Dsm Fine Chemicals Austria Nfg Gmbh & Co. Kg

Basf Se Corporation

Patheon Austria Gmbh & Co. Kg

Dsm IP Assets B.v.

Roche Diagnostics Operations, Inc.

Sandoz Ag

Siemens Matsushita Components Gmbh & Co Kg

Dsm Chemie Linz Gmbh

Dsm Fine Chemicals Austria Gmbh

Dpx Holdings B.v.

Patheon Holdings I B.v.

Roche Diagnostics Gmbh

F. Hoffmann-la Roche Ag

Helmut Schwab

Wolfgang Skranc

Harald Pichler

Herfried Griengl

Kerstin Steiner

Christoph Kratky

Bernhard Hauer

Anton Glieder

Hans Wolfgang Höffken

Irma Wirth

Herbert Mayrhofer

Gerhard Steinbauer

Rudolf Neuhofer

Marcel G Wubbolts

Peter Pöchlauer

Cecilia Kvarnström Branneby

Peter Pojarliev

Christoph Reisinger

Martin Kietzmann

Rodolfo Bona

Ingrid Dreveny

Romana Wiedner

Micheal Stanek

Joannes Kierkels

Manuela Hermann

Christoph Zenzmaier

Sabine Feichtenhofer

Marlene Buchebner

Brigitte Pohn

Ingrid Osprian

Mandana Gruber

Hans Schoemaker

Rainer Mueller

Harald Sobek

Franz Effenberger

Alfred Engel

Michael Greif

Dominic De Souza

Oliver May

Michael Stanek

Marco Thomann

Martin Albert

Bernhard Suppmann

Andreas Berger

Sebastian Malik

Bernd Nidetzky

Harald Wajant

Joerg Salchenegger

Christine Jung

Robert Karner

Ferdinand Zepeck

Christiane Luley

Siegfried Fellner

Daniel Luschnig

Ernst Steiner

Sigurd Greiderer

Wijnand Peter Helena Peeters

Sabine Zitzenbacher

Natascha Hubertina Johannes Smeets

Mirela Ivancic

Siegfried F&ouml;rster

Ulrike Wagner

Meinhard Hasslacher

Michael Schall

Holger Buhler

Elfriede Marianne Hayn

Sepp Kohlwein

Gernot Strohmeier

Amin El-Heliebi

Peter Lauble

Rudolf Gijsbertus Marie Luiten

Kateryna Mykolayivna Lypetska

Christine Winkler

Norbert Landfahrer

Andreas Braun

Waander Riethorst

Peter Remler

Doris Osl

Tibor Czabany

Doris Ribitsch

Martin Schurmann

Katharina Schmoelzer

Marcel Wubbolts

Martin SCHÜRMANN

Dominic Desouza

The present invention relates to a method for producing chiral &#x3b2;-nitro alcohol compounds. The invention relates in particular to an (R)-selective cupin-nitroaldolase, which enantioselectively can catalyze the Henry reaction, wherein an aldehyde or ketone compound is converted to the corresponding &#x3b2;-nitro alcohol compound in the presence of a nitroalkane compound and a cupin-nitroaldolase.

(R)-selective nitroaldol reaction catalysed by proteins of the cupin superfamily

The present invention relates to a method for the enzymatic synthesis of enantiomerically enriched (R)-amines of general formula [1][c] from the corresponding ketones of the general formula [1][a] by using novel transaminases. These novel transaminases are selected from two different groups: either from a group of some 20 proteins with sequences as specified herein, or from a group of proteins having transaminase activity and isolated from a microorganism selected from the group of organisms consisting ofsp.,, and

(R)-selective amination

The invention relates to a method for the enzyme-catalysed hydrolysis of polyacrylic acid esters. According to the method, at least one polyacrylic acid ester is provided and incubated with at least one enzyme selected from enzymes (EC 3.1) acting on ester bindings, until the ester groups contained in the polyacrylic acid ester are partially or fully hydrolytically split, and optionally the modified polymer obtained thereby is isolated. The invention also relates to the enzymes used and mutants thereof, nucleic acids coding for the enzymes, vectors comprising the nucleic acids, micro-organisms comprising the vectors, and the use of the enzymes, the vectors or the micro-organisms for carrying out a method for the enzyme-catalysed hydrolysis of polyacrylic acid esters. The present application also relates to polymer reaction products that can be obtained by the method, and methods for producing esterases.

Method for the enzyme-catalysed hydrolysis of polyacrylic acid esters, and esterases used therefor

The present disclosure is directed to the use of certain glycosyltransferase variants having N-terminal truncation deletions. It was found that the combination of two different truncation variants of human &#x3b2;-galactoside-&#x3b1;-2,6-sialyltransferase I (hST6Gal-I) exhibited different specific sialyltransferase enzymatic activities. In one example, under conditions wherein the first variant &#x394;89 hST6Gal-I catalyzed formation of bi-sialylated target molecules the second variant &#x394;108 hST6Gal-I catalyzed formation of mono-sialylated target molecules. Thus, disclosed are variants of mammalian glycosyltransferase, nucleic acids encoding the same, methods and means for recombinantly producing the variants of mammalian glycosyltransferase and use thereof, particularly for sialylating in a quantitatively controlled manner terminal acceptor groups of glycan moieties being part of glycoproteins such as immunoglobulins.

Quantitative control of sialylation and specific mono-sialylation

The present invention relates to a recombinantstrain characterized in that the organisms contains a gene coding for a protein having esterase activity. Suchis suitable for the preparation of a protein with esterase activity, whereby the expression takes place without coexpression of GroEL and/or GroES from a plasmid. The expression of glutathione reductase and/or thioredoxin reductase may be abolished by mutation. Furthermore, the ability of the organism to grow under oxygen-rich conditions has been restored by mutation. The expression of the gene of the protein with esterase activity is unaccompanied by the expression of an additional gene encoding a heat shock chaperone protein.

Preparation of an esterase

The invention relates to an isolated polypeptide having esterase activity comprising an amino acid sequence shown in any one of SEQ ID NO's 2, 4, 6, 8, 10, 12 or 14 or a homologue thereof, comprising an amino acid substitution or deletion of one or more amino acids as shown in said SEQ ID NO's and resulting in a mutant polypeptide having an increased concentration of the fraction of the mutant polypeptide being present as an active and soluble protein in cleared lysate of the mutant polypeptide expressed inrelative to the concentration of the fraction of the polypeptide without the mutation being present as an active and soluble protein in cleared lysate of the polypeptide without the one or more deletion or substitution expressed inunder the same conditions. The invention also relates to nucleic acid encoding the polypeptides according to the invention, and the use of the polypeptides.

Pig liver esterases

Polypeptide and recombinant protein having esterase activity which exhibit the amino acid sequence SEQ. ID. No. 1 and the use thereof.

Polypeptide having esterase activity and recombinant esterase and use thereof

The present invention relates to processes for the preparation of 5-methyl-3-nitromethyl-hexanoic acid ester and its salts. Also disclosed are processes for the preparation of 5-methyl-3-nitromethyl-hexanoic acid salt and a process for the preparation of 3-(aminomethyl)-5-methylhexanoic acid. (S)-5-Methyl-3-nitromethyl-hexanoic acid or (R)-5-methyl-3-nitromethyl-hexanoic acid in enantioenriched form or enantiopure form as well as salts thereof, (S)-5-methyl-3-nitromethyl-hexanoic acid ester or (R)-5-methyl-3-nitromethyl-hexanoic acid ester in enantioenriched form or enantiopure form and a compound, namely Formula (XIII), in racemic form, enantioenriched form or enantiopure form are also disclosed. 

Process for the stereoselective enzymatic hydrolysis of 5-methyl-3-nitromethyl-hexanoic acid ester

Method of resolving stereoselectively racemic 2-alkyl-5-halopent-4-ene-carboxylic esters of the formula (I) 

The invention relates to a method for producing chiral &#x3b1;-hydroxycarboxylic crystalline acids consisting in transforming cyanhydrins (R) or (S) into &#x3b1;-hydroxycarboxylic acids (R) or (S), respectively by enzymatic hydrolysis in the presence ofNCIMB 11540.

Method for producing chiral &#x3b1;-hydroxycarboxylic acids by enzymatic hydrolysis of chiral cyanohydrins

Method for producing chiral &#x3b1;-hydroxycarboxylic crystalline acids

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

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Graz, Austria

Helmut Schwab