(S)-hydroxynitrile lyases with improved substrate acceptance and their use
AssigneeDSM Fine Chemicals Austria GmbH
InventorsFranz Effenberger, Harald Wajant, Peter Lauble, Siegfried Förster, Holger Buhler, Helmut Schwab, Christoph Kratky, Ulrike Wagner, Ernst Steiner
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Abstract
(S)-Hydroxynitrile lyases which have an improved substrate acceptance and which are derived from the Hevea brasiliensis and Manihot esculenta (S)-hydroxynitrile lyases, wherein one or more bulky amino acid residues within the hydrophobic channel leading to the active center have been replaced with less bulky amino acid residues.
Claims13
An (S)-hydroxynitrile lyase obtained from Hevea brasiliensis or Manihot esculenta which (1) comprises a hydrophobic channel leading to an active center, (2) has one or more tryptophan residues within said hydrophobic channel replaced with alanine, glycine, valine or phenylalanine, and (3) has a higher percentage yield of cyanohydrin product than the wild-type (S)-hydroxynitrile lyase from substrates selected from the group consisting of aliphatic aldehydes, aromatic aldehydes and ketones.
Dependencies are inferred from the claim text.