• Bulletin of the Korean Chemical Society
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• v.25 no.6
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• pp.873-877
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• 2004

The relationship between the behaviors of c.c.lipase back-extraction and their percolation phenomena by using AOT reverse micellar systems (RVMS) has been studied by the addition of a small amount of additives to organic phase such as thiols and nonionic-surfactants focusing on micelle-micelle interactions. The values of ${\beta}_t$ defined by the variation of percolation processes and back-extraction behaviors of c.c.lipase have a good linear correlation. The hydrophobicity of additive molecules suppressing the cluster formation of reverse micelles (high values of ${\beta}_t$) improved the back-extraction behavior of c.c.lipase. The back-extraction fraction and its rate of c.c.clipase are increased with decreasing of the value of hydrophilic lipophilic balance (HLB) and increasing of the hydrophobicity per additive molecules added to reverse micellar systems (RVSM) in the same additives concentration.

• Bulletin of the Korean Chemical Society
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• v.22 no.8
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• pp.897-902
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• 2001

The protein back-extraction processes were discussed from the viewpoint of the micelle-micelle interaction. Bovine serum albumin (BSA) suppressing the cluster formation of reverse micelle (positive value of ${\beta}pr)$ has the high back-extra cted fraction (Eb), but cytochrome c enhancing the formation of reverse micelle (negative value of ${\beta}pr)$ has the low back-extracted fraction, relatively. We have also examined quantitatively the effects of alcohol addition and protein solubilization on the percolation process of reverse micelle. The alcohols suppressing the formation of micellar cluster (high values of ${\beta}t)$, remarkably improved the back-extraction rates of BSA and cytochrome c. The values of ${\beta}t$, defined by the variation of percolation process, and the back-extraction behavior of proteins have a good linear correlation. These results indicate that the micelle-micelle interaction or micellar clustering plays an important role in the back-extraction process of proteins.