Abstract

Immobilization has been proposed as a way to simplify the separation and repeated reuse of enzymes, which is essential for their feasible application at industrial scales. However, in their immobilized form, enzyme activity is fully utilized, due primarily to the additional diffusion limitations. Here, the immobilization of lipase on zeolite and its use in catalyzing oil hydrolysis is studied. Adsorption isotherms were investigated, and the data identified the model that best describes the process, which is the Sips model. The adsorption capacity of zeolite was determined as 62.6 mg/g, which is relatively high due to the high porosity of the support. The rate of enzymatic hydrolysis of olive oil, using the immobilized lipase, was determined at a pH of 7 and a temperature of 40 °C and was compared to that when using free enzymes. The results determined the parameters for a diffusion-reaction model. The effects of both the surface reaction and diffusion were found to be significant, with a slightly higher effect from surface reactions.

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