Abstract
The efficiency of enzymatic depolymerization in a membrane reactor was investigated. The model analysis was performed on bovine serum albumin hydrolysis reaction led by three different enzymes, for which kinetic equations have different forms. Comparing to a classic reactor, the reaction yield turns out to be distinctly higher for all types of kinetics. The effect arises from increasing (thanks to the proper selectivity of the applied membrane) the concentration of reagents in the reaction volume. The investigations indicated the importance of membrane selectivity election, residence time and at non-competitive inhibition the substrate (biopolymer) concentration in feed stream. Presented analysis is helpful in these parameters choice for enzymatic hydrolysis of different biopolymers.