Triton X-100

Lee and Biellmann (1987)

Protease from Bacillus sp. ATCC 21536

Woll et al (1987)



Fletcher and Parrot (1988)


Isotridecanol in iso-octante/ Aliquat 336

Jolivalt et al (1990)



Dekker et al (1991)

Horseradish peroxidase


Paradkar and Dordick (1991)



Ayala et al (1992)






Ichikawa et al (1992)



Krei & Hustedt (1992)

Yeast alcohol dehydrogenase (YADH)


Sarcar et al (1992)

The solubilization of the proteins in the reverse micelles depends upon several factors. These include pH, ionic strength and ion type, choice of surfactant and solvent, water content of the micellar core and the physicochemical properties of the protein such as isoelectric point, hydrophobicity, size, charge density and charge distribution. Temperature has also been found to affect the solubilization process.

Leodidis and Hatton (1989) have reviewed the interphase transfer for selective solubilization of ions, aminoacids and proteins in reversed micelles. A phenomological model capable of predicting the selectivity of the water pools for the different cations in the AOT system has been developed by them. Solubilization of various amino acids in AOT reverse micelles has been analyzed and the partition coefficient has been correlated with a number of meaningful parameters. Similarly, the liquid-liquid extraction of proteins from an aqueous solution to a reversed micellar organic phase have been analyzed for the effect of pH, surfactant concentration and salt.

Hatton and his coworkers (Goklen and Hatton, 1987; Hatton 1989; Woll et al, 1989; Rahaman et al, 1988) have shown that the selective extraction of targetted protein and extra cellular alkaline protease can be achieved by manipulating several parameters such as the aqueous phase pH, ionic strength and the biospecific nature and concentration of ligand.

The denaturation of proteins has been reviewed by Sadana (1994). He has discussed the effects of concentration of surfactant, type of solvent, temperature, processing conditions and solubilization process on the protein inactivation by compiling data from different sources.

Reverse micelle extraction is of great importance as it can be made selective, is easily scalable, and can be operated continuously. The solubilized protein can be partitioned back into aqueous phase by suitable modification of the conditions such as pH, ionic strength, etc.

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