Purification of S-oxynitrilase from Sorghum bicolor by immobilized metal ion affinity chromatography on different carrier materials

J Chromatogr. 1992 Dec 11;584(1):85-92. doi: 10.1016/0378-4347(92)80012-f.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Aldehyde-Lyases / isolation & purification*
  • Chromatography, Affinity / methods*
  • Chromatography, Gel
  • Chromatography, Ion Exchange
  • Copper / chemistry
  • Edible Grain / enzymology*
  • Hydrogen-Ion Concentration
  • Imino Acids
  • Metals
  • Polyethylene Glycols
  • Spectrophotometry, Ultraviolet

Substances

  • Imino Acids
  • Metals
  • Polyethylene Glycols
  • Copper
  • Aldehyde-Lyases
  • hydroxymandelonitrile lyase
  • iminodiacetic acid