Henkel Ag & Company, Kgaa

Henkel Kommanditgesellschaft Auf Aktien

Basf Se Corporation

Inken Prueser

Nina Mussmann

Susanne Wieland

Christian Degering

Daniela Herbst

Sabine Griemert

Timothy O'Connell

Thorsten Eggert

Layla Fernandez

Christian Leggewie

Daria Strauss

Karl-Heinz Maurer

Beatrix Kottwitz

Guenter Uphues

Albrecht Weiss

Thorsten Bastigkeit

Thomas Eiting

Ulrich Pegelow

Petra Siegert

Marc-Steffen Schiedel

Konstantin Benda

Regina Stehr

Sven Mueller

Astrid Spitz

Laura Polanyi-Bald

Brian Laufs

Ayhan Aydemir

Dorota Sendor-Mueller

Marita Grothus

Renée Charlott Eichstaedt

Barbara Peiffer

Michael Puls

Thomas Weber

Proteases may include an amino acid sequence having at least 70% sequence identity with the amino acid sequence given in SEQ ID NO:1 over its entire length. The proteases may further have, in each case based on the numbering according to SEQ ID NO:1, amino acid substitutions 9T, 130D/V, 133A, 144K, 217M, 252T and 271E at the positions corresponding to positions 9, 130, 133, 144, 217, 252 and 271. The proteases may further include at least one further amino acid substitution at at least one of the positions corresponding to positions 6, 89, 131, 166, 189, 211 or 224, and to the production and use thereof. Such proteases exhibit very good stability with good cleaning performance.

Stability-enhanced protease variants VI

Proteases may include an amino acid sequence having at least 70% sequence identity with the amino acid sequence given in SEQ ID NO: 1 over its entire length and, in each case based on the numbering according to SEQ ID NO: 1, may include (i) amino acid substitutions, such as selected from amino acid substitutions 9T, 144K, 252T and 271E, at positions corresponding to positions 9, 144, 252 and 271, and (ii) at least one additional amino acid substitution at least at one of the positions corresponding to positions 53, 120, 131, 149, 159, 162, 166, 172, 189, 192, 211, 215, 217, 224 and 274. Production and use of said proteases are described herein. Proteases of this kind demonstrate very good stability with a good cleaning performance.

Proteases having improved enzyme stability in washing and cleaning agents III

Proteases may include an amino acid sequence which has at least 70% sequence identity with the amino acid sequence given in SEQ ID NO:1 over its entire length and has (i) one or more first amino acid substitutions at positions corresponding to positions 3, 4, 99, 199, or combinations thereof, and (ii) one or more second amino acid substitutions at positions corresponding to positions 9, 21, 42, 44, 105, 112, 113, 131, 137, 139, 141, 145, 159, 168, 176, 177, 182, 193, 198, 204, 205, 206, 210, 212, 230, 234, 250, 253, 255, 259, 267, or combinations thereof based on the numbering according to SEQ ID NO:1, and relates to the preparation and use thereof. Proteases of this kind demonstrate very good stability with good cleaning performance.

Performance-enhanced and storage stable protease variants

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

Proteases may include an amino acid sequence which has at least 70% sequence identity with the amino acid sequence given in SEQ ID NO:1 over its entire length and has, based on the numbering according to SEQ ID NO:1, (i) two or more first amino acid substitutions at positions corresponding to positions 3, 4, 99, 199, or combinations thereof; and (ii) one or more second amino acid substitutions at positions corresponding to positions 74, 136, 143, 154, 161, 163, 171, 200, 203, 209, 212, 256, or combinations thereof. Proteases of this kind demonstrate very good stability with good cleaning performance.

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 N130D on the position corresponding to the position 30 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 101, 133, 144, 224, 252 or 271, 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 III

The present disclosure relates to proteases comprising an amino acid sequence which has at least about 70% sequence identity to the amino acid sequence indicated in SEQ ID NO. 1, over the entire length thereof, and in which the amino acids in the positions corresponding to positions 24, 33, 53, 78, 101, 128 and 217 according to SEQ ID NO. 1 are substituted at 24G, 33T, 53G, 78N, 101N, 128A and 217Q, and to the production and use thereof. Said type of proteases have a very good cleaning performance compared to reference proteases.

Protease with improved washing performance

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.

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

The invention relates to novel perhydrolases, derived from the protease Carlsberg by amino acid exchange in positions 11, 15, 21, 38, 50, 54, 58, 77, 83, 89, 93, 96, 107, 117, 120, 134, 135, 136, 140, 147, 150, 154, 155, 160, 161, 171, 179, 180, 181, 194, 205, 208, 213, 216, 217, 238, 239, 251, 253, 257, and/or 261. The invention further relates to methods for production of said novel perhydrolases, products comprising said novel perhydrolases, particularly bodycare, haircare, shampoo, hair-dyeing, hair-bleaching, oral-care, dental-dare, dental-prosthesis-care, cosmetic, therapeutic (textile) washing, cleaning, rinsing, handwash, washing-up and dish-washing products, and corresponding applications of said novel perhydrolases.

Subtilisin variants with improved perhydrolase activity

A detergent or disinfectant composition comprising is presented having 0.5 to 10 percent by weight of an activator compound which under perhydrolysis conditions forms a percarboxylic acid, and releases a leaving group capable of being used as a substrate for enzymes, and up to 50 percent by weight of a peroxygen compound. The composition increases the oxidation of peroxide compounds in oxidation, bleaching, detergent, cleaning and disinfecting solutions, especially at low temperatures.

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Duesseldorf, Germany

Inken Prueser