E. Michalková

TL;DR: A simple method for the direct measurement of the catalytic properties of immobilized cells in the flow minicalorimeter, the enzyme thermistor (ET), is presented and it was shown that the rate of reaction catalyzed by T. variabilis entrapped in calcium pectate gel was limited by internal diffusion to an extent depending on the cell concentration in the biocatalyst particle.

TL;DR: A simple method for the direct measurement of the catalytic properties of immobilized cells in the flow minicalorimeter, the enzyme thermistor (ET), is presented and it was shown that the rate of reaction catalyzed by T. variabilis entrapped in calcium pectate gel was limited by internal diffusion to an extent depending on the cell concentration in the biocatalyst particle.

TL;DR: The storage stability of immobilized biocatalysts with MnO2 was nearly doubled and production of 2-oxoadipyl-7-aminocephalosporanic acid was 2–3-fold higher than by entrapped cells without MnO1 and the process was evaluated in terms of activity, immobilization yield, storage stability and oxo-product formation by immobilized preparations.

TL;DR: Direct activity determination by a flow-through microcalorimetry in the enzyme thermistor system was employed for a fast comparison of (poly)acrylamide gel-entrapped penicillin G acylase preparations and the validity of the results was corroborated by spectrophotometric measurements.