The role of hydrogen mass transfer for the growth kinetics of Methanobacterium thermoautotrophicum in batch and chemostat cultures

Hydrogen concentration was determined in batch and chemostat cultures of Methanobacterium thermoautotrophicum, both in the headspace and in the medium using mass spectrometry. The calculated dissolved hydrogen concentration in the medium as derived from the headspace hydrogen concentration when equilibrium conditions between gas and liquid phase were assumed, was ten times higher than the experimentally determined hydrogen concentration. Variation of the partial pressure of hydrogen resulted in different values for substrate affinity for hydrogen (K_s) and yield (Y) of the cells. Upon hydrogen limitation, K_s decreased while the yield coefficient for hydrogen increased, indicating a change in the affinity of the cells towards hydrogen. Received 15 November 1996/ Accepted in revised form 21 July 1997     

Influence of oxygen adsorption on the dynamic K(L)a measurement in three-phase slurry reactors

To check for possible mass transfer limitations of oxygen and/or carbon dioxide in kinetic experiments on microbial desulphurization of coal, it is important to properly measure the volumetric mass transfer coefficient (k(L)a) especially at high slurry densities. Volumetric mass transfer coefficients of oxygen, at different solid hold-up values (epsilon(s) = 0 to 0.28) of coal slurries (d(par) < 100 * 10(-6) m), were measured in a lab scale fermentor and in a lab scale pachuca tank, using the dynamic gas-liquid absorption method. It was shown that serious errors could occur due to oxygen adsorption at the coal surface. Using the data of an independently measured adsorption isotherm, the real k(L)a could be calculated from the measured apparent k(L)a. The results show a k(L)a decrease of 40% to 50% at a volumetric solid hold-up of 28%. Estimation of the oxygen and carbon dioxide transfer rates, from the measured mass transfer coefficients, indicates that the stirred fermentor is suitable for kinetic experiments at high slurry densities, whereas the pachuca tank and shake flask are not. (c) 1992 John Wiley & Sons, Inc.     

Peptide NMHRYPNQ of the Cellular Prion Protein (PrP) Inhibits Aggregation and Is a Potential Key for Understanding Prion-Prion Interactions

Pathogenesis of transmissible spongiform encephalopathies is correlated with a conversion of the normal cellular form of the prion protein (PrP^C) into the abnormal isoform (scrapie form of PrP). Contact of the normal PrP with its abnormal isoform, the scrapie form of PrP, induces the transformation. Knowledge of molecules that inhibit such contacts leads to an understanding of the mechanism of the aggregation, and these molecules may serve as leads for drugs against transmissible spongiform encephalopathies. Therefore, we screened a synthetic octapeptide library of the globular domain of the human PrP^C for binding affinity to PrP^C. Two fragments with binding affinity, 149YYRENMHR156 and 153NMHRYPNQ160, were identified with K_d values of 21 and 25 μM, respectively. A 10-fold excess of peptide 153NMHRYPNQ160 inhibits aggregation of the PrP by 99%. NMR and mass spectrometry showed that the binding region of the peptide 153NMHRYPNQ160 is located at helix 3 of the PrP.