Purification of S-oxynitrilase from Sorghum bicolor by immobilized metal ion affinity chromatography on different carrier materials.
The purification of the hydroxynitrile lyase (EC 4.1.2.11, S-oxynitrilase) from Sorghum bicolor is compared using different strategies. A new procedure is presented, which exploits the affinity of S-oxynitrilase towards metal ions as a key step in purification. The metal ions are immobilized by chelators on different carrier materials, e.g. Sepharose beads, microporous membranes or poly(ethylene glycol). A systematic examination demonstrates the excellent potential of immobilized metal affinity chromatography as a preparative separation method.
Woker
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R
Institut für Enzymtechnologie Heinrich-Heine-Universität Düsseldorf, Jülich, Germany.
Champluvier
B
B
Kula
M R
MR
D000446:Aldehyde-Lyases / Q000302:isolation & purification*; D002846:Chromatography, Affinity / Q000379:methods*; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D003300:Copper / Q000737:chemistry; D002523:Edible Grain / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D007098:Imino Acids; D008670:Metals; D011092:Polyethylene Glycols; D013056:Spectrophotometry, Ultraviolet
D007098:Imino Acids; D008670:Metals; D011092:Polyethylene Glycols; D003300:Copper; D000446:Aldehyde-Lyases; C079359:hydroxymandelonitrile lyase; C008109:iminodiacetic acid