Abstract: Proteases that comprise an amino acid sequence that is at least 95% identical to the amino acid sequence indicated in SEQ ID NO. 1 over its entire length and that comprise, in the count in accordance with SEQ ID NO. 1, the amino acid substitution R99D or R99E in combination with the further amino acid substitutions of S3T, V4I, and V199I, display very good cleaning performance in particular on blood-containing stains, as well as very good temperature stability.

Abstract: Proteases that comprise 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 that comprise, in the count in accordance with SEQ ID NO. 1, the amino acid substitution R99D in combination with at least two further amino acid substitutions that are selected from the group consisting of S3T, V4I, and V199I, display very good cleaning performance in particular on blood-containing stains, as well as very good temperature stability.

Abstract: 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.

Abstract: Proteases that comprise 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 that comprise, in the count in accordance with SEQ ID NO. 1, the amino acid substitution R99D in combination with at least two further amino acid substitutions that are selected from the group consisting of S3T, V4I, and V199I, display very good cleaning performance in particular on blood-containing stains, as well as very good temperature stability.

Abstract: 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.

Abstract: The invention relates to peroxidases having activity for carotenoids and comprising an amino acid sequence that has at least 70% sequence identity to the amino acid sequence specified in SEQ ID NO:1 across its entire length, washing and cleaning agents that contain such peroxidases and the use thereof.

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

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

Abstract: Proteases that comprise 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 that comprise, in the count in accordance with SEQ ID NO. 1, the amino acid substitution R99E or R99D in combination with at least two further amino acid substitutions that are selected from the group consisting of S3T, V4I, and V199I, display very good cleaning performance in particular on blood-containing stains, as well as very good temperature stability.

Abstract: 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.

Abstract: 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.

Abstract: 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 phthaloylglutamic acid and/or a phthaloylaspartic acid.

Abstract: A hydrolytic enzyme is stabilized in a liquid surfactant preparation by using a component that stabilizes the hydrolytic enzyme and includes a monosaccharide glycerate.

Abstract: 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.

Abstract: A novel subtilisin-type alkaline protease from Bacillus gibsonii and to sufficiently related proteins and the derivatives thereof. Also, washing and cleaning agents comprising the novel subtilisin-type alkaline protease, sufficiently related proteins and the derivatives thereof, corresponding washing and cleaning methods and their use in washing and cleaning agents, and other possible technical uses.

Abstract: A novel subtilisin-type alkaline protease from Bacillus pumilus and sufficiently related proteins and derivatives thereof. Also washing and cleaning agents comprising the novel subtilisin-type alkaline protease, sufficiently related proteins and derivatives thereof, corresponding washing and cleaning methods, and washing and cleaning agents and other possible technical uses.