Biosynthesis of ethyl caproate and other short ethyl esters catalyzed by cutinase in organic solvent

Barros, Dragana P.C. de; Fonseca, Luís P.; Fernandes, Pedro; Cabral, Joaquim M. S.; Mojović, Ljiljana

doi:10.1016/j.molcatb.2009.05.004

Cited by 41 publications

(42 citation statements)

References 36 publications

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“…For this reason it is interesting to evaluate the performance of Amano lipase PS in comparison to other enzymes such as commercial C. rugosa lipase and F. s. pisi cutinase, produced as previously reported (Calado et al, 2003). These enzymes were also successfully used on the biosyntheses of alkyl esters mainly in the others different reactions media (de Barros et al, 2009b;Nagayama et al, 2002;Salum et al, 2008).…”

Section: Influence Of Different Enzymes On Esterification Yield In MImentioning

confidence: 97%

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: Influence Of Different Enzymes On Esterification Yield In MImentioning

confidence: 97%

Miniemulsion as efficient system for enzymatic synthesis of acid alkyl esters

Barros

Fonseca

Aschenbrenner

et al. 2010

Biotech & Bioengineering

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“…This may be ascribed to the acidification of the microenvironment of the enzyme induced by acids and to tampering with the three-dimensional active structure of the enzyme, as well as a possible interaction with the enzyme essential water, promoted by a short chain alcohol (ethanol) of polar nature. Nevertheless a 97% yield was obtained for ethyl caproate, for an alcohol: acid molar ratio R=2 and 0.2 mol L −1 alcohol, and a reaction period of 6 h. 30 The present work aims to establish key conditions that allow for the sustained use of lyophilized cutinase for esterification in long-term operations, in the presence of organic solvents. The influence of the nature of reaction media on the cutinase activity was measured at fixed a w = 0.75, the value optimized in previous work.…”

Section: Introductionmentioning

confidence: 98%

“…The stability of lyophilized cutinase, specially in organic solvent media, on the other hand, was rarely addressed, despite the wide use of such formulation. The main goal of the present work was to evaluate the catalytic activity and stability of lyophilized cutinase as a function of the medium composition, which was shown to play a key role in cutinase performance in esterification reaction in an organic solvent system, 30 in order to optimize the enzymatic synthesis of short chain ethyl esters.…”

Section: Introductionmentioning

confidence: 99%

Operational stability of cutinase in organic solvent system: model esterification of alkyl esters

Barros

Fernandes

Fonseca

2010

J of Chemical Tech & Biotech

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BACKGROUND: The present work aims to gain further insight on the use of Fusarium solani pisi cutinase from a Saccharomyces cerevisiae strain for the synthesis of short chain ethyl esters, a group of important fruit flavor compounds, in a non-conventional environment. Synthesis is promoted by cutinase in organic media, in particular, in iso-octane, an organic solvent recognized as a safe ingredient in food and beverage industrial processes.

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“…Enzymatic esterification in miniemulsion using lipases and cutinase, an enzyme that is functionally related to the lipases, but also able to work in the aqueous phase [30], was used in miniemulsion for the preparation of industrially relevant flavor esters (acids: C6-C10, C18; alcohols: C2-C6) [35][36][37]46]. When cutinase is used for esterification in organic solvents, such as, e.g., hexane [37] or iso-octane [47][48][49] or reverse micellar systems [50,51], a preference for short-chain carboxylic acids is observed, which is manifested in higher reaction rates and significant ester yields. In miniemulsion, only low yields of up to 20% of ester were obtained when ethanol was esterified with hexanoic or heptanoic acid, using Lipase PS, lipase from Candida rugosa or recombinant cutinase from Fusarium solani pisi.…”

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%

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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Biosynthesis of ethyl caproate and other short ethyl esters catalyzed by cutinase in organic solvent

Cited by 41 publications

References 36 publications

Miniemulsion as efficient system for enzymatic synthesis of acid alkyl esters

Miniemulsion as efficient system for enzymatic synthesis of acid alkyl esters

Operational stability of cutinase in organic solvent system: model esterification of alkyl esters

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

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