Stability of cutinase, wild type and mutants, in AOT reversed micellar system—effect of mixture components of alkyl esters production

Badenes, Sara M.; Lemos, F.

doi:10.1002/jctb.2505

Cited by 7 publications

(11 citation statements)

References 26 publications

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“…AOT has been shown to have an inactivating effect on cutinases. For example, the F. solani pisi cutinase (1 mg/mL) lost 45 % of activity, when incubated in reverse micelles of AOT at 30°C for 3 h. Methanol, which was used as the substrate in addition to triolein in the transesterification reactions studied, was also found to inactivate the cutinase; 90 % of enzyme activity was lost in the presence of 390 mM methanol already after 10 min (Badenes et al 2011b). AOT has been reported to cause a conformational change in the active site.…”

Section: Cutinases In Biocatalysismentioning

confidence: 97%

Which properties of cutinases are important for applications?

Nyyssölä

2015

Appl Microbiol Biotechnol

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Cutinases (EC 3.1.1.74) are extracellular enzymes that belong to α/β hydrolases. They are serine esterases with the classical Ser-His-Asp triad similar to several lipases and serine proteases. In nature, cutinases catalyse the hydrolysis of the polyesters of the cuticle and the suberin layers, which protect plant surfaces. Cutinase production is typical for plant pathogenic fungi, but also, bacterial cutinases and cutinases from plant pollen have been discovered. Cutinases are promiscuous esterases catalysing reactions with a wide range of different substrates, such as short-chain soluble esters, water-insoluble medium and long-chain triacylglycerols, polyesters and waxes. In the current work, an overview is given on suggested applications of cutinases in the textile industry, in laundry detergents, in processing of biomass and food, in biocatalysis and in detoxification of environmental pollutants. The applications are discussed from the point of view of cutinase properties-which properties of cutinases are already advantageous and which would be desired. In addition, improvements that have been made on cutinase performance by protein and reaction engineering are reviewed.

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Section: Cutinases In Biocatalysismentioning

confidence: 97%

Which properties of cutinases are important for applications?

Nyyssölä

2015

Appl Microbiol Biotechnol

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“…In the first case, 32 h recirculation, the conversion decreases to a residual value after starting the continuous mode, most likely due to a dilution effect, as the enzyme was already fully denatured. This denaturation is caused by the toxic effect that methanol has towards cutinase wild type, as already observed in batch incubation tests in the presence of methanol (Badenes et al, 2011). In the second case, the 3 h were not enough to reach a steady-state to ensure that the enzyme was adsorbed onto the membrane.…”

Section: Evaluation Of Cutinase Membrane Reactor Performance In Contimentioning

confidence: 87%

“…In previous work, mutants of cutinase were evaluated in terms of their activity in the reversed micellar system and their stability in the presence of AOT (Badenes et al, 2011). It was found that the cutinase mutant T179C has a high resistance to the denaturing effect of AOT, and, even more, it has a higher stability in the presence of methanol when compared with cutinase wild type.…”

Section: Evaluation Of Cutinase Membrane Reactor Performance In Totalmentioning

confidence: 98%

“…This was confirmed by comparison of the specific activities calculated in the first 15 min of the transesterification of the two different commercial triolein, which was performed in a batch reactor. The specific activities were 2.64 mmol/min/mg (Badenes et al, 2011) and 0.14 mmol/min/mg/ for the first and the second batches, respectively.…”

Section: Evaluation Of Cutinase Membrane Reactor Performance In Totalmentioning

confidence: 99%

“…The fact that isooctane is used to stabilize the emulsion is consistent with the current use of biodiesel, which is mixed with diesel fuel. The activity and stability of the cutinase wild type and three mutants (L153Q, T179C, and S54D; Brissos et al, 2008a,b) in this system, and in the presence of the reaction components, were also assessed (Badenes et al, 2011).…”

Section: Introductionmentioning

confidence: 99%

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Performance of a cutinase membrane reactor for the production of biodiesel in organic media

Badenes

Lemos

Cabral

2011

Biotech & Bioengineering

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The enzymatic transesterification of oils with an alcohol, using recombinant cutinase of Fusarium solani pisi microencapsulated in sodium bis(2-ethylhexyl) sulfosuccinate (AOT)/isooctane reversed micelles, was performed in a membrane bioreactor (MBR). A tubular ceramic membrane with a nominal molecular weight cut off of 15,000 Da was used to retain the enzyme, and characterized in terms of rejection coefficients of the reaction components by transmission experiments. The performance of the MBR in a total recirculation-batch mode was compared with results obtained in a stirred batch tank reactor. The continuous operation of the MBR was also evaluated and the influence of the alcohol type and permeate flow rate on conversion degree and productivity (up to 500 g(product) /day/g(enzyme) was attained) were analyzed. Cutinase wild type and mutant T179C were tested for this process and the high long-term operational stability of the cutinase mutant demonstrated its potential as biocatalyst for the enzymatic continuous production of biodiesel.

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Membrane Bioreactors for Biofuel Production

Badenes

Ferreira

2013

Separation and Purification Technologies in Biorefineries

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Stability of cutinase, wild type and mutants, in AOT reversed micellar system—effect of mixture components of alkyl esters production

Cited by 7 publications

References 26 publications

Which properties of cutinases are important for applications?

Which properties of cutinases are important for applications?

Performance of a cutinase membrane reactor for the production of biodiesel in organic media

Membrane Bioreactors for Biofuel Production

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