Degussa Aktiengesellschaft

Other

California Institute of Technology

Forschungszentrum Juelich Gmbh

Degussa - Huls Ag

University of Stuttgart

Degussa Aktiengesellchaft

Andreas Bommarius

Karlheinz Drauz

Maria-Regina Kula

Matthias Kottenhahn

Fritz Wagner

Carsten Bolm

Hans-Dieter Jakubke

Christian Wandrey

Michael Schwarm

Ralf Mattes

Wilhelm Tischer

Gunter Knaup

Michael Karrenbauer

Christoph Syldatk

Anja Wiese

Kyriakos Makryaleas

Burkard Wilms

Dirk Volkel

Ursula Stelkes-Ritter

Klaudia Wyzgol

Arne Gerlach

Uwe Eichhorn

Frances H Arnold

Udo Kragl

Guido Giffels

Stefan Verseck

Josef Altenbuchner

Guenter Knaup

Oliver May

Olaf Burkhardt

Hans Henniges

Andreas Karau

Jean-Louis Philippe

Karl-Heinz Drauz

Alexander Schwarz

Andreas Fischer

Nadine Derrien

Marcel Felder

Dirk Ullmann

Peter Kuhl

Thomas Wagner

Britta Hantke

Jens W&ouml;ltinger

Joseph Altenbuchner

Kai Boldt

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 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

Hydantoinase enzymes which are mutants of a previously isolated hydantoinase having the amino acid SEQ. ID. NO. 2. The mutants include amino acid substitutions at positions 95, 154, 180, 251 and/or 255 of the wild type hydantoinase (SEQ. ID. NO. 2). The mutant hydantoinases, like the parent hydantoinase, are used in the production of optically pure amino acids.

Hydantoinase variants with improved properties and their use for the production of amino acids

Process for the production of organic compounds in a membrane reactor. Inorganic membranes composed of an inorganic backing layer and an inorganic interlayer are used in the membrane reactor. The inorganic interlayer may be modified with organic groups.

Process for the production of organic compounds in a membrane reactor

The present invention is directed to an N-acetyl amino acid racemase (AAR) as well as the gene coding for it, to a plasmid, vector and microroganism containing the gene. A method of producing enantiomer-enriched amino acids, and derivatives thereof, is also provided.

N-acetyl amino acid racemase

A plant peptide amidase from the flavedo of oranges is known; this can be obtained only in small quantities and is seasonal. The proposed new enzymes are microbial peptide amidases which can be obtained from micro-organisms recovered from soil samples in a &ldquo;double screening&rdquo; and grown. These microbial peptide amidases are particularly useful for (a) the production of peptides and N-terminal-protected amino acids, (b) racemate splitting of N-protected amino acid amides, (c) obtaining non-proteinogenous D-amino acids, and (d) obtaining new N,-protected D-amino acid amides.

Process for obtaining microorganisms containing peptide amidase, microorganisms obtained therewith, peptide amidases contained in them and use thereof

It is known that dihydroquinine or dihydroquinidine derivatives can be successfully used as ligands in the enantioselective dihydroxylation. The new disclosed ligand systems based on dihydroquinine/quinidine, unlike the prior art ligands, can be recycled after enantioselective dihydroxylation by precipitating and filtering the reaction medium, and be reused in the reaction medium. Also disclosed are the ligand systems (I) and (IV), process for preparing the same and their use in the enantioselective dihydroxiation of double bonds.

Process for preparing MeO-Peg-protected dihydroquinine or dihydroquinidine derivatives, new dihydroquinine or dihydroquinidine derivatives and their use

The invention concerns a process for the enzymatic preparation of protected di- and oligopeptides and the separation of the protective groups used. The process according to the invention enables peptides to be synthesized simply and economically and the protective group to be separated carefully. The process comprises three reaction steps: 1. Preparation of N-carbamoyl amino acid or N-carbamoyl amino acid derivatives; 2. Formation of the peptide bond between the carbamoyl-protected electrophile and nucelophile; and 3. Separation of the carbamoyl-protective group.

Process for preparing peptides and N-carbamoyl-protected peptides

Process for the formation of MeO-Peg-protected dihydroquinine or dihydro quinindine derivatives, new dihydroquinine-or dihyroquinidine derivatives as well as the use thereof. It is known that dihydroquinine or dihydroquinidine derivatives can be successfully used as ligands in the enantioselective dihydroxylation. The new disclosed ligand systems based on dihydroquinine/quinidine, unlike the prior art ligands, can be recycled after enantioselective dihydroxylation by precipitating and filtering the reaction medium, and be reused in the reaction medium. Also disclosed are the ligand systems (I) and (IV), process for preparing the same and their use in the enantioselective dihydroxiation of double bonds.

The invention involves a procedure for the catalytic enantioselective reduction of ketones to chiral alcohols. Heretofore, this reaction was carried out batch-wise. Because, in this procedure, one utilizes a catalyst increased in size with polymer, it is possible to carry out the reaction in a quasi-continuous manner in a membrane reactor. In contrast to the state of the art, one thus dramatically increases the operative life of the catalyst.

Process for the catalytic enantioselective reduction of ketones

The disclosure relates to a process for obtaining optically active L-.alpha.-aminocarboxylic acids from the corresponding racemic D,L,.alpha.-aminocarboxylic acids. The following steps are involved: (a) the D,L,.alpha.-aminocarboxylic acids are acetylated; (b) the N-acetyl-L-.alpha.-aminocarboxylic acid present in the mixture of N-acetyl-D,L,.alpha.-aminocarboxylic acids thus obtained is broken down enzymatically into the L-.alpha.-aminocarboxylic acid; (c) the L-.alpha.-aminocarboxylic acid is separated from the mixture, a quantity of a solution of N-acetyl-D(L)-.alpha.-aminocarboxylic acids and a quantity of acetate equivalent to the L-.alpha.-aminocarboxylic acid being retained; and (d) the N-acetyl-D(L)-.alpha.-aminocarboxylic acid is racemized and recycled for enzymatic breakdown. Known extraction processes involving steps (a) to (d) have the disadvantage of producing large quantities of salt. Specifically, the processes are far removed from the ideal equation, according to which one hundred percent of the acetic anhydride and the D,L,.alpha.-aminocarboxylic acids are converted to L-.alpha.-aminocarboxylic acids and acetic acid. Adjusting the retained solution from step (c) in such a way as to obtain a solution consisting essentially of N-acetyl-D-(L)-.alpha.-aminocarboxylic acid salt and free acetic acid in equilibrium with acetate and free N-acetyl-D(L)-.alpha.-aminocarboxylic acid and from which acetic acid is extracted by distillation makes it surprisingly easy to feed the solution formed as 'mother liquor' following separation of the L-.alpha.-aminocarboxylic acid in the circuit and to achieve a materials balance as close as possible to the ideal.

Process for obtaining active L-.alpha.-amino carboxylic acids from

With known methods of racemizing N-acetyl-D(L)-.alpha.-amino carboxylic acids in the non-aqueous state by heating them to temperatures above room temperatures, significant quantities of by-products are formed, especially acetyl dipeptides. By converting at least a proportion of the N-acetyl-D(L)-.alpha.-amino carboxylic acids to corresponding N-acetyl-D(L)-.alpha.-amino carboxylic acid salts before or during the heating, it is possible to increase the sojourn time of the educt which is to be racemized at higher temperatures without any evident increase in the quantity of by-product formed (in particular acetylated dipeptides). Also disclosed is the production of optically active amino acids by enzymatic splitting of racemic compounds.

Process for racemization of N-acetyl-(D)L-.alpha.-amino carboxylic acids

Peptide amidase from xanthomonas

The invention relates to novel microorganisms, their use and method of producing L-.alpha.-amino acids. In particular, microorganisms DSM 7329 and 7330 are suitable for the production of L-.alpha.-amino acids from corresponding hydantoins or carbamoyl-.alpha.-amino acids. These novel microorganisms are simple to cultivate and make possible high L-.alpha.-amino acid yields from different substrates.

Microorganisms their use and method of producing L-.alpha.-amino acids

DSM 9771 is a mutant of DSM 7330 which was obtained under selective pressure. Its enzymatic activity is higher by a factor of 2.3 than that of its parent organism. In the presence of an inducer, this activity may be farther increased by a factor of 2.7. The reaction catalyzed by this microorganism or enzymes therefrom is the enantioselective conversion of a D-5-monosubstituted hydantoin or an L-5-monosubstituted hydantoin or a D-N-carbamoyl amino acid or an L-N-carbamoyl amino acid to a corresponding L-.alpha.-amino acid.

Microorganism, use thereof and process for the production of

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Frankfurt am Main, Germany

Andreas Bommarius