Dsm Fine Chemicals Austria Nfg Gmbh & Co. Kg

Dsm Fine Chemicals Austria Gmbh

Christoph Kratky

Helmut Schwab

Anton Glieder

Wolfgang Skranc

Herbert Mayrhofer

Irma Wirth

Rudolf Neuhofer

Peter Pöchlauer

Rodolfo Bona

Ingrid Dreveny

Franz Effenberger

Harald Wajant

Ernst Steiner

Ulrike Wagner

Holger Buhler

Siegfried F&ouml;rster

Peter Lauble

New genes containing a DNA sequence coding for hydroxynitrile lyase, which genes can be prepared via a primer combination based on the DNA sequence of the 5'-region of the mdl genes from theand fromand/or a primer 2 based on the 3&#x2032;-region of the DNA sequences of one of the hydroxynitrile lyase isoenzymes fromor from, subsequent amplification with a DNA polymerase using a DNA from organisms, containing genes coding for hydroxynitrile lyase, as templates and cloning, and also recombinant proteins which can be prepared in suitable host cells by heterologous expression of the DNA sequence of said HNL genes, and proteins and fusion proteins derived therefrom and use of said proteins for preparing (R)- or (S)-cyanohydrins.

Isolated protein having hydroxynitrile lyase activity

New genes containing a DNA sequence coding for hydroxynitrile lyase, which genes can be prepared via a primer combination based on the DNA sequence of the 5'-region of the mdl genes fromand fromand/or a primer 2 based on the 3&#x2032;-region of the DNA sequences of one of the hydroxynitrile lyase isoenzymes fromor from, subsequent amplification with a DNA polymerase using a DNA from organisms, containing genes coding for hydroxynitrile lyase, as templates and cloning, and also recombinant proteins which can be prepared in suitable host cells by heterologous expression of the DNA sequence of said HNL genes, and proteins and fusion proteins derived therefrom and use of said proteins for preparing (R)- or (S)-cyanohydrins.

Genes containing a DNA sequence coding for hydroxynitrile lyase, recombinant proteins derived therefrom and having hydroxynitrile lyase activity, and use thereof

(S)-Hydroxynitrile lyases which have an improved substrate acceptance and which are derived from the,and,(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.

(S)-hydroxynitrile lyases with improved substrate acceptance and their use

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Graz, Austria

Christoph Kratky