Optimization of Chemo‐Enzymatic Epoxidation of Cyclohexene Mediated by Lipases

Moreira, Matheus T.; Bitencourt, Thiago Bergler; Nascimento, Maria da Graça

doi:10.1081/scc-200066705

Cited by 37 publications

(11 citation statements)

References 15 publications

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“…Moreover these techniques exhibit a high potential to catalyze unwanted hydrolytic side reactions. If possible the handling of the hazardous peroxy acids on an industrial scale generally is to be avoided [7,9,10]. Therefore, on an industrial level, epoxides are typically synthesized either by direct oxidation, by the chlorohydrin method or by the in situgeneration of peroxy acids from formic or acetic acid and hydrogen peroxide, and often with addition of minc 2012 Verlag der Zeitschrift für Naturforschung, Tübingen · http://znaturforsch.com Scheme 1.…”

Section: Introductionmentioning

confidence: 99%

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: 99%

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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“…17,22 It has been described that CAL-B efficiently hydrolyzes triacylglycerols because it produces free fatty acids that form peracids in the presence of hydrogen peroxide, which then epoxidize the unsaturated bonds. 24 The reactivity and concentration of the peracid may also be responsible for lipase denaturation.…”

Section: Comparison Between Mono and Biphasic Systemmentioning

confidence: 99%

“…16,21,22 In biocatalyzed reactions, enzymatic activity may also be lost due to elevated concentrations of hydrogen peroxide or to temperature effects. However, some recent papers have shown that Candida antarctida B lipase remained stable above 50 °C, although this was not favorable, mainly due to the decomposition of hydrogen peroxide.…”

Section: Introductionmentioning

confidence: 99%

Chemo-enzymatic epoxidation of sunflower oil methyl esters

Schneider¹,

Lara²,

Bitencourt³

et al. 2009

J. Braz. Chem. Soc.

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“…As the oxygen from the peracid is utilized for epoxidation of the double bond in the unsaturated compound, the acid is regenerated and becomes available to the enzyme for further reaction. Such a method has mostly been used for epoxidation of fatty acids having internal double bonds [8], but has also been reported for epoxidation of various other organic compounds ranging from cyclohexene to alpha-pinene and styrene [9][10][11][12]. In this context it should be stressed that the choice of alkene substrate has an enormous impact on the results, as different molecules vary greatly in their readiness to be epoxidised.…”

Section: Introductionmentioning

confidence: 99%

Production of glycidyl ethers by chemo-enzymatic epoxidation of allyl ethers

Tufvesson

Adlercreutz

Lundmark

et al. 2008

Journal of Molecular Catalysis B: Enzymatic

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Production of glycidyl ethers is industrially carried out by reacting alcohols with epichlorhydrin, a potentially carcinogenic compound. This paper investigates a less hazardous alternative -that of a chemo-enzymatic process in which Candida antarctica lipase B catalysed generation of peracid from a carboxylic acid is followed by a Prileshajev epoxidation of the corresponding allyl ether.Trimethylolpropane monoallyl ether (TMPME) was used as a model substrate. A maximal epoxide product yield of 77% was achieved through the optimization of temperature, acid concentration and hydrogen peroxide concentration. Peracid formation was considerably faster than the subsequent epoxidation step, and accumulation of the peracid was found to be important to drive the epoxidation forward.

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Optimization of Chemo‐Enzymatic Epoxidation of Cyclohexene Mediated by Lipases

Cited by 37 publications

References 15 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

Chemo-enzymatic epoxidation of sunflower oil methyl esters

Production of glycidyl ethers by chemo-enzymatic epoxidation of allyl ethers

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