Properties and Applications of Reversed Micelles

Kon-No, Kijiro

doi:10.1007/978-1-4615-3002-2_3

Cited by 12 publications

(8 citation statements)

References 51 publications

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“…Reverse micellar systems have attracted the attention of research workers from various fields of science and technology owing to their unique ability to solubilize water in organic solvents in the presence of surfactants [1][2][3][4][5][6][7][8][9][10][11][12][13][14]. ture and valence of the counterion, the temperature, etc.…”

Section: Introductionmentioning

confidence: 99%

Water solubilization capacity of mixed reverse micelles: Effect of surfactant component, the nature of the oil, and electrolyte concentration

Paul¹,

Mitra²

2005

Journal of Colloid and Interface Science

103

105

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Section: Introductionmentioning

confidence: 99%

Water solubilization capacity of mixed reverse micelles: Effect of surfactant component, the nature of the oil, and electrolyte concentration

Paul¹,

Mitra²

2005

Journal of Colloid and Interface Science

103

105

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“…odium bis(2-ethylhexyl)sulfosuccinate (NaAOT) is an ionic surfactant widely used in chemical and biophysical work for solubilization, separation, catalysis, drug delivery, nanoparticle synthesis, and generating membrane-mimetic systems [1][2][3]. It has two branched alkyl chains as shown in Figure 1, and is soluble in various solvents with the ability to assemble into direct or reverse micelles.…”

mentioning

confidence: 99%

Mass Spectrometry Study of Multiply Negatively Charged, Gas-Phase NaAOT Micelles: How Does Charge State Affect Micellar Structure and Encapsulation?

Fang

Liu

2012

J. Am. Soc. Mass Spectrom.

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Abstract. We report the formation and characterization of multiply negatively charged sodium bis(2-ethylhexyl) sulfosuccinate (NaAOT) aggregates in the gas phase, by electrospray ionization of methanol/water solution of NaAOT followed by detection using a guided-ion-beam tandem mass spectrometer. Singly and doubly charged aggregates dominate the mass spectra with the compositions of [Na n-z AOT n ] z-(n01-18 and z01-2). Solvation by water was detected only for small aggregates [Na n-1 AOT n H 2 O] -of n03-9. Incorporation of glycine and tryptophan into [Na n-z AOT n ] z-aggregates was achieved, aimed at identifying effects of guest molecule hydrophobicity on micellar solubilization. Only one glycine molecule could be incorporated into each [Na n-z AOT n ] z-of n≥7, and at most two glycine molecules could be hosted in that of n≥13. In contrast to glycine, up to four tryptophan molecules could be accommodated within single aggregates of n≥6. However, deprotonation of tryptophan significantly decrease its affinity towards aggregates. Collision-induced dissociation (CID) was carried out for mass-selected aggregate ions, including measurements of product ion mass spectra for both empty and amino acid-containing aggregates. CID results provide a probe for aggregate structures, surfactant-solute interactions, and incorporation sites of amino acids. The present data was compared with mass spectrometry results of positively charged [Na n+z AOT n ] z+ aggregates. Contrary to their positive analogues, which form reverse micelles, negatively charged aggregates may adopt a direct micelle-like structure with AOT polar heads exposed and amino acids being adsorbed near the micellar outer surface.

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“…At low Wo values, injected water may be used mainly for the hydration of the surfactant molecule. 17,18 As a result, the quantity of free water that is necessary for the enzyme's catalytic reaction in the water-pool may be insufficient. At high water contents, on the other hand, surplus water would be present as free water and provide a suitable environment for the enzyme reaction.…”

Section: Methodsmentioning

confidence: 98%

Enzyme processing of wool fabrics in a non‐ionic surfactant reverse micellar system

Sawada

Ueda

2004

J of Chemical Tech & Biotech

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Modification of wool fabrics with an enzyme in a reverse micellar system has been investigated using polyoxyethylene sorbitan trioleate as a surfactant. The protease, Bioprase 30L, used in this study was satisfactorily solubilized in the reverse micellar system and maintained its activity even in an organic media. Modification of wool fabrics with Bioprase 30L was evaluated by the fabric's weight loss, measurement of tear strength, scanning electron microscopy, and measurement of shrinkage. Effective modification of wool fabrics with enzymatic hydrolysis can be attained without causing serious loss of fiber strength.

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Properties and Applications of Reversed Micelles

Cited by 12 publications

References 51 publications

Water solubilization capacity of mixed reverse micelles: Effect of surfactant component, the nature of the oil, and electrolyte concentration

Water solubilization capacity of mixed reverse micelles: Effect of surfactant component, the nature of the oil, and electrolyte concentration

Mass Spectrometry Study of Multiply Negatively Charged, Gas-Phase NaAOT Micelles: How Does Charge State Affect Micellar Structure and Encapsulation?

Enzyme processing of wool fabrics in a non‐ionic surfactant reverse micellar system

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