• Journal of Pharmaceutical Investigation
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• v.35 no.5
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• pp.333-336
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• 2005

The objective of this study was to investigate the stability of tetracycline HCl on encapsulation into and inside reverse micelles. To do so, tetracycline HCl was first mixed with cetyltrimethylammonium bromide, water and ethyl formate to make reverse micelles. The degradation kinetics of tetracycline HCl inside the reverse micelles was then assessed by scrutinizing its stability data. Under our experimental conditions, the reverse micelles formed spontaneously in absence of any mixing devices. During the preparation of the reverse micelles, however, considerable portions of tetracycline HCl underwent a chemical reaction (e.g., epimerization). For instance, $51.4{\pm}0.6%$ of an initial concentration of tetracycline HCl was transformed into a degradation product. Once dissolved inside the reverse micelles, the degradation of tetracycline HCl followed an exponential decay pattern. The plot of log{the degradation rate of tetracycline HCl} versus log{tetracycline HCl concentration} made it possible to determine the order of degradation reaction and rate constant. It was proven that the degradation of tetracycline HCl inside the reverse micelles followed a first order kinetics with a rate constant of 0.0027 $hour^{-1}$. Meriting further investigation might be formulation studies to stabilize tetracycline HCl on encapsulation into and inside the reverse micelles.

• Bulletin of the Korean Chemical Society
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• v.27 no.2
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• pp.251-254
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• 2006

The formation of polyaniline (PANI) in the reverse micelles of poly(oxyethylene) nonylphenyl ether, $(NP5, H(CH_2)_9Ph(OC_2H_4)_5OH)$, was investigated by small-angle neutron scattering (SANS). The reverse micellar solution containing initiators in the inner part of reverse micelle was prepared with surfactant (NP5), water, cyclohexane and an initiator (ammonium persulfate (APS)). The core-shell sphere model containing smearing effect reveals that the polymerization occurs on the shell layer of the reverse micelles. Shell thickness averages varied from 48 $\AA$ to 109 $\AA$ with increases of monomer concentration.

• Applied Chemistry for Engineering
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• v.35 no.5
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• pp.399-403
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• 2024

Lecithin is one type of surfactant with amphiphilic properties, which forms spherical reverse micelles in various organic solvents. Salts with markedly low solubility in organic solvents can significantly increase their solubility through ionic interactions through the hydrophilic head of lecithin, leading to changes in the molecular morphology of lecithin. As a result, spherical reverse micelles can transform into cylindrical reverse micelles, which can cause abrupt rheological changes when these cylindrical reverse micelles form a transient network. This study precisely analyzes the formation of self-assembled structures and rheological changes by simultaneously adding two types of salts to a lecithin solution, using small-angle X-ray scattering analysis and rheometry.

• KSBB Journal
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• v.7 no.1
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• pp.51-58
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• 1992

The use of watersoluble enzymes for chemical synthesis suffers from several limitations. The solubilization of biocatalyst (Enzymes and Cells) with reverse micelles or microemulsion could be a method for bioconveision of low water soluble substrates. In this review, We will discuss the properties and the potentials of reverse micelle for catalytic bioconversion and biotechnology.

• Journal of Photoscience
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• v.4 no.2
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• pp.53-59
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• 1997

Absorption and fluorescence studies of E-1-(p-methoxyphenyl)-2-(p-nitrophenyl) ethene in homogeneous solvents, polymer matrix and normal and reverse micelles showing strong solvatochromic fluorescent emission properties with quasi-planar intramolecular charge transfer characteristics in the electronically excited singlet state are discussed.

• Korean Journal of Food Science and Technology
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• v.32 no.3
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• pp.736-741
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• 2000

The abilities of petroleum ether-extracts prepared from 75 plants to inhibit tyrosinase activity were evaluated in reverse micelles composed of isooctane/AOT(100 mM)/phosphate buffer(20 mM, pH 8.0) containing tyrosinase(105.3 units/mL) and 3,4-dihydroxyphenylalanine(0.18 mM). Compared with control which has no plant extracts, garlic could completely inhibit in vitro melanogenesis by tyrosinase, and Chinese quince, sweet potato, onion, radish bud and apple did more than 60%. Lipophilic extracts of medicinal plants and herbs such as rosemary, coriander, cinnamomi ramulus, crataegii fructus, ramulus biotae folium, mume fructus, menthae herba, eucommiae cortex and clove also inhibited tyrosinase activity more than 60%. When the extraction yield of lipophilic materials was considered together with their inhibition effect on tyrosinase, it was possible to select plants of which tyrosinase inhibitors could be produced in high quantity from unit weight. Using reverse micelles, the analysis of the capacity of lipophilic materials to inhibit tyrosinase activity which was difficult up to present could be possible.

• Macromolecular Research
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• v.16 no.1
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• pp.62-65
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• 2008

The morphology of the $D_2O$-induced reverse micellar structure of an amphiphilic block copolymer of poly( ethylene oxide )-b-poly(propylene oxide )-b-poly( ethylene oxide )($EO_{76}PO_{29}EO_{76}$) was investigated in hydrophobic media by small angle neutron scattering (SANS). Increasing $D_2O$ in the styrene/divinylbenzene solution of $EO_{76}PO_{29}EO_{76}$ led to a change in morphology of the reverse micelles from a short range ordered molecular aggregate to a hexagonally arranged micelle, and further to a spherical micelle.

• Applied Chemistry for Engineering
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• v.32 no.6
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• pp.679-683
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• 2021

Lecithin, a zwitterionic phospholipid, forms spherical reverse micelles in nonpolar organic solvents such as decane. The addition of monovalent ions like lithium chloride (LiCl) to lecithin organosols induces the transformation of organosols into organogels due to the entanglement of reverse cylindrical micelles. In this study, we investigate the effect of pentanol acting as co-surfactant on rheological properties of lecithin/LiCl mixtures. From rheological studies, we find that the viscosity and elastic property of organogels decreased upon the addition of pentanol to organogels. The decrease in viscosity and elastic property can be attributed to the shortening of reverse cylindrical micelles confirmed by small angle X-ray scattering (SAXS).

• Food Science and Biotechnology
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• v.14 no.1
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• pp.131-136
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• 2005

The selective extraction behavior of lactoferrin (Lf) from whey protein mixture was examined using reverse micelles formed by the cationic surfactant, cetyldimethylammonium bromide (CDAB). The major whey proteins, including ${\beta}$-lactoglobulin, ${\alpha}$-lactalbumin and bovine serum albumin, were solubilized from aqueous phase to organic phase while Lf was recovered in the aqueous phase. The solubilization behaviors of the proteins were manipulated by the process parameters such as the pH and salt concentration of the aqueous phase and the surfactant concentration in the organic phase. Efficient forward extraction was achieved with sodium borate buffer (50 mM, pH 9) containing 50 mM KCl and organic phase containing 100 mM CDAB. Based on SDS-PAGE and densitometry, about 96% of the initial Lf remained in the aqueous phase after forward extraction. The dialyzed Lf fully maintained its bacteriostatic activity against E. coli O157:H7.

• Microbiology and Biotechnology Letters
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• v.18 no.5
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• pp.517-524
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• 1990

The solubilization and desolubilization of proteins in CTAB/hexanol/isooctane reverse micellar system were investigated for the selective separation of proteins. Several proteins were used, including bovine serum albumin (BSA), pepsin, trysin and ribonuclease-a. Most proteins could be solubilized into reverse micelles in the pH range above the isoelectric point of each protein, where the net charge of protein was opposite to that of surfactant. However BSA was solubilized above pH 10, which is serveral pH units above the pI 4.9. The kinds of anions in aqueous phase influenced on protein solubilization while no significant trend was observed with different cations, Protein solubilization decreased with increase of the ion size in the order of F -, C1-, Br- and I -. The size of CTAB micelles did not change significantly with increasing ionic strength, but the solubilization decreased. Protein desolubilization showedropposite behaviors to the solubilization. Several model mixtures such as pepsin/ trypsin, pepsin/ribonuclease-a and BSAlribonucleaee-a were successfully separated from each other without changing enzymatic activities.