Higher order structure of Mucor miehei lipase and micelle size in cetyltrimethylammonium bromide reverse micellar system.

The higher order structure of Mucor miehei lipase and micelle size in a cationic cetyltrimethylammonium bromide (CTAB) reverse micellar system was investigated. Circular dichroic (CD) measurement revealed that the lipase far-UV CD spectra changed markedly, going from buffer solution to the reverse micellar solution, and were very similar for any organic solvent used. The ellipticity of the solubilized lipase in the far-UV region markedly decreased with increasing water content (W(0): molar ratio of water to CTAB), indicating that the secondary structure of lipase changed with the water content.

Liquid-liquid extraction of alpha-lactalbumin using reverse micellar organic solvent.

The liquid-liquid extraction of alpha-lactalbumin based on reverse micellar organic solvents was investigated. Forward extraction of the protein in the reverse micellar organic phase from aqueous feed solutions was strongly dependent on the initial pH of the feed solution and the complete forward extraction of 0.03 mM alpha-lactalbumin was successfully achieved at pH 6.

Higher order structure of proteins solubilized in AOT reverse micelles.

The higher order structure of proteins solubilized in an bis(2-ethylhexyl) sulfosuccinate sodium (AOT) reverse micellar system was investigated. From circular dichroic (CD) measurement, CD spectra of cytochrome c, which is solubilized at the interface of reverse micelles, markedly changed on going from buffer solution to the reverse micellar solution, and the ellipticity values in the far- and near-UV regions decreased with decreasing the water content (W0: molar ratio of water to AOT), indicating that the secondary and tertiary structures of cytochrome c changed with the water content. The ellipticity of ribonuclease A, which is solubilized in the center of micellar water pool, in the near-UV region was dependent on W0 and became minimum when W0 of ca.