USE OF CANDIDA-RUGOSA LIPASE IMMOBILIZED IN A SPIRAL WOUND MEMBRANE REACTOR FOR THE HYDROLYSIS OF MILKFAT

Lipase from C. rugosa was immobilized by adsorption on flat sheets made of microporous polypropylene and placed into a reactor in a spiral wound (axial-annular flow) configuration. Equations based on a Ping Pong Bi Bi kinetic mechanism are used to model the effect of the water content of the feed emulsion on the rate of hydrolysis of milkfat triglycerides. The kinetic data are consistent with a mechanism which assumes that deacylation of the enzyme is the rate-limiting step of the hydrolysis reaction. The optimum pH for hydrolysis is ca. 7.0. Operation of the reactor yielded relatively high conversions at short space times, thus indicating that this type of reactor is an interesting option for use on an industrial scale for the production of lipolysed butteroil.