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Kinetic characterization of esterification catalyzed by Rhizopus delemar lipase in lecithin-AOT microemulsion systems


, : Kinetic characterization of esterification catalyzed by Rhizopus delemar lipase in lecithin-AOT microemulsion systems. Journal Of Molecular Catalysis B Enzymatic. 4(1-2): 25-32,. 2

The esterification of oleic acid with octyl alcohol catalyzed by Rhizopus delemar lipase in microemulsion systems was investigated in terms of the kinetic parameters. The amphiphiles used were AOT and lecithin, both singly and as dual components. The enzyme activity in the lecithin system was high under hydrophobic conditions, i.e., at a WL (tbd (H2O)/(lecithin)) of 4.5, whereas in the AOT system it was high at W (tbd (H2O)/(AOT)) = 7. The reaction kinetics were recognized to follow the ping-pong bi-bi mechanism. A dual lecithin-AOT amphiphile system was effective in lipase catalyzed esterification, the maximum initial reaction rate being larger than those obtained in either of the single systems. The optimal molar fraction of lecithin for the maximum initial reaction rate differed with the water concentration in the microemulsion phase. Under relatively hydrophobic conditions, i.e., in a system with a lower WD (tbd (H2O)/(lecithin + AOT)), the initial reaction rate had a higher maximum value.

US$19.90

DOI: 10.1016/s1381-1177(97)00017-9


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