Immobilized enzyme kinetics analyzed by flow-through microfluorimetry : Resorufin-β-d-galactopyranoside as a New Fluorogenic Substrate for β-Galactosidase

Bioreactor kinetics depend on the dispersion of catalytic parameters within the catalyst particle population. In the conventional determination, reactor performance is assessed from the total turnover rate. In the proposed method the dispersion of turnover rates in reacting immobilized enzyme gel spheres of a continuously stirred tank reactor is evaluated. This more informative method is based on flow-through microfluorimetry and is exemplified with β-galactosidase immobilized on Sepharose 4B, with resorufin-β-d-galactopyranoside as a new fluorogenic substrate. By use of sieved gel fractions, effectiveness factors and Damköhler numbers determined in individual beads can be correlated with integral turnover rates of the reactor.