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Degussa Aktiengesellschaft

Universitãt Stuttgart

University of Stuttgart

Evonik Degussa Gmbh

Burkard Wilms

Ralf Mattes

Christoph Syldatk

Anja Wiese

Josef Altenbuchner

Andreas Bommarius

Wilhelm Tischer

Markus Pietzsch

Joseph Altenbuchner

A whole cell catalyst is described comprising a hydantoinase, a racemase and a carbamoylase. Thus this catalyst is able to degrade hydantoins directly into the amino acids. Additionally, a process for the production of this catalysts and for the production of amino acids is claimed.

Whole cell catalyst

A novel rec-L-N-carbamoylase fromand its method of use for producing L-amino acids. The recombinantly produced L-carbamoylase is unexpectedly stable, so that an industrial method of producing L-amino acids can be established with it, in contrast to previously known L-carbamoylases.

Recombinant L-N-carbamoylase from Arthrobacter aurescens and method of producing L-amino acids therewith

A microorganism is described which is transformed with DNAs which encode a hydantoinnase, a racemase, and a carbamoylase. As a result, the microorganism is able to degrade hydantoins directly to amino acids. A process for the production of the microorganism and a process for producing amino acids with the microorganism is also described.

Whole cell catalysts

A novel rec-L-N-carbamoylase from and its method of use for producing L-amino acids. The recombinantly produced L-carbamoylase is unexpectedly stable, so that an industrial method of producing L-amino acids can be established with it, in contrast to previously known L-carbamoylases.

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Stuttgart, Germany

Burkard Wilms