Henkel Ag & Company, Kgaa

Basf Se Corporation

Evocatal Gmbh

Evonik Degussa Gmbh

Henkel Kgaa

Thorsten Eggert

Christian Degering

Karl-Heinz Maurer

Nina Mussmann

Daniela Herbst

Inken Prueser

Sabine Griemert

Christian Leggewie

Stefan Evers

Johannes Bongaerts

Susanne Wieland

Timothy O'Connell

Daria Strauss

Thomas Haas

Harald Haeger

Werner Hummel

Andreas Karau

Harald Häger

Layla Fernandez

Andreas Schmid

Volker Sieber

Lars Mathias Blank

Peter Welters

Katrin Grammann

Andreas Michels

Bruno Buehler

Guido Jach

Andrea Weckbecker

Bruno Bühler

Katrin Schullehner

Michael Puls

Inken Prüser

Bernd Lalla

Andreas Mueller

Jennifer Andexer

André Pütz

Karl-Erich Jäger

Sascha Hausmann

Timothy O'connell

Karl-Erich JÄGER

Frank Rosenau

Andrea Seidel

Andreas MÜLLER

An amino acid sequence may have at least 70% sequence identity to the amino acid sequence identified in SEQ ID No. 1 over its entire length, and (a) an amino acid substitution on the position corresponding to the position 271, and (b1) at least one other amino acid substitution for at least one of the positions corresponding to the positions 18, 61, 92, 99, 137, 149, 156, 159, 162, 166, 172, 192, 199, 217, 265, or combinations thereof; and/or (b2) an amino acid substitution on the position corresponding to the position 9, and another amino acid substitution for at least one position corresponding to the positions 29, 48, 101, 130, 31, 133, 144, 217, 224, 252, or combinations thereof. Such proteases are useful for in washing or cleaning agents.

Performance-enhanced protease variants I

The present disclosure relates to proteases having an amino acid sequence with at least 70% sequence identity to the amino acid sequence given in SEQ ID No. 1, across its whole length, and comprising an amino acid substitution on at least one of the positions P9, Q10, Q62, L82, P86, N130, T141, N187, S236 or T253, relating in each case to the numbering according to SEQ ID No. 1. The present disclosure also relates to the production and use thereof. Said type of proteases have a very good cleaning performance.

Proteases with improved enzyme stability in detergents

An amino acid sequence may have at least 70% sequence identity to the amino acid sequence identified in SEQ ID No. 1 over its entire length, and (a) amino acid substitutions at the positions corresponding to the positions 9 and 271 in each case based on the numbering according to SEQ ID No. 1, and (b) an amino acid substitution on at least one of the positions corresponding to the positions 29, 48, 101, 30, 131, 133, 144, 224 or 252, in each case based on the numbering according to SEQ ID No. 1. Such proteases are particularly suitable for having an improved cleaning performance.

Performance-enhanced protease variants II

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 present disclosure relates to proteases having an amino acid sequence with at least about 70% sequence identity to the amino acid sequence given in SEQ ID NO:2, over the entire length thereof, and comprising an amino acid substitution at at least one of the positions P9, Q62, D101, N130, G166, N187, 5216, N238 or Q271, based in each case on the numbering according to SEQ ID NO:2. The present disclosure also relates to the production and use thereof. Such proteases exhibit very good stability, in particular storage stability, while at the same time having a good cleaning performance.

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

The present invention relates to a cell, which has been genetically modified relative to its wild type, so that in comparison with its wild type it is able to produce more &#x3c9;-aminocarboxylic acids, more &#x3c9;-aminocarboxylic acid esters or more lactams derived from &#x3c9;-aminocarboxylic acids, starting from carboxylic acids or carboxylic acid esters. Furthermore, the present invention relates to a method for the production of a genetically modified cell, the cells obtainable by this method, a method for the production of &#x3c9;-aminocarboxylic acids, of &#x3c9;-aminocarboxylic acid esters or of lactams derived from &#x3c9;-aminocarboxylic acids, the &#x3c9;-aminocarboxylic acids, &#x3c9;-aminocarboxylic acid esters or lactams derived from &#x3c9;-aminocarboxylic acids obtainable by this method, a method for the production of polyamides based on &#x3c9;-aminocarboxylic acids or based on lactams and the polyamides obtainable by this method.

&#x3c9;-Aminocarboxylic acids, &#x3c9;-aminocarboxylic acid esters, or recombinant cells which produce lactams thereof

The invention concerns a polypeptide which can be isolated from the Brassicaceae family and which has at least the activity of a hydroxynitrile lyase (HNL). The hydroxynitrile lyase of the invention is the first HNL from the Brassicaceae family. The plants () from which this enzyme or its gene is isolated is also described as non-cyanogenic. All HNL-containing plants described so far are cyanogenic plants and so it has until now been assumed that only cyanogenic plants contain hydroxynitrile lyases. Surprisingly, it transpires that a polypeptide (AtHNL) of the invention is (R)-selective. The amino acid sequence gives a theoretical molecular weight of 29.2 kDa for the AtHNL subunit. The calculated molecular mass of the protein of approximately 30 kDa can be confirmed by SDS gel electrophoresis.

Method for the synthesis of chiral cyanohydrins via a hydroxynitrile lyase from brassicaceae

The invention relates to agents containing esterases, and to the use thereof for dressing fibres, in particular, artificial fibres, washing and cleaning agents comprising esterases and corresponding washing and cleaning methods, in addition to additional technical areas of application. The invention also relates to the use of esterases for protecting against or reducing and/or preventing pilling, preferably in textiles, particularly plastic fibres, more preferably polyester fibres, in addition to the use of esterases for separating the plastics, in particular, polyester compounds. The invention further relates to novel esterases and to sufficiently related proteins and to derivatives thereof, agents containing them and to the use thereof.

Esterases for separating plastics

The present invention provides variants of fluorescent proteins, which are improved with regard to their properties for use as reporter proteins and/or in analytics. In particular, variants of fluorescent proteins are provided, which fluoresce brighter, show improved quantum yield and/or have shifted excitation or emission spectra. The fluorescent proteins according to the invention comprise in their LOV domain besides the substitution of a cysteine with an amino acid that does not covalently bind FMN at least one further point mutation.

Fluorescent proteins, their production and use

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Hattingen, Germany

Thorsten Eggert