03-01-2013 дата публикации
Номер: US20130005637A1
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, resp. agents that encompass such proteases, display very good cleaning performance on protease-sensitive stains. 1. A protease 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 exhibits the amino acid substitution I21V in the count in accordance with SEQ ID NO. 1.2. A second protease that is obtainable from a first protease as an initial molecule by single or multiple conservative amino acid substitution , the second protease exhibiting the amino acid substitution I21V in the count in accordance with SEQ ID NO. 1 ,and/orthe second protease is obtainable from the first protease as an initial molecule by fragmentation or by deletion, insertion, or substitution mutagenesis, and encompasses an amino acid sequence that matches the initial molecule over a length of at least 50, 60, 70, 80, 90, 100, 110, 120, 130, 140, 150, 160, 170, 180, 190, 200, 210, 220, 230, 240, 250, 260, 265, 266, or 267 continuously connected amino acids, the amino acid substitution I12V contained in the initial molecule still being present,and/or{'i': 'Bacillus lentus', 'the second protease is obtainable from the first protease as an initial molecule by way of one or more amino acid substitutions in positions that are associated in an alignment with the positions 3, 4, 36, 42, 47, 56, 61, 69, 87, 96, 99, 101, 102, 104, 114, 118, 120, 130, 139, 141, 142, 154, 157, 188, 193, 199, 205, 211, 224, 229, 236, 237, 242, 243, 255, and 268 of the first protease from in accordance with SEQ ID NO. 3, such that the second protease exhibits the amino acid substitution I21V in the count in accordance with SEQ ID NO. 1.'}3. The protease according to claim 2 , wherein the ...
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