Enzyme and organic solvents: Horse liver alcohol dehydrogenase in non‐ionic microemulsion: Stability and activity

Lee, Kangmin; Biellmann, Jean‐François

doi:10.1016/0014-5793(87)80504-5

Cited by 26 publications

(9 citation statements)

References 12 publications

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“…The T/max was higher at wo = 10, where the ratio V,,,/K,,, amounted to 21% of that in buffer. These results are similar to the data obtained for other enzymes [3]. The effect of water volume fraction (8) in the catecholase activity at (JO constant (WO = 10) is shown in fig.4a.…”

Section: Resultssupporting

confidence: 89%

“…Although a number of enzymes have been investigated in such media, most work has been carried out on hydrolases (a-chymotrypsin and lipases) and dehydrogenases but not on oxidases [l]. The surfactants mostly employed are AOT, CTAB, SDS and Triton X-100 [3] but only few enzymes have been entrapped in Brij 96 [4]. We describe here for the first time some kinetic parameters of a mem- The standard reaction media contained 0.5 mM 4-methyl catechol, 0.166 M Brij 96, ~0 = 10, B = 0.6%, 15 pg/ml of PPO in 50 mM acetate buffer, pH 5.0, at 25"C, unless stated otherwise.…”

Section: Introductionmentioning

confidence: 99%

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Kinetic properties of polyphenoloxidase in organic solvents A study in Brij 96‐cyclohexane reverse micelles

1988

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Polyphenoloxidase entrapped in Brij 96-cyclohexame reverse micelles showed both cresolase activity towards monophenols and catecholase activity towards diphenols. The kinetic parameters, such as apparent K,,,, temperature effect and pH profile, were determined for catecholase activity, the findings being very close to those found in aqueous systems. The enzyme activity was dependent on the molecular ratio of water to surfactant (o,), obtaining a maximum activity at o, = IO. The stability of the system with time increased with the water content until W, = 10, and then decreased. An inverse relation was found between activity and water volume fraction (6)

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Section: Resultssupporting

confidence: 89%

Section: Introductionmentioning

confidence: 99%

Kinetic properties of polyphenoloxidase in organic solvents A study in Brij 96‐cyclohexane reverse micelles

1988

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“…In the case of SDS microemulsion, the velocity increased as the water content increased but in CTAB microemulsion, the velocity did not show a clear dependence on the water content. The same group studied the behavior of HLADH in a cyclohexane/Triton X-100/1-butanol/water system where 1-butanol worked as both co-surfactant and a substrate [108]. They concluded that the enzyme in the above microemulsion has a higher stability over time in comparison to other microemulsions with anionic surfactants.…”

Section: Dehydrogenasesmentioning

confidence: 99%

Oxidation Catalysis by Enzymes in Microemulsions

2017

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Microemulsions are regarded as "the ultimate enzyme microreactors" for liquid oxidations. Their structure, composed of water nanodroplets dispersed in a non-polar medium, provides several benefits for their use as media for enzymatic transformations. They have the ability to overcome the solubility limitations of hydrophobic substrates, enhance the enzymatic activity (superactivity phenomenon) and stability, while providing an interface for surface-active enzymes. Of particular interest is the use of such systems to study biotransformations catalyzed by oxidative enzymes. Nanodispersed biocatalytic media are perfect hosts for liquid oxidation reactions catalyzed by many enzymes such as heme peroxidases, phenoloxidases, cholesterol oxidase, and dehydrogenases. The system's composition and structural properties are important for better understanding of nanodispersion-biocatalyst interactions.

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“…While lipases, for example, show good stabilities in several organic reaction media (Stamatis et al, 1999), alcohol dehydrogenases are less stable, having half-life times in microemulsions of only hours (Chen et al, 1995;Lee and Biellmann, 1987;Orlich and Schomäcker, 1999a) or even minutes (Samama et al, 1987). The stability depends on the microemulsion parameters and additionally on the reaction components and salts, mainly the water and the surfactant concentration.…”

Section: Introduction Generalmentioning

confidence: 99%

Stability and activity of alcohol dehydrogenases in W/O‐microemulsions: Enantioselective reduction including cofactor regeneration

Orlich

Berger

Lade

et al. 2000

Biotech & Bioengineering

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Microemulsions provide an interesting alternative to classical methods for the conversion of less water‐soluble substrates by alcohol dehydrogenase, but until now stability and activity were too low for economically useful processes. The activity and stability of the enzymes are dependent on the microemulsion composition, mostly the water and the surfactant concentration. Therefore, it is necessary to know the exact phase behavior of a given microemulsion reaction system and the corresponding enzyme behavior therein. Because of their economic and ecologic suitability polyethoxylated fatty alcohols were investigated concerning their phase behavior and their compatibility with enzymes in ternary mixtures. The phase behavior of Marlipal O13‐60 (C13EO6 in industrial quality)/cyclohexane/water and its effect on the activity and stability of alcohol dehydrogenase from Yeast (YADH) and horse liver (HLADH) and the carbonyl reductase from Candida Parapsilosis (CPCR) is presented in this study. Beside the macroscopic phase behavior of the reaction system, the viscosity of the system indicates structural changes of aggregates in the microemulsion. The changes of the enzyme activities with the composition are discussed on the basis of transitions from reverse micelles to swollen reverse micelles and finally, the transition to the phase separation. The formate dehydrogenase from Candida boidinii was used for the NADH‐regeneration during reduction reactions. While the formate dehydrogenase did not show any kinetic effect on the microemulsion composition, the other enzymes show significant changes of activity and stability varying the water or surfactant concentration of the microemulsion. Under certain conditions, stability could be maintained with HLADH for several weeks. Successful experiments with semi‐batch processes including cofactor regeneration and product separation were performed. © 2000 John Wiley & Sons, Inc. Biotechnol Bioeng 70: 638–646, 2000.

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Enzyme and organic solvents: Horse liver alcohol dehydrogenase in non‐ionic microemulsion: Stability and activity

Cited by 26 publications

References 12 publications

Kinetic properties of polyphenoloxidase in organic solvents A study in Brij 96‐cyclohexane reverse micelles

Kinetic properties of polyphenoloxidase in organic solvents A study in Brij 96‐cyclohexane reverse micelles

Oxidation Catalysis by Enzymes in Microemulsions

Stability and activity of alcohol dehydrogenases in W/O‐microemulsions: Enantioselective reduction including cofactor regeneration

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