Abstract
An unsteady-state kinetic model has been proposed for the hydrolysis of palm oil by lipase in a stirred batch bioreactor. The hydrolysis model was derived from a reaction mechanism and simplified for conditions of low enzyme concentration. From it, the regions where the quasi-steady-state assumption for the intermediates is applicable is identified and verified experimentally. The experimental results showed that the hydrolysis of palm oil by lipase in a well-stirred reactor has a short induction time for the penetration of enzyme at the interface and for the formation of the enzyme–substrate complex. This indicates that the quasi-steady-state assumption for the intermediates is applicable under the operating conditions used in this study. It is also shown that increasing the agitation speed results in reduced induction time.
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