Abstract: Disclosed are catalytically active water-insoluble protein aggregates comprising fusion proteins which comprise a coiled-coil domain and a catalytic domain, methods of manufacturing such protein aggregates, and their use.

Abstract: Disclosed are catalytically active water-insoluble protein aggregates comprising fusion proteins which comprise a coiled-coil domain and a catalytic domain, methods of manufacturing such protein aggregates, and their use.

Abstract: A lyase has an amino acid sequence selected from SEQ ID NOs: 1, 2 and 3, wherein the amino acid isoleucine in position no. 468 in the protein ApPDC-E469G, which is modified with respect to the wild type from Acetobacter pasteurianus, is replaced by an amino acid which occupies less space than isoleucine.

Abstract: The invention relates to a lyase and a lyase-encoding DNA, to vectors containing the DNA and to a method for the asymmetric synthesis of (S)-phenylacetylcarbinol. According to the invention, a lyase is provided, in which tryptophan is replaced with an amino acid at position 543 in protein ApPDC-E469G, said protein being modified with respect to the wild type of Aceobacter pasteurianus, or in which it is less space-filling than tryptophan. According to the invention, deoxyribonucleic acids are furthermore provided, which encode the lyase. (S)-phenylacetylcarbinol can be produced with the lyase according to the invention from the educts benzaldehyde and pyruvate or acetaldehyde with an enantiomeric excess of at least 94%.

Abstract: A method for producing cathine ((1S,2S)-norpseudoephedrine), in which, in a first reaction step, benzaldehyde is reacted with an acetyl donor according to formula (1), where R?H or COOH, by way of an (S)-selective lease to yield an enantiomer mixture according to formulas (2) and (3) and, in a second step, the compound according to formula (3) is reacted with an amine donor by way of an (S)-selective transaminase to yield (1S,2S)-norpseudoephedrine.

Abstract: A lyase has an amino acid sequence selected from SEQ ID NOs: 1, 2 and 3, wherein the amino acid isoleucine in position no. 468 in the protein ApPDC-E469G, which is modified with respect to the wild type from Acetobacter pasteurianus, is replaced by an amino acid which occupies less space than isoleucine.

Abstract: The invention relates to a lyase and a lyase-encoding DNA, to vectors containing the DNA and to a method for the asymmetric synthesis of (S)-phenylacetylcarbinol. According to the invention, a lyase is provided, in which tryptophan is replaced with an amino acid at position 543 in protein ApPDC-E469G, said protein being modified with respect to the wild type of Aceobacter pasteurianus, or in which it is less space-filling than tryptophan. According to the invention, deoxyribonucleic acids are furthermore provided, which encode the lyase. (S)-phenylacetylcarbinol can be produced with the lyase according to the invention from the educts benzaldehyde and pyruvate or acetaldehyde with an enantiomeric excess of at least 94%.

Abstract: A method for producing cathine ((1S,2S)-norpseudoephedrine), in which, in a first reaction step, benzaldehyde is reacted with an acetyl donor according to formula (1), where R?H or COOH, by way of an (S)-selective lease to yield an enantiomer mixture according to formulas (2) and (3) and, in a second step, the compound according to formula (3) is reacted with an amine donor by way of an (S)-selective transaminase to yield (1S,2S)-norpseudoephedrine.

Abstract: The present invention relates to a nucleotide sequence which encodes a benzaldehyde lyase and to its use in a process for stereoselectively preparing 2-hydroxyketone group-containing compounds.

Abstract: The present invention relates to a nucleotide sequence which encodes a benzaldehyde lyase and to its use in a process for stereoselectively preparing 2-hydroxyketone group-containing compounds.

Abstract: Novel improved enzymes prepared by recombination, especially to rec-FDHs. Directed evolution has made it possible to generate catalytically more active and more stable muteins which can preferably be used in an industrial process for the preparation of e.g. amino acids. The invention further relates to the nucleic acids coding for these enzymes, to vehicles containing these nucleic acids and to advantageous primers for the preparation of the nucleic acids by means of PCR. The invention additionally relates to a process for the preparation of further improved rec-FDHs, and a method of screening more stable and/or more active dehydrogenases is claimed.

Abstract: The invention relates to new mutants of formate dehydrogenase from Candida boidinii, new gene sequences encoding these and use of the new formate dehydrogenases. The wild type FDH used hitherto in the industrial process for preparing amino acids becomes inactive after a certain time. New mutants of this wild type have been produced by targeted mutagenesis of a recombinant FDH from E. coli. The new mutants are preferably used in an enzymatic process for preparing chiral compounds.

Abstract: A process for obtaining a pyruvate decarboxylase by isolation from a producer organism. The pyruvate decarboxylase is capable of forming (R)-(-)-phenylacetylcarbinole (I) in .gtoreq.95% enantiomer unit with a product ratio of (I) to 2-hydoxypropiophenone of .gtoreq.95%. In addition, the pyruvate decarboxylase has a specific activity with regard to phenylacetylcarbinole formation of >1U/mg. It is the aim of the invention to obtain a pyruvate decarboxylase with improved synthesis capacity concerning the formation of (R)-(-)-phenylacetylcarbinole. The process of the invention developed for this purpose is characterized in that use is made of a producing organism with a gene coding for pyruvate decarboxylase from Zymomonas mobilis, in the DNA sequence of which the tryptophane radical coding codon TGG is replaced at position 1174-1176 by a codon which codes for an amino acid radical with a reduced volume ratio.