Stability and stabilization of enzymes from mesophilic and thermophilic organisms in respect to their use in FIA-systems for the determination of L-lactate and acetate

The stabilization effect of 'bilayer encagement' on enzymes from mesophilic organisms and their 'thermophilic' counterparts was compared. Lactate dehydrogenases from pig heart and from a thermophilic bacterium (Clostridium thermohydrosulfuricum), respectively, showed stabilization factors of 4.5 (at 47 degrees C) and 12.8 (at 70 degrees C), respectively. For 'thermophilic' acetate kinase no stabilization effect of encagement was observed. Lactate dehydrogenase and acetate kinase from Clostridium thermohydrosulfuricum were immobilized to controlled porous glass and tested for their long-term stability. The 'thermophilic' enzymes showed by far a longer half-life as compared with the corresponding enzymes from pig heart and Escherichia coli, respectively, the half-life time of the flow injection system response with thermophilic lactate dehydrogenase at 35 degrees C attaining 250 h (mesophilic enzyme 89 h), and with thermophilic acetate kinase 79 h (mesophilic enzyme 24 h).