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In situ-downstream processing of recombinant histidine-tagged proteins from cultivations of Bacillus megaterium

English · Paperback / Softback

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Purification of (recombinant) proteins for industrial and pharmaceutical use is accompanied by high costs and difficulties in the scale-up with the necessity of many purification steps. This thesis demonstrates the use of functionalized superparamagnetic iron oxide nanoparticles for the purification of recombinant histidine-tagged proteins directly from a growing culture of the gram-positive bacterium Bacillus megaterium. The separation was performed using commercial hand held magnets. Regenerability and reusability are shown in shake flask scale. Automation of the process is demonstrated at lab scale bioreactors using two model proteins, Protein A and the antibody fragment ¿-Lysozyme D1.3scFv. The process demonstrates a quick and easy way to yield a product of high purity within a short period of time.

About the author










Johannes Gädke, born in Alfeld (Leine), Germany, has studied biotechnology with focus on bioprocess engineering from 2008 until 2013 at the Technische Universität Carolo-Wilhelmina in Braunschweig, Germany. After his studies in Waterloo, Ontario, Canada from 2011 until 2012, aided by a scholoarship from the German Academic Exchange Service, he completed his master thesis in Germany with the degree M. Sc. Biotechnology. He started his PhD-studies in the autumn of 2013 at the Institute of Biochemical Engineering which he finished in early 2017. His research was situated within the scientific research group SynFoBia, Novel synthesis and formulation methods for poorly soluble drugs and sensitive biopharmaceuticals, at the Center of Pharmaceutical Engineering in Braunschweig, Germany.

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