Kerasina Dimoula, Martina Pohl, Jochen Büchs, Antje Spieß:
Substrate and water adsorption phenomena in a gas/solid enzymatic reactor
Biotechnology Journal, 2009, 4(5), 712-721
The adsorption of water and substrates to dry deposited alcohol dehydrogenase from Lactobacillus brevis (LBADH) is studied in a continuous enzymatic gas/solid reactor. This work is aiming at obtaining a deeper and more thorough understanding of the enzyme microenvironment in the gas/solid system of acetophenone reduction with concomitant oxidation of 2-propanol. Extensive water adsorption studies showed that the effect of sucrose in the enzyme preparation on the water adsorption isotherm is significant for water activities exceeding 0.5 and reaches a factor 2 with respect to bead mass at water activity of 0.9. Significant hysteresis during water desorption is identified, resulting in up to 0.6 mgwater/mgprotein, for lyophilized enzyme preparation and up to 10 mgwater/mgprotein for deposited enzyme preparation. The adsorption of the substrates is quantified here for the first time. Whereas the adsorption of the main substrate, acetophenone, may reach a significant level of up to 6 mg/mgprotein, at an acetophenone activity of 0.32, the secondary substrate, 2-propanol is not adsorbed at a detectable degree. The presence of water leads to a decrease of the adsorbed amount of acetophenone, by approximately 25%, at a water activity of 0.54.
adsorption, adsorption isotherm, alcohol dehydrogenase, gas/solid biocatalysis, thermodynamic activity