Enzymatic Esterification in Aqueous Miniemulsions

Aschenbrenner, Eugen M.; Weiss, Clemens K.; Landfester, Katharina

doi:10.1002/chem.200801691

Cited by 41 publications

(42 citation statements)

References 37 publications

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“…Moreover, many biocatalytic processes use water-organic solvent biphasic systems as reaction media (Cunnah et al, 1996;Gröger et al, 2006;Taden et al, 2003). Aqueous miniemulsions have proven to be a suitable and convenient reaction system for acid and lipase catalyzed reactions (Aschenbrenner et al, 2009;Barrère and Landfester, 2003;de Barros et al, 2009a). Miniemulsions are heterophase systems where small droplets with high stability in a continuous phase are created by using high shear forces, for example, created by ultrasonication.…”

Section: Introductionmentioning

confidence: 99%

Miniemulsion as efficient system for enzymatic synthesis of acid alkyl esters

Barros

Fonseca

Aschenbrenner

et al. 2010

Biotech & Bioengineering

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The aim of this work is to devise an efficient enzymatic process for the production of linear alkyl esters in aqueous miniemulsion systems. The esterification reactions of linear alcohols and carboxylic acids were performed with three different enzymes, commercial Amano lipase PS from Pseudomonas cepacia, Lipase type VII from Candida rugosa, and lyophilized Fusarium solani pisi cutinase expressed in Saccharomyces cerevisiae SU50. The miniemulsion system shows a high potential for the synthesis of linear alkyl esters, for example, hexyl octanoate, which could be synthesized with an ester yield of 94% using Amano lipase PS. Even with hydrophilic alcohols as ethanol, ethyl decanoate could be obtained with a concentration of 0.45 M and a yield of 62% using F. s. pisi cutinase as catalyst. High esterification rates for ethyl- and hexyloleate in miniemulsion showed a significant shift in cutinase selectivity towards longer chain length carboxylic acids. The stepwise addition of the alcohol led to an increase of the esterification yield. Moreover, increasing the amount of dispersed organic phase, mainly consisting of the substrates, led to a significant increase of the final ester concentration (e.g., concentration of 1.4 M for ethyl decanoate for the esterification with Amano Lipase PS).

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Section: Introductionmentioning

confidence: 99%

Miniemulsion as efficient system for enzymatic synthesis of acid alkyl esters

Barros

Fonseca

Aschenbrenner

et al. 2010

Biotech & Bioengineering

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“…Among these, are reports about triglyceride hydrolysis [33], ester synthesis [34][35][36][37] and the preparation of polyesters [38,39].…”

Section: Scheme 2 General Structure Of a Triacylglycerol (Triglycerimentioning

confidence: 99%

“…Inspired by these results, a detailed basic study on the esterification of carboxylic acids and phenylalkanoles in miniemulsion was presented by Aschenbrenner et al [34]. This study covers a variety of the aspects of lipase catalyzed esterification in miniemulsion.…”

Section: Small Moleculesmentioning

confidence: 99%

“…Lipase PS was found to be inhibited by the presence of excessive acid [34]; cutinase was found to be inhibited by excesses of alcohol in the reaction mixture in miniemulsion or organic solvents [49] and by excessive acid in reverse micelles with cetyl trimethyl ammonium bromide (CTAB) [50]. The conformation of cutinase was found to be crucially dependent on the ratio of acid/alcohol in the miniemulsion droplet, which may be a reason for the inhibitory effect [35].…”

Section: Small Moleculesmentioning

confidence: 99%

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Enzymatic Catalysis at Interfaces—Heterophase Systems as Substrates for Enzymatic Action

Weiss

Landfester

2013

Catalysts

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Several important enzymatic reactions occurring in nature, such as, e.g., the digestion of fat, proceed only at the interface of two immiscible phases. Typically, these systems consist of an organic substrate, dispersed in an aqueous continuous phase, with a specialized enzyme capable of working at the interface. For adopting such a system for organic synthesis, a stable heterophase system with a large interfacial area is required. These prerequisites can be found in so-called miniemulsions. Such liquid-liquid heterophase systems feature droplets with sizes smaller than 500 nm, and more importantly, these emulsions do not suffer from Ostwald ripening, as conventional emulsions do. Consequently, the droplets show long-term stability, even throughout reactions conducted in the droplets. In this review, we will briefly discuss the physicochemical background of miniemulsions, provide a comprehensive overview of the enzymatically catalyzed reactions conducted in miniemulsions and, as data are available, to compare the most important features to conventional systems, as reverse microemulsions, (macro)emulsions and solvent-based systems.

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“…[29][30][31] A substantial number of investigations have been performed to entrap lipases inside mesoporous silicas that were tailored with various organic groups. Owing to its unique catalytic mechanism, lipases feature notable sensitivity towards hydrophilic/hydrophobic surfaces.…”

Section: Introductionmentioning

confidence: 99%

Enzyme Entrapped in Polymer‐Modified Nanopores: The Effects of Macromolecular Crowding and Surface Hydrophobicity

Liu

Peng

Shen

et al. 2013

Chemistry A European J

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Macromolecular crowding is an ubiquitous phenomenon in living cells that significantly affects the function of enzymes in vivo. However, this effect has not been paid much attention in the research of the immobilization of enzymes onto mesoporous silica. Herein, we report the combined effects of macromolecular crowding and surface hydrophobicity on the performance of an immobilized enzyme by accommodating lipase molecules into a series of mesoporous silicas with different amounts of inert poly(methacrylate) (PMA) covalently anchored inside the nanopores. The incorporation of the PMA polymer into the nanopores of mesoporous silica enables the fabrication of a crowded and hydrophobic microenvironment for the immobilized enzyme and the variation in polymer content facilitates an adjustment of the degree of crowding and surface properties of this environment. Based on this system, the catalytic features of immobilized lipase were investigated as a function of polymer content in nanopores and the results indicated that the catalytic efficiency, thermostability, and reusability of immobilized lipase could all be improved by taking advantage of the macromolecular crowding effect and surface hydrophobicity. These findings provide insight into the possible functions of the macromolecular crowding effect, which should be considered and integrated into the fabrication of suitable mesoporous silicas to improve enzyme immobilization.

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Enzymatic Esterification in Aqueous Miniemulsions

Cited by 41 publications

References 37 publications

Miniemulsion as efficient system for enzymatic synthesis of acid alkyl esters

Miniemulsion as efficient system for enzymatic synthesis of acid alkyl esters

Enzymatic Catalysis at Interfaces—Heterophase Systems as Substrates for Enzymatic Action

Enzyme Entrapped in Polymer‐Modified Nanopores: The Effects of Macromolecular Crowding and Surface Hydrophobicity

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