• Journal of Microbiology and Biotechnology
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• v.1 no.3
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• pp.197-201
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• 1991

Glycerolysis of triolein by lipase from Chromobacterium viscosum lipase was studied batchwise in AOT-isooctane reversed micelles. The reaction mixture was extracted with chloroform and the content of triolein, 1, 2-diolein, 1, 3-diolein, 1-monoolein, and free fatty acid in the condensed chloroform solution was determined using high performance liquid chromatography (HPLC). The effect of agitation speed on the initial rate of conversion was examined. As the speed of agitation increased up to 700 rpm, the reaction rate increased. However, above 700 rpm, the rate approached maximum and did not increase that much. The glycerolysis activity and the stability of the enzyme were affected by stirring and addition of histidine or copper. Addition of histidine and copper increased the rates of glycerolysis but they are detrimental to the operational stability in reversed micelles.

• KSBB Journal
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• v.5 no.4
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• pp.411-414
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• 1990

The extraction behavior of an alkaline protease using reversed micelles was investgated. The reversed micellar solution consisted of AOT in isooctane. It was found that distribution of arkaline protease into the organic phase increased at lower pH, lower ionic strength, and higher AOT concentration. When the real fermentation broth was extracted of alkaline protease, an activity yield of 20% and a purification factor of 2.0 were obtained.

• Proceedings of the Membrane Society of Korea Conference
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• 2004.05a
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• pp.7-10
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• 2004

Reversed micelles (RMs) are nanometer-scale molecular assemblies in organic media. Their surface films (membranes) are composed of surfactant molecules normally holding two hydrocarbon hydrophobic chains. Di-2-ethylhexyl sulfosuccinate (AOT), which is a negatively charged molecule, is most popular surfactant utilized to form reversed micelles.(omitted)

• Korean Journal of Food Science and Technology
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• v.29 no.1
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• pp.26-31
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• 1997

Bee venom (Apis mellifera) phospholipase $A_2$ solubilized in reversed micelles containing small amount of water stabilized by surfactant could catalyze the hydrolysis of dipalmitoyl phosphatidylcholine (DPPC). A sensitive and simple high performance liquid chromatographic (HPLC) methodology of phospholipase $A_2$ assay for the hydrolysis of DPPC was developed. Kinetic analysis of the phospholipase $A_2$-catalyzed reaction was found to be possible in reversed micelles. Among the surfactants and organic solvents tested, aerosol-OT and isooctane were most effective for the hydrolysis of DPPC in reversed micelles. Optimal temperature, optimal pH, $K_{m,app.},\;V_{max.,app.}$ and activation energy were determined to be $35{\sim}40^{\circ}C$, 7.0, 8.73 mM, 2.83 units/㎎ protein and 12.31 kcal/mole, respectively. The hydrolysis activity was dependent on water content and maximum activity was obtained at R value (=[water]/[aerosol-OT]) of 10.0.

• KSBB Journal
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• v.18 no.3
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• pp.202-206
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• 2003

A study of hen egg lysozyme extraction using reversed micelles and pressurized CO₂ phase was conducted. The relationship between the lysozyme extraction and water content (W/sub 0/) under the pressurized CO₂ conditions was investigated. The water content of the micellar organic phase was a significant parameter affecting the mass transfer of protein and enzymatic activity in reversed micellar process. It was found that the reversed micelles in the organic phase with pressurized CO₂ were larger than the organic phase without CO₂. Therefore, the extractionrate of lysozyme in the interface of the aqueous phase and the organic phase was increased. W/sub 0/ value was increased at the high surfactant concentration and the extraction rate of lysozyme was enhanced.

• KSBB Journal
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• v.14 no.6
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• pp.661-664
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• 1999

Proteins were extracted from an aqueous phase with reversed micelles. The effect of pH, and salt concentration on the solubilization of lysozyme in AOT/isooctane solution was studied to explore the potential for employing this solvent system in the large-scale recovery and concentration of proteins using liquid extraction. For pH values below the isoelectric point, pl of the protein, solubilization was high, probably owing to strong electrostatic interactions between the positively charged proteins and the anionic surfactant heads forming the inner micelle wall. At low ionic strength complete solubilization of the protein was observed. A pH higher than the pl of lysozyme and a salt concentration lower than that of the water pool were required for the recovery aqueous phase to ensure the back extraction of lysozyme from the AOT reversed micelles.

• KSBB Journal
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• v.16 no.3
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• pp.241-245
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• 2001

Mass transfer rates have been measured for the extraction of enzyme from aqueous solution into a reverse-micelle phase at $25^{\circ}C$. The 420 mL vessel was carefully designed to maintain a planar interface between the aqueous and solvent phases, so allowing precise measurement of interfacial area, has been investigated. Sodium di-2-ethylhexyl sulfosuccinate(AOT) was the surfactant used. Factors varied included: agitator speed, pH, ionic strength and surfactant concentration. Samples were taken from the solvent phase at 15min intervals, and the amount of enzyme extracted was measured by UV absorption at 280 nm. The observed Sherwood numbers for the aqueous phase $Sh_1$were correlated interms of the aqueous phase Reynolds number $Re_1$, and modified Schmidt number $Sc_1$. $Sh_1=0.664Re_1^{0.5}Sc_1^{0.33}$

• Journal of the Society of Cosmetic Scientists of Korea
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• v.39 no.4
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• pp.271-279
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• 2013

Water-soluble collagen (30 wt%) was entrapped within oil phase of lipstick using reversed micelle method to improve the moisture capacity of the lipstick. Reversed micelles containing collagen were prepared using caprylic/capric triglyceride as external phase and polyoxyethylene (10) octylphenyl ether (Triton X-100) and 1-dodecanol as surfactant and co-surfactant, respectively. The formation of reversed micelle encapsulating collagen was confirmed by measuring electric conductivity and UV-vis spectrum using methylene blue (MB). The stability and moisture capacity of the lipstick containing 20 wt% collagen encapsulated reversed micelles were observed by measuring rheology property, moisture content and amino acid content. The molecular ratio (W, water-pool) of water to surfactant (Triton X-100) in the most stable reversed micelle was ${\leq}$ 10. The hardness of the lipstick had no difference with that of the lipstick without reversed micelle, and the moisture content was increased to 59% and the amino acid content was 92.7%.

• Korean Journal of Food Science and Technology
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• v.34 no.2
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• pp.157-163
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• 2002

An investigation was carried out to study the characteristics of lipoxygenase in dioctyl sulfosuccinate (aerosol-OT, AOT)/isooctane revered micelles of microaqueous system containing infinitesimal water. ${\alpha}-Linoleic$ acid as a substrate could be analyzed by the colorimetric methodology using 5%(w/v) cupric acetate-pyridine solution and the activity of lipoxygenase was able to be assayed by the degree of ${\alpha}-linoleic$ acid consumption per minute. Optimal pH, temperature, and R-value ([water]/[AOT]) were determined as the value of 5.0, $25^{\circ}C$, and 10.0, respectively. Kinetic analysis of the enzyme reaction under the optimal conditions showed that the values of $K_m$ and $V_{max}$ were 0.31 mM of ${\alpha}-linoleic$ acid and $384.16{\mu}mol$ of ${\alpha}-linoleic$ acid decomposed/min, respectively. The results indicate the reaction to be lipoxygenase-catalyzed oxidation of ${\alpha}-linoleic$ acid in AOT/isooctane reversed micellar system. The inhibitory effect of natural antioxidants on lipoxygenase showed little inhibitory effect of L-ascrobic acid while ${\alpha}-tocopherol$ showed 72% of inhibitory effect.

• KSBB Journal
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• v.6 no.4
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• pp.337-344
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• 1991

The liquid-liquid extraction of lipase A from Candide cylindracea and lipase B from porcine pancrease was carried out using reversed micellar organic solvents. Effects of various factors such as ionic strength, pH, and species and concentration of surfactant, on lipase solubilization were studied. A cationic surfactant cetyl-trimethyl ammonium bromide (CTAB) in isooctane/nhexanol(1:1) was found to be an effective solvent and its optimum concentration was 50 mM. KCl among various salts tested was the most effective and the efficiency of solubilization of lipase increased with decreasing the ionic strength of salts. The maximum activity and solubiliz ation of protein were obtained at pH 8. The stripping efficiency has a maximum value at pH 4 and increases with KCl concentration in the range of 0.2∼1.0 M. After the solubilization and stripping, the overall recovery efficiency of mass and specific activity of lipases was 62% and 66%, respectively.