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The influence of water content on the lipase-catalyzed acidolysis of triolein (glycerol-trioleate, TO) and caprylic acid (CA) in hexane, using an immobilized enzyme was studied. An adequate water content (R W ) ranged from near zero to 0.1 g of water/g of dry enzyme. Over these values there was a decrease in the rate of incorporation of CA into triglyceride. This decrease was attributed to the progressive flooding of the carrier's pores, in which the enzyme was immobilized. The flooding reduced the number of the enzyme molecules at the water-hexane interface and therefore, hindered the accessibility of the hydrophobic substrates (TO and CA) to the enzyme. A simple physical model based on a characterization of the immobilized enzyme particle by mercury porosimetry was developed. The model agreed well with both the experimental data and the prior published data. The model may partly explain the observed inhibition when using low molecular weight alcohols and carboxylic acids in immobilized lipase-catalyzed processes.

The influence of the molar ratio caprylic acid/triolein, enzyme concentration and water content on the kinetics of the interesterification reaction of triolein (TO) and caprylic acid (CA) were studied. The enzyme used was the 1,3-specific Rhizomucor miehei lipase. Data modelling was based on a simple scheme in which the acid was only incorporated in positions 1 and 3 of the glyceride backbone. In addition, it was assumed that positions 1 and 3 of the triglycerides were equivalent and that the events at position 1 did not depend on the nature of the fatty acid in position 3 and vice versa. Monoglycerides and diglycerides were not detected during the experiments. This was attributed to the low water content of the immobilised enzyme particles. The value of the equilibrium constant, K, for the exchange of caprylic and oleic acids was 2.7, which indicated that the incorporation of caprylic acid into triglycerides was favoured compared with the incorporation of oleic acid. Simple first order kinetics could describe the interesterification reaction. Using this model and the calculated equilibrium constant, the apparent kinetic constants were calculated. The model fitted all the experimental data except for the CA/TO molar ratios larger than 6. Moreover, the interesterification reaction rate had a maximum value at CA/TO molar ratios of 4-6 mol mol À1.

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