For the compounds studied, delta Cp was not negligible and was closer to delta Sf than to zero. However, neither of the two assumptions was valid for accurately estimating the ideal solubility as given by the full equation.

The influences of water activity and solvent hydrophobicity on the kinetics of the lipase-catalyzed enantioselective esterification of flurbiprofen with nbutanol were investigated. The solvent effect was not similar for lipases from Candida rugosa (Crl), Mucor javanicus (Mjl), and porcine pancreas (Ppl). The lipasecatalyzed reaction rates in different solvents across a wide range of water activities revealed that the Pplcatalyzed reaction exhibited no enantioselectivity and no substantial water activity or solvent dependence. The Mjl-catalyzed reaction proceeded faster, preferring the R-enantiomer reaction over that of its antipode, but had little solvent or water activity dependence. The Crlcatalyzed reactions in n-heptane and n-nonane had similar water activity dependence, but the reaction was considerably faster and more enantioselective (preferring the S-enantiomer reaction) in isooctane, a solvent whose hydrophobicity is intermediate between that of the other two alkanes. Substrate enantiomeric excess, for the Crl-catalyzed reaction at 96 hours and at a water activity of 0.65, in n-heptane, isooctane, and nnonane was 40.9, 93.0, and 50.0%, respectively. Since the three solvents possess similar physical properties, the explanation for this anomalous behavior might be the effect of the solvent structural characteristics on Crl, since isooctane is the only branched alkane.