Henkel Ag & Company, Kgaa

Henkel Kommanditgesellschaft Auf Aktien

Basf Se Corporation

Henkel Kommanditgesellschaft Auf Aktien (henkel Kgaa)

Henkel Kgaa

B.r.a.i.n. Biotechnology Research and Information Network Ag

Henkel Corporation

Cognis Deutschland Gmbh & Co. Kg

Cognis Deutschland Gmbh

Cognis Gesellschaft Fuer Biotechnologie Mbh

Cognis Gesellschaft Fuer Bio Und Umwelttechnologie Mbh

Karl-Heinz Maurer

Beatrix Kottwitz

Albrecht Weiss

Petra Siegert

Hendrik Hellmuth

Stefan Evers

Marion Merkel

Angrit Weber

Angela Hellebrandt

Roland Breves

Cornelius Bessler

Thorsten Eggert

Patrick Lorenz

Regina Stehr

Rolf Wachter

Christian Degering

Ansgar Behler

Christian Nitsch

Peter Schmiedel

Susanne Wieland

Timothy O'Connell

Holger Tesmann

Ulrich Schwaneberg

Thomas Weber

Horst Upadek

Charles R Wilson

Teresa M Christianson

George A Smith

Hans-Christian Raths

Nina Mussmann

Wolfgang Von Rybinski

Frank Janssen

Thorsten Bastigkeit

Inga Kerstin Vockenroth

Christian G Paech

Inken Prueser

Dean W Goddette

Manfred Biermann

Horst-Dieter Speckmann

Thomas Eiting

Michael Krebs

Jürgen Eck

Kathleen Paatz

Marc-Steffen Schiedel

Hanns Misiak

Rolf Tenhaef

Konstantin Benda

Charles B Allen

J Frederick Hessel

Holger Zinke

Sven Mueller

Susanne Tondera

Irmgard Schmidt

Johannes Bongaerts

Laura Polanyi-Bald

Frank Niehaus

Ronny Martinez

Astrid Spitz

Maria R Tang

Gerhard Gottschalk

Winfried Pochandke

Birgit Veith

Hermanus Bernardus Maria Lenting

Pieter Van Solingen

Rudolf Franciscus Wilhelmus Cornelis Van Beckhoven

Jörg Feesche

Christina Herzberg

Michael Hansberry

Monika Boecker

Brian Laufs

Andreas Michels

Lukas Maksym

Petra Padurschel

Armin Ehrenreich

Heiko Liesegang

Anke Henne

Felix Jakob

Ayhan Aydemir

Sören Hölsken

Dorota Sendor-Mueller

Dorota Sendor-Müller

Jorg Poethkow

Sven Müller

Cornelia Kluin

Inken Prüser

Heribert Kaiser

Tobias Kueppers

Victoria Steffen

Jörg Poethkow

Wilfried Howorka

Renee Charlott Eichstadt

Ramona Knab

Ulrich Haas

Meine Georg

Terri Christianson

C Ron Wilson

André Pütz

Karl-Erich Jäger

Ralf Weidenhaupt

Renée Charlott EICHSTÄDT

The aim of the invention is to improve the secretion of a protein from a host cell in order to increase the product yield of protein in a fermentation process. This is achieved by an expression vector comprising a) a promoter sequence and b) a nucleic acid sequence that codes for a protein. The protein comprises a signal peptide and an additional amino acid sequence, and the signal peptide comprises an amino acid sequence that is at least 80% identical to the amino acid sequence specified in SEQ ID NO: 2, at least 80% identical to the amino acid sequence specified in SEQ ID NO: 4, at least 80% identical to the amino acid sequence specified in SEQ ID NO: 6, or the signal peptide comprises an amino acid sequence that is structurally homologous to at least one of said sequences.

Expression vectors with promoter and nucleic acid

The aim of the invention is to improve the secretion of a protein from a host cell in order to increase the product yield of protein in a fermentation process. This is achieved by an expression vector comprising a promoter sequence and a nucleic acid sequence that codes for a protein. The protein comprises a signal peptide and an additional amino acid sequence, and the signal peptide comprises an amino acid sequence that is at least 80% identical to the amino acid sequence specified SEQ ID NO: 2, at least 80% identical to the amino acid sequence specified in SEQ ID NO: 4, at least 80% identical to the amino acid sequence specified in SEQ ID NO: 6, or the signal peptide comprises an amino acid sequence that is structurally homologous to at least one of said sequences.

Expression vectors for an improved protein secretion

In a microbial fermentation, the aim is to increase the product yield of protein. This is achieved by a method in which an expression construct is introduced into a microorganism of the specieswhich comprises a promoter and a nucleic acid coding for the protein, and the protein is expressed in said expression construct.

Expression method

The stabilization of a hydrolytic enzyme in a liquid preparation is to be improved through a component that stabilizes the hydrolytic enzyme. This is accomplished by a method for adapting a hydrolytic enzyme to a component that stabilizes the hydrolytic enzyme, comprising the following method steps: a) providing a hydrolytic enzyme (starting enzyme) and a component that stabilizes the hydrolytic enzyme and that comprises a reversible inhibitor of the hydrolytic enzyme; b) changing the amino acid sequence of the hydrolytic enzyme in at least one position, by substitution, deletion or insertion; c) determining the relative activity of the hydrolytic enzyme from step b) and the relative activity of the starting enzyme in a liquid preparation; d) selecting the hydrolytic enzyme that has a reduced relative activity by comparison with the relative activity of the starting enzyme.

Method for adapting a hydrolytic enzyme to a component that stabilizes the hydrolytic enzyme

The aim is to increase the protein product yield in microbial fermentation. This is achieved by a method which introduces into a microorganism not only a first expression construct which encodes the protein, but also a second expression construct which encodes an auxiliary protease which differs from the protein, is proteolytically active and which comprises an amino acid sequence which is at least 50% identical to the amino acid sequence indicated in SEQ ID NO. 1.

The present invention relates to 25 hitherto undescribed genes ofand gene products derived therefrom and all sufficiently homologous nucleic acids and proteins thereof. They occur in five different metabolic pathways for the formation of odorous substances. The metabolic pathways in question are for the synthesis of: 1) isovalerian acid (as part of the catabolism of leucine), 2) 2-methylbutyric acid and/or isobutyric acid (as part of the catabolism of valine and/or isoleucine), 3) butanol and/or butyric acid (as part of the metabolism of butyric acid), 4) propyl acid (as part of the metabolism of propionate) and/or 5) cadaverine and/or putrescine (as parts of the catabolism of lysine and/or arginine). The identification of these genes allows biotechnological production methods to be developed that are improved to the extent that, to assist these nucleic acids, the formation of the odorous substances synthesized via these metabolic pathways can be reduced by deactivating the corresponding genes in the micro-organism used for the biotechnological production. In addition, these gene products are thus available for preparing reactions or for methods according to their respective biochemical properties.

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Proteases encompassing an amino acid sequence that is at least 70% identical to the amino acid sequence indicated in SEQ ID NO. 1 over its entire length, and exhibit the amino acid substitution I21V in the count in accordance with SEQ ID NO. 1, agents that encompass such proteases, display very good cleaning performance on protease-sensitive stains.

Performance-enhanced protease variant

The present invention relates to &#x3b1;-amylase variants that are stabilized to dimerization and/or multimerization, in particular at elevated temperatures or high pH, by point mutagenesis of positively polarized or charged or neutral surface amino acids to give more negatively polarized or charged amino acids. The invention further relates to methods of increasing the stability of an &#x3b1;-amylase to dimerization and/or multimerization brought about by electrostatic interactions whereby at least one amino acid residue on the surface of the starting molecule, which makes a neutral or positively polar or charged contribution to the electrostatic potential of said molecule, is replaced with a more negatively polar or negatively charged amino acid residue. The &#x3b1;-amylase variants obtained thereby exhibit better stability to influences of the solvent, increased processivity, and are suited for numerous industrial areas of use, in particular as active ingredients in detergents and cleansers.

Alpha-amylase variants stabilized against dimerization and/or multimerization, method for the production thereof, and detergents and cleansers containing these alpha-amylase variants

Proteases encompassing an amino acid sequence, which are at least 70% identical to the amino acid sequence specified in SEQ ID NO. 1 over the entire length thereof and which, in the listing according to SEQ ID NO. 1, have the amino acid substitution I21V in combination with at least one further amino acid substitution, the further amino acid substitution being selected from the group consisting of Q12L, M122L, N177V, A222S, V228I and T247N, and agents encompassing such proteases, exhibit very good cleaning performance on egg-containing stains.

Performance-enhanced protease variants

Phosphonate-containing liquid washing or cleaning agent exhibiting advantageous proteolytic activity and improved storage stability comprising a protease having an amino acid sequence which is at least 80% identical to the amino acid sequence stated in SEQ ID NO. 1 and which comprises in position 99 in the numbering according to SEQ ID NO. 1 the amino acid glutamic acid (E) or aspartic acid (D) or the amino acid asparagine (N) or glutamine (Q) or the amino acid alanine (A) or glycine (G) or serine (S).

Storage-stable liquid washing or cleaning agent containing proteases

A hydrolytic enzyme is stabilized in a liquid surfactant preparation using a component that stabilizes the hydrolytic enzyme and encompasses an oligoaminobiphenyl oligocarboxylic acid.

Stabilized liquid tenside preparation comprising enzymes

A hydrolytic enzyme is stabilized in a liquid surfactant preparation using a component that stabilizes the hydrolytic enzyme and includes a phenylalkyldicarboxylic acid.

A hydrolytic enzyme is to be stabilized in a liquid surfactant preparation. This is achieved by using a component that stabilizes the hydrolytic enzyme and encompasses a multiply substituted benzenecarboxylic acid that has a carboxyl group on at least two carbon atoms of the benzene residue.

Stabilized liquid tenside preparation comprising enzymes and benzenecarboxylic acid

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Erkrath, Germany

Karl-Heinz Maurer