Hydrolysis of palm and olive oils by immobilised lipase using hollow fibre reactor

Lipase from Mucor miehei immobilised by adsorption on microporous, asymmetric hollow fibre membrane reactors was used to hydrolyse two different oils, namely, palm and olive oils. The hydrolysis reaction was carried out at a temperature of 40 °C, an average transmembrane pressure (TMP) of 115 mmHg and oil and aqueous flow rates of 2.5 and 3.0 ml min^-1, respectively. It was experimentally proven that adsorption of lipase increased with temperature and was higher on hydrophobic membranes than hydrophilic ones. The effluent concentrations of fatty acid products were measured using gas chromatograph with FID detector. Hydrolysis experimental results were fitted to a multisubstrate kinetic model derived from the Ping Pong Bi Bi mechanism. The final model expression is useful for predicting the free fatty acid profile of the enzymatic hydrolysis of palm and olive oils for different substrate flow rates and enzyme loading.