• 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.

• Journal of the Korean Ceramic Society
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• v.35 no.6
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• pp.594-602
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• 1998

Titanium hydroxide (TiO({{{{ {OH }_{2 } }})) fine particles were produced by the reverse micelle technique. For the formation of titanium hydroxide (TiO({{{{ {OH }_{2 } }})) particles with the technique reversed micellar solution was prepared by solubilizing water into organic solvent (isooctane) with a surfactant and titanium alkoxide (tetraisopropyl orthotitanate) diluted with isopropyl alcohol was added to the reversed micellar solution. The hdrolyzed species (TiO({{{{ {OH }_{2 } }})) was formed by the hydrolysis of titanium alkoxide and titanium dioxide is then formed by the condensation of the hydrolyzed species. There are several process variables such as surfactants concentration of surface cosurfactant hydrolysis temperature and pH. In this work the ef-fects of process variables on paticle shapes particle size distribution and paticle agglomeration were bi-nodal for an anionic surfactant(AOT) in the whole range of temperature pH and surfactant concentration of this experiment. The addition of ethanol as a cosurfactant resulted in narrow particle size distribution of the experiment. The additiono of ethanol as a cosurfactant resulted in narrow particle size distribution and 0.12${\mu}{\textrm}{m}$ of smaller average particle diameter. FT-IR spectrum of particles shows the absorption peak of Ti-OH bonding and Ti-O bonding. An exothermic peak around 41$0^{\circ}C$ in TGA-DTA curve shows that crys- tallized anatase phase appears and completely transits to anatase around 45$0^{\circ}C$.

• 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.

• Journal of Microbiology and Biotechnology
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• v.24 no.12
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• pp.1690-1698
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• 2014

Partial purification of glucoamylase from solid-state fermentation culture was, firstly, investigated by reverse micellar extraction (RME). To avoid back extraction problems, the glucoamylase was kept in the original aqueous phase, while the other undesired proteins/enzymes were moved to the reverse micellar organic phase. The individual and interaction effects of main factors (i.e., pH and NaCl concentration in the aqueous phase, and concentration of sodium bis-2-ethyl-hexyl-sulfosuccinate (AOT) in the organic phase) were studied using response surface methodology. The optimum conditions for the maximum recovery of the enzyme were pH 2.75, 100 mM NaCl, and 200 mM AOT. Furthermore, the optimum organic to aqueous volume ratio ($V_{org}/V_{aq}$) and appropriate number of sequential extraction stages were 2 and 3, respectively. Finally, 60% of the undesired enzymes including proteases and xylanases were removed from the aqueous phase, while 140% of glucoamylase activity was recovered in the aqueous phase and the purification factor of glucoamylase was found to be 3.0-fold.

• Bulletin of the Korean Chemical Society
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• v.33 no.10
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• pp.3493-3496
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• 2012

• Proceedings of the Korean Powder Metallurgy Institute Conference
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• 2006.04a
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• pp.50-50
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• 2006

• Bulletin of the Korean Chemical Society
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• v.27 no.3
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• pp.377-380
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• 2006

The semiconductor PbS nanobelts (width 50-120 nm and length over 3 $\mu$m) were self-assembled in a simple reverse micelle solvent system containig the surfactant of polyoxyethylene (9) dodecy ether $(C_{12}E_9)$. The nanobelts synthesized were found to possess cube galena poly-crystal structure with high purity when analyzed by ED and X-ray diffraction. Significant “blue shift” from bulk material was observed on the PbS nanobelts using photoluminescence and UV-Vis spectroscopy. A mechanism involving the possible formation of nanobelts based on surfactant template was also proposed.

• KSBB Journal
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• v.6 no.1
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• pp.105-109
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• 1991

In separating alkaline protease from the bacteria (Bacillus licheniformis) fermentation broth using reverse micelle, effects of various factors;ionic strength, pH and surfactant concentration, on separation efficiency were studied. KCl controls the ionic strength. The lower KCl concentration was in the feed solution, the more protein and activity was recovered. The higher KCl concentration was in the stripping solution, the more protein and activity was recovered. Using sodium-di-2-ethylhexyl sulfosuccinate(Aerosol-OT or AOT) as a surfactant, the higher AOT concentration in the solvent, the more activity and protein were recovered. 0.1N NaOH and IN HCl were used to adjust pH. Maximum recovery of protein mass and activity were obtained at feed solution of pH 5.3. Maximum activity was recovered at stripping solution of pH 7.5

• Food Science of Animal Resources
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• v.24 no.1
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• pp.80-85
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• 2004

This study was carried out to separate immunoglobulin G(IgG) from colostrum using reverse micellar extraction of cationic surfactant and to suggest suitable extraction conditions. The reconstituted colostrum powder was solubilized into a reverse micellar phase containing CDAB(cetyldimethylethyl ammonium bromide) by mixing equal volume of the aqueous and organic phase with constant stirring. The solubilization of proteins from the aqueous to the organic phase was manipulated by pH and ionic strength of the aqueous phase and concentration of surfactant in the organic phase. Based on the SDS-PAGE and densitometry, about more than 90% of initial IgG was remained in the aqueous phase after reverse micellar extraction. Although the aqueous phase contained lactoferrin and bovine serum albumin as minor components, about 93% of the total protein was IgG. The efficient extraction was achieved by the reaction of sodium phosphate buffer(pH 8) containing 50 mM KCl and organic phase containing 100 mM CDAB. The separation of IgG using reverse micellar extraction was simple, highly efficient and easy to be scaled up.

• Journal of the Korean Chemical Society
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• v.20 no.3
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• pp.193-197
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• 1976

The ultrasonic absorption has been measured in aqueous solution of dodecyl pyridinium chloride (DPC) at $20^{\circ}C$ over the frequency range of 0.1${\sim}$90 Mc.The excess absorption was observed only in solutions in which the concentration was higher than the critical micellar concentration(cmc). The mechanism for this feature was attributed to the reaction $M_2\;{\rightleftharpoons}\;M_1\;＋\;1.2Cl^-$ Where $M_2$ and $M_1$ and M1 are two types of micelle. The rate constants of the forward and the reverse reactions were $6.6{\times}10^5 sec^{-1}\;and\;2.7{\times}10^11sec^{-1}mol^{-1.2}$respectively. Some kinetic charateristics including the free energy, enthalpy and entropy were calculated.