Barbaric and Luisi

Figure 9.11 A case of selective compartmentation in reverse micelles, permitting the synthesis of a peptide by the reverse protease action. The product C, produced in the water pool, is expelled into the outside hydrocarbon environment due to its insolubility in water. (Adapted from Barbaric and Luisi, 1981.)...

Figure 9.11 shows a classic example of compartmentation of reverse micelles (Barbaric and Luisi, 1981) chymotrypsin entrapped in reverse micelles catalyzes... 

Figure 9.16 Reverse micelles as microreactors an overview of the compartmenta-tion behavior of reverse micelles with basic references (a) Zampieri et al, 1986 Haring et al., 1988 Leser and Luisi, 1990. (b) Barbaric and Luisi, 1981 Luthi and Luisi, 1984 Walde and Luisi, 1989 Luisi and Laane, 1986. (c) Haring et al., 1985 Hochkoppler and Luisi, 1989 Famiglietti et al., 1992. (d) Imre and Luisi, 1982 Palazzo and Luisi, 1992 Pietrini and Luisi, 2002 Ousfuri et al., 2005.

The properties of a protein in a reverse micelle depend strongly on water content. Typically, at mole ratios of water to surfactant (wo) of less than about 3, there is no enzyme activity. As Wg is increased the activity sharply rises, sometimes to an optimum value at Wg — 5-20. The value of kcat for chymotrypsin is as much as 5-fold greater in AOT reverse micelles than it is in aqueous solution (Barbaric and Luisi, 1981 Fletcher... 

Barbaric, S. and Luisi, P. L. (1981). Micellar solubilization of biopolymers in organic solvents. 5. Activity and conformation of a-chymorypsin in isooctane-AOT reverse micelles. J. Am. Chem. Soc., 103,4239 4. 

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