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

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In situ-downstream processing of recombinant histidine-tagged proteins from cultivations of Bacillus megaterium (Volumen 79) (Tienda española)

Johannes Gädke (Autor)

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Indice, PDF (52 KB)
Lectura de prueba, PDF (73 KB)

ISBN-13 (Impresion) 9783736995512
ISBN-13 (E-Book) 9783736985513
Idioma Inglés
Numero de paginas 128
Edicion 1.
Serie Schriftenreihe des Institutes für Bioverfahrenstechnik der Technischen Universität Braunschweig
Volumen 79
Lugar de publicacion Göttingen
Lugar de la disertacion Braunschweig
Fecha de publicacion 15.06.2017
Clasificacion simple Tesis doctoral
Area Microbiología y biotécnica
Palabras claves In situ, downstream processing, purification, SPION, superparamagnetism, Bacillus megaterium, scale-up
Descripcion

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 α-Lysozyme D1.3scFv. The process demonstrates a quick and easy way to yield a product of high purity within a short period of time.