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  Aufreinigung und Charakterisierung des rekombinant hergestellten Enzyms Glycerokinase aus Pichia farinosa

Seidemann, J. (2010). Aufreinigung und Charakterisierung des rekombinant hergestellten Enzyms Glycerokinase aus Pichia farinosa. Diploma Thesis, Jena.

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Seidemann, J.1, 2, Autor           
Affiliations:
1Bioprocess Engineering, Max Planck Institute for Dynamics of Complex Technical Systems, Max Planck Society, ou_1738140              
2University of Applied Sciences Jena, Germany, persistent:22              

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 Zusammenfassung: Glycerokinase can be used as a coupling enzyme for sensitive enzyme activity measurements. The main goal of this work was the development of a purification strategy for recombinant Glycerokinase produced in Pichia pastoris. Subsequently, the purified enzyme was characterized with regard to pH- and temperature optima, as well as maximum reaction rate (Vmax) and Michaelis-Menten constant (Km) for ATP. The purification cascade included the following steps: cell disruption, solid liquid phase separation, immobilized metal chelate affinity chromatography, anion exchange chromatography, and a subsequent buffer exchange. The specific enzyme activity could be increased by a factor of 60 to 201.6 U/mg. A pH optimum of 7.0 was determined for purified Glycerokinase, whereas the temperature optimum was found to be 45°C. The enzyme kinetic constants Vmax 277.8 U/mg and Km 2.47 mM were obtained using Lineweaver-Burk plotting.

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Sprache(n): deu - German
 Datum: 2010-01
 Publikationsstatus: Angenommen
 Seiten: -
 Ort, Verlag, Ausgabe: Jena
 Inhaltsverzeichnis: -
 Art der Begutachtung: -
 Identifikatoren: eDoc: 443861
Anderer: Seidemann2010
 Art des Abschluß: Diplom

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