Adsorption behaviour of lipase from Staphylococcus carnosus on a hydrophobic adsorbent.
The adsorption of proteins on a solid surface with a subsequent desorption is a well known final purification step in downstream processing. Here the adsorption behaviour of a microbial lipase on the hydrophobic Fractogel TSK butyl 650 in a crude fermentation supernatant is investigated. The measured equilibrium curves differ from fermentation to fermentation by up to +/- 65%. The adsorption capacity increases with decreasing particle diameter of the adsorbent and is influenced by the method of contacting the supernatant with the adsorbent. The rate of desorption depends largely on the adsorption conditions, which is an indication of different orientations of the adsorbed enzyme.
Kerzel
P
P
Department B of Chemical Engineering, Technical University of Munich, Germany.
Mersmann
A
A
D000327:Adsorption; D000645:Ammonium Sulfate; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D002846:Chromatography, Affinity; D004983:Ethanolamines; D005285:Fermentation; D008049:Lipase / Q000737:chemistry* / Q000302:isolation & purification; D010316:Particle Size; D011108:Polymers; D013210:Staphylococcus / Q000201:enzymology*
C069349:DEAE Fractogel TSK 650M; D004983:Ethanolamines; D011108:Polymers; D008049:Lipase; D000645:Ammonium Sulfate