Zu Ad- und Desorption von Proteinen an hydrophoben Adsorbentien (2007) Dissertation, Logos-Verlag 2007 .
Zeitschriftenbeiträge (peer-reviewed)
Prof. Dr. Marcus Millitzer,
Edda Wenzig,
Wolfgang Peukert
Berechtigungen: Peer Reviewed
Process modeling of in situ‐adsorption of a bacterial lipase (2005) Biotechnology and Bioengineering 92 (6), S. 789-801.
DOI: 10.1002/bit.20661
In situ adsorption, known as an in situ‐roduct removal (ISPR) technique for low molecular mass bioproducts, was in this study applied to a bacterial exoenzyme proving that this method is also suitable for the separation of macromolecules like proteins. For this, adsorbent particles were added to growing cultures of Staphylococcus carnosus rec., therefore both production and adsorption occurred simultaneously in shaking flasks, stirred tank, or airlift bioreactor as the chosen types of fermenters. The exoenzyme lipase adsorbed rapidly and, after separating cells and adsorbents, desorbed in a packed bed column. Up to 85% of the produced lipase were recovered, fractions of these had been concentrated up to the factor 20 and purified up to a factor of 40 by the procedure. By using the airlift bioreactor an enhancement of biomass production was observed, but the necessity of the addition of an anti‐foam reagent resulted in higher product losses in adsorption as well as in desorption. Production and adsorption kinetics have been modeled and applied to in situ‐adsorption. The model was used to perform a parameter study in which the influence of biological and physical parameters as well as process parameters on discontinuous and continuous in situ‐adsorption was investigated.
Vorträge
Prof. Dr. Marcus Millitzer,
Edda Wenzig,
Wolfgang Peukert
In situ-Adsorption of a Bacterial Lipase: Realization, Modelling and Influence of Parameters (2005) Vortrag auf dem 1st European Congress on Life Science Process Technology, Nürnberg 11.-13. Oktober 2005 .
Zeitschriftenbeiträge
Prof. Dr. Marcus Millitzer,
Edda Wenzig,
Wolfgang Peukert
Adsorption Isotherms and Irreversible Binding of Proteins on Commercially Available Hydrophobic Adsorbents (2005) Chemical Engineering & Technology 28 (7), S. 756-761.
DOI: 10.1002/ceat.200500072
Quantitative data about the behavior of proteins in different downstream processing unit operations are needed. Adsorption isotherms that are usually used to design such process steps may not be sufficient as for protein binding there is to distinguish between an adsorbing and a desorbing branch of the isotherm, leading to different apparent adsorption coefcients for adsorption and desorption, respectively. It is demonstrated that two different proteins show simultaneously reversible as well as irreversible ”adsorption” in hydrophobic interaction protein chromatography and that the reversible and the irreversible part of the apparent ”adsorption” isotherm can be separated.
Prof. Dr. Marcus Millitzer,
Edda Wenzig,
Wolfgang Peukert
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