Hoechst Aktiengesellschaft

Aventis Pharma Deutschland, Gmbh

Hoechst Marion Roussel Deutschland Gmbh

Johannes Meiwes

Gerhard Kretzschmar

Peter Hammann

Dieter Wullbrandt

Carlo Giani

Ulrich Lerch

Susanne Grabley

Manfred Schudok

Klaus-Peter Koller

Reinhardt Rothert

J&uuml;rgen Bongs

Wolfgang Kruse

Paul Habermann

Joachim Wink

Gerhard Seibert

Astrid Markus

Gerhard Seipke

Rudiger Marquardt

Michael Dorschug

Johann Ertl

Manfred Worm

Brigitte Hoersch

Ruediger Marquardt

Andreas Seiffert-Stoeriko

Jürgen Bongs

L&aacute;szl&oacute; Vertesy

The invention relates to a method for catalysing complex reactions or large molecules, more specifically, to enzyme-catalysed reactions during which undesirable consecutive or subsidiary reactions usually occur; using enzymes which are bonded to a polymer support. According to the invention, undesirable consecutive or subsidiary reactions are to a large extent avoided by selecting a non-porous or almost non-porous support material. In particular, the invention relates to a method for the enzymatic extraction of biomolecules, preferably peptides, proteins, oligosaccharides or polysaccharides from their biologically inactive precursors using enzymes which are bonded to a polymer support, especially a method for extracting insulins or their analogs from the corresponding precursors using enzymes which are bonded to a polymer support. As a result of selecting a non-porous almost non-porous support material, this method leads to a selective formation of biomolecules, especially of insulins or insulin analogs and corresponding valuable substances which can be split into said insulins or their analogs, undesirable consecutive or subsidiary reactions being to a large extent avoided.

Method for extracting an insulin using enzymes which are bonded to a non-porous polymer support

The present invention relates to a process for delaying the deactivation of glutaryl amidase during enzyme catalysis. The enzyme catalyst is, after maximum conversion of the substrate, separated off by filtration and can be reused in a subsequent reaction batch. In each reaction cycle, the enzyme catalyst loses activity. The inactivation of the enzyme catalyst can be delayed by bringing it into contact with a thiol during the reaction.

Process for delaying the deactivation of glutaryl amidase during enzyme catalysis

C peptide for improved preparation of insulin and insulin analogs

A process is provided for delaying the deactivation of glutaryl amidase during catalysis. The amidase is, after maximum conversion of a substrate, separated off by filtration and can be reused in a subsequent reaction batch. In each reaction cycle, the amidase loses activity. The inactivation of the amidase can be delayed by bringing it into contact with a thiol during the reaction. The thiol is preferably 2-mercaptoethanol or cysteine.

Process for delaying the deactivation of glutaryl amidase during catalysis with a thiol

The invention relates to lipopeptides with very homologous amino-acid sequences but different fatty acid residues (lipid portion) which are synthesized by Actinoplanes sp. during fermentation and are released into the culture medium, to a process for isolating the lipopeptides from the culture medium and purifying them, to the use of the lipopeptides as pharmacologically active substances, in particular against Gram-positive bacteria, and to Actinoplanes sp. DSM 7358 for producing the abovementioned lipopeptides.

Lipopeptides from actinoplanes sp. with pharmacological action, process for their production and the use thereof

The invention relates to the preparation of the compound 4-(4-(4-(hydroxydiphenyl)-1-piperidinyl)-1-hydroxybutyl)-.alpha.,.alpha.-d imethylphenylacetic acid and its phosphorylated derivatives. These compounds can be prepared from .alpha.-(p-tert-butylphenyl)-4-(.alpha.-hydroxy-.alpha.-phenylbenzyl)-1-pi peridinylbutanol with the aid of fungi of the genus Cunninghamella or Absidia. The compounds according to the present invention can be used as pharmaceuticals for the treatment of allergic disorders, allergic rhinitis or asthma. Compounds of the formula II in which R.sup.1 is --CH.sub.2 --O--P(O)(OH).sub.2 and R.sup.2 is --OH; R.sup.1 is --CH.sub.3 and R.sup.2 is --O--P(O)(OH).sub.2 ; or

Process for the preparation of

The present invention relates to an improved process for isolating and purifying sugar nucleotides, in particular cytidine monophosphate-activated N-acetylneuraminic acid (CMP-Nana), from biological sources. The sugar nucleotides can be obtained from a sugar nucleotide-containing solution, which has been freed of proteins by alcoholic precipitation, by means of an improved column-chromatographic method which uses silica gel as the stationary phase, and at a purity level which requires only a subsequent desalting step to obtain a substantially pure product.

Process for isolating and purifying nucleotide-activated sugars from

Process for the biotechnological preparation of L-thienylalanines in enantiomerically pure form from 2-hydroxy-3-thienylacrylic acids, and their use. L-Thienylalanines are prepared via the hydantoin or the azlactone route. The starting substances used for the biotransformation are 2-hydroxy-3-thienylacrylic acids. The innovative step consists in the transamination of the enol form of the 2-hydroxy-3-thienylacrylic acids to give L-thienylalanines with the aid of biotransformation. The transaminiation is carried out in the presence of L-aspartic acid or L-glutamic acid as amino donor.

Process for the biotechnological preparation of L-thienylalanines in

A process is described to specifically hydrolyze the amino acid chain of preproinsulin analogs to give the corresponding insulins. The hydrolysis is catalyzed by clostripain and, if necessary, carboxypeptidase B.

Clostripain catalyzed hydrolysis of preproinsulin analogs into

Process for the biotechnological preparation of L-thienylalanines in enantiomerically pure form from 2-hydroxy-3-thienylacrylic acids L-Thienylalanines are prepared via the hydantoin or the azlactone route. The starting substances used for the biotransformation are 2-hydroxy-3-thienylacrylic acids. The innovative step consists in the transamination of the enol form of the 2-hydroxy-3-thienylacrylic acids to give L-thienylalanines with the aid of biotransformation. The transaminiation is carried out in the presence of L-aspartic acid or L-glutamic acid as amino donor.

Bacterial strains are capable of the formation of rhamnolipids, which they generate in the culture solution. If bacteria of the type Pseudomonas aeruginosa are employed for the fermentation, these microorganisms synthesize rhamnolipids in a concentration of 70-120 g/l of culture solution. The L-rhamnose can be recovered directly from the culture solution by hydrolysis of the rhamnolipids, i.e. without a complicated separation of the cell material and without isolation of the rhamnolipids before hydrolysis.

Pseudomonas aeruginosa and its use in a process for the biotechnological

The invention relates to .alpha.-L-rhamnosidase, which catalyzes the cleavage of the bond between terminal rhamnose and the aglycone of rhamnose-containing glycosides, a process for preparing it by biotechnological means, and its use for preparing L(+)-rhamnose (6-deoxy-L-mannose).

.alpha.-l-rhamnosidase for obtaining rhamnose, a process for its

Pseudomonas aeruginosa and its use in a process for the biotechnological production of L-rhamnose Bacterial strains are capable of the formation of rhamnolipids, which they generate in the culture solution. If bacteria of the type Pseudomonas aeruginosa are employed for the fermentation, these microorganisms synthesize rhamnolipids in a concentration of 70-120 g/l of culture solution. The L-rhamnose can be recovered directly from the culture solution by hydrolysis of the rhamnolipids, i.e. without a complicated separation of the cell material and without isolation of the rhamnolipids before hydrolysis.

L-Thienylalanines are prepared via the hydantoin or the azlactone route. The starting substances used for the biotransformation are 2-hydroxy-3-thienylacrylic acids. The innovative step consists in the transamination of the enol form of the 2-hydroxy-3-thienylacrylic acids to give L-thienylalanines with the aid of biotransformation. The transaminiation is carried out in the presence of L-aspartic acid or L-glutamic acid as amino donor.

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Idstein, Germany

Johannes Meiwes