Effect of hydrophobicity on reversed micellar extraction of oligopeptides.

Reverse Micelle Liquid-Liquid Extraction of a Pharmaceutical Product

“…To date, the reverse micelle system has been used for the separation of proteins (Goklen and Hatton, 1987;Aires-Barros and Cabral, 1991;Su and Lee, 1999;Noh and Imm, 2005;Hecth and Peled, 2006;Shen and Yu, 2007), peptides (Kishi and Furusaki, 1992), amino acids Furusaki and Kishi, 1992;Adachi et al, 2000;Ddvyap et aI., 2006), bovine serum albumin (BSA) (Zhang et al, 1999), enzymes (Moreno-Hagelsieb et al, 1999;Liu et al, 2004;Debnath et al, 2007) and metals (Nakashio et al, 1992;Ismael and Tondre, 1992;Zhang et aI., 2006;Majumdar and Mahapatra, 2007) as well as in a bioreactor to carry out biotransformation (Kamiya et al, 1995). Thus, reverse micelle has been demonstrated to be capable of hosting large quantities of biomolecules without causing denaturation by adjusting operational parameters (Hatton, 1985;Paradkar and Dordick, 1994;Goto et al, 1998;Cardoso et al, 1999;Shen and Yu, 2007).…”

“…Leodidis and Ratton (1989) pointed out the importance of hydrophobic effects as a driving force for interfacial solubilisation by correlating hydrophobicity with the free energy of transfer of a large number of amino acids from water to the surfactant interfaces. Reverse micelle extraction of oligopeptides was investigated by Kishi and Furusaki (1992) who found that the partition coefficient ofthe peptides increased with an increase in the hydrophobicity of the peptide. It is also likely that proteins with surface hydrophobic regions exhibit an anomalous behavior, being extracted to the reversed micelle organic phase at unfavorable values of pR or high salt concentration as observed by Aires- Barros and Cabral (1991).…”