corresponding lactones with excellent isolated yields and purities, under mild reaction conditions and after a simple extraction protocol.

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Section: Introductionmentioning

confidence: 99%

Lactonization reactions through hydrolase-catalyzed peracid formation. Use of lipases for chemoenzymatic Baeyer–Villiger oxidations of cyclobutanones

González‐Martínez

Rodríguez‐Mata

Méndez-Sánchez

et al. 2015

Journal of Molecular Catalysis B: Enzymatic

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“…Many of these studies involve lipases. Lipases are used in chemo-enzymatic epoxidations of diverse substances (Table 1) [10,11,[240][241][242][243]. In this reaction, hydrogen peroxide (or some derivative) is one of the reaction substrate, and it has been shown that the catalytic residue of the enzyme is involved [244].…”

Section: Immobilizationmentioning

confidence: 99%

Hydrogen Peroxide in Biocatalysis. A Dangerous Liaison

Hernández

Berenguer-Murcia²,

Rodrigues³

et al. 2012

COC

138

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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“…Recently, lipase-catalyzed perhydrolysis of carboxylic acids or esters, resulting in the formation of reactive peroxycarboxylic acids, have been studied as interesting cases of lipase catalytic promiscuity [8]. The in situ generated peroxycarboxylic acids by perhydrolysis have been directly used to oxidize ketones, alkenes, sulfides, enaminones, and amines [9][10][11][12][13][14]. However, lipase-catalysis of other oxidative reactions has been less explored, especially with alcohols as starting substrates.…”

Section: Introductionmentioning

confidence: 99%