engleski

Laccase-Catalyzed L-DOPA Oxidation on Macro and Microreactor Scale

Enzymatic oxidation of 3, 4-dihydroxyphenyl-L- alanine (L-DOPA) with laccase from Trametes versicolor was investigated in a batch laboratory-scale reactor and in a continuously operated microreactor. The reaction was described with double-substrate Michaelis- Menten kinetics. Kinetic parameters, evaluated in a 50 mL batch reactor, were used for the modelling of a microreactor, based on diffusion, convection and a non-linear reaction term, considering the velocity profile for laminar flow in a microchannel at steady-state conditions. Experimental data on L-DOPA conversions for both systems revealed good agreement with models predictions. Up to 87 % conversions of L-DOPA were achieved in a microreactor at residence times below 2 minutes.

laccase ; L-DOPA ; microreactor ; modelling

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