Purification and Characterization of a Novel (R)-Mandelonitrile Lyase from the Fern Phlebodium aureum.

@article{Wajant1995PurificationAC,
  title={Purification and Characterization of a Novel (R)-Mandelonitrile Lyase from the Fern Phlebodium aureum.},
  author={Harald Wajant and Stephan Forster and Dirk Selmar and Franz Effenberger and Klaus Pfizenmaier},
  journal={Plant physiology},
  year={1995},
  volume={109 4},
  pages={1231-1238}
}
Using high-performance liquid chromatography and nuclear magnetic resonance we identified vicianin as the cyanogenic compound of Phlebodium aureum. The (R)-hydroxynitrile lyase involved during cyanogenesis in the catabolism of the aglycon ([R]-mandelonitrile) was purified to apparent homogeneity. The purified holoenzyme is a homomultimer with subunits of Mr = 20,000. At least three isoforms of the enzyme exist. In contrast to other hydroxynitrile lyases, mandelonitrile lyase (MDL) from P… CONTINUE READING

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