Characterization of benzaldehyde lyase from Pseudomonas fluorescens: A versatile enzyme for asymmetric C-C bond formation.

@article{Janzen2006CharacterizationOB,
  title={Characterization of benzaldehyde lyase from Pseudomonas fluorescens: A versatile enzyme for asymmetric C-C bond formation.},
  author={Elena Janzen and Michael M{\"u}ller and Doris Kolter-Jung and Malea M. Kneen and Michael J McLeish and Martina Pohl},
  journal={Bioorganic chemistry},
  year={2006},
  volume={34 6},
  pages={
          345-61
        }
}
The thiamin-diphosphate-dependent enzyme benzaldehyde lyase is a very import catalyst for chemoenzymatic synthesis catalyzing the formation and cleavage of (R)-hydroxy ketones. We have studied the stability of the recombinant enzyme and some enzyme variants with respect to pH, temperature, buffer salt, cofactors and organic cosolvents. Stability of BAL in chemoenzymatic synthesis requires the addition of cofactors to the buffer. Reaction temperature should not exceed 37 degrees C. The enzyme is… CONTINUE READING
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