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Levashov, A. V.; Klyachko, N. L.

doi:10.1023/a:1014361508512

Cited by 12 publications

(9 citation statements)

References 105 publications

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“…Such aggregates capable of solubilization substantial amounts of polar compounds including water molecules, which become localized in the internal cavity of micelles [1]. Heightened interest for hydrated reversed micelles is due to the application of such systems (surfactant/water/organic solvent) as the environment for the realization of fermentative reactions.…”

Section: Introductionmentioning

confidence: 99%

“…Heightened interest for hydrated reversed micelles is due to the application of such systems (surfactant/water/organic solvent) as the environment for the realization of fermentative reactions. Unique properties of water pools of reversed micelles such as high polarity, high microviscosity, high concentration of the functional groups -give the reason to consider the internal cavity of micelles as a very realistic model of a microenvironment of active center of ferments [1,2].…”

Section: Introductionmentioning

confidence: 99%

“…The influence of ω on size and shape of micelles was detected. Dependencies of lifetime (1), difference of lifetime values in bulk and micellar water (2), and absorption cross-section (3) of R6G in reversed micelles on the hydratation power…”

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confidence: 99%

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Fluorescence saturation of dye molecules in water pools of reversed micelles

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Saletsky²

2005

Laser Phys. Lett.

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Rhodamine 6G has been used as a fluorescence probe in AOT reversed micelles systems with the different amounts of solubilized water (hydratation power ω). The saturation of fluorescence and the lifetime of dye molecules were measured. The absorption cross section values were calculated from the saturation curves. We showed the differences in values of the absorption cross section, lifetime and velocity of fluorescence saturation in micellar phase with different ω and in comparison to bulk phase. Additionally, the structure of hydrated reversed micelles has been studied by the method of correlation spectroscopy. The influence of ω on size and shape of micelles was detected.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Fluorescence saturation of dye molecules in water pools of reversed micelles

Потапов

Saletsky²

2005

Laser Phys. Lett.

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“…2 One of such systems is the system of reversed micelles, the advantages of which for the catalysis by various enzymes have already been demonstrated many times [1][2][3]. It was shown that enzymes not only preserve their activities in this system, but also, in some cases, exhibit higher activities and stabilities in comparison with their solutions in water or in pure organic media.…”

Section: Introductionmentioning

confidence: 99%

Effect of Chemical Modification of Lipase on the Regulation of Its Lipolytic Activity in Reversed Micelles

2005

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Hydrophilized and hydrophobized forms of the lipase from Mucor miehei were obtained by its chemical modification with cellobiose and N-hydroxysuccinimidyl palmitate with a modification degree of 4 in both cases. A comparative analysis of the regulation of the catalytic activities of the native and modified lipases was carried out in the system of reversed micelles of OT aerosol (AOT) in isooctane. The level of catalytic activity of all the lipase preparations in the micellar medium was found to be higher than that in aqueous solution. The chemical modification of lipase did not result in a change in the regulation of the oligomeric composition of the enzyme controlled by the degree of micelle hydration omega0 (micelle size). The kcat dependences on omega0 for each lipase preparation exhibit two maxima, corresponding to the functioning of lipase monomers and tetramers. The changes in the hydrophilic-lipophilic balance of the lipase surface significantly affect the character of the regulation of enzyme activity due to changes in the surfactant concentration (the number of micelles). The lipase hydrophobization results in a decrease in the enzyme activation effect with an increase in the AOT concentration in comparison with the native lipase. The lipase hydrophilization dramatically decreases the activity of lipase tetramer when the AOT concentration is increased. The catalytic activity of the monomer of hydrophilized lipase is practically independent of the AOT concentration. Kinetic data indicate a mixed type of activation of both oligomeric forms of the native and the hydrophobized lipase by AOT molecules and the noncompetitive type of the activation and AOT inhibition of the monomer and the tetramer of the hydrophilized lipase, respectively. The English version of the paper: Russian Journal of Bioorganic Chemistry, 2005, vol. 31, no. 6; see also http://www.maik.ru.

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“…Such systems are not only a convenient model for intracellular protein immobilization and functioning, but also have numerous applications in chemical and biochemical reactions which are disadvantageous in aqueous medium. To understand the molecular reasons for the extraordinary functional activity of enzymes in the reverse micelles, the influence of the microemulsion reaction medium on their structural and catalytic stability is examined from va¡ ous points of view [8,9]. However, it should be kept in mind that a catalytic system "enzyme-reverse micelle" is ah indivisible one and as the micelle affects the protein properties, so there has to be an opposite action.…”

Section: Introductionmentioning

confidence: 99%

Effects of protein solubilization on the structure of the surfactant shell of reverse micelles

2003

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The influence of protein encapsulation in the water pool of the reverse mice|les has been studied by the electron spin resonance (ESR) spin-label technique and electrical conductivity measurements. For this purpose water-sodium-bis(2-ethylhexyl)-sulfosuccinate (AOT)-decane water-in-oil microemulsions with so|ubilized trypsin were used. The ESR data, obtained with the help of 4-(2-n-undecyl-3-oxyl-4,4-dimethyloxazolidin-2-yl) butyric acid as a label, show that the protein molecule encapsulated in the water core of a reverse micelle forces a portion of water out from the aqueous core into the hydrophobic shell of a micelle. As a result, changes in the packing of AOT hydrocarbon chains and in the polarity of their microenvironment are induced. The effect of the encapsulated protein depends on -the difference in the sizes of the protein molecule and the micelle aqueous core. The perturbations in the dynamic structure of the surfactant shell tum out to be most pronounced when the dimensions of the water cavity ate close to the size of the protein molecule. The solubilization of protein in the reverse mice|les results in remarkable va¡ in mass exchange between micelles.

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Cited by 12 publications

References 105 publications

Fluorescence saturation of dye molecules in water pools of reversed micelles

Fluorescence saturation of dye molecules in water pools of reversed micelles

Effect of Chemical Modification of Lipase on the Regulation of Its Lipolytic Activity in Reversed Micelles

Effects of protein solubilization on the structure of the surfactant shell of reverse micelles

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