Abstract: A phytase chimera, a nucleic acid having a nucleic acid sequence encoding such a phytase chimera, a vector having such a nucleic acid, a host cell having such a nucleic acid or such a vector, and the use of such a phytase chimera in food and animal feed production.

Abstract: The object of the present invention is a method for the production of block polymers comprising a firstand a second block comprising the method steps: A) providing a first block having a nucleophilic peptide sequence for afirst transpeptidase enzyme, B) providing a second block having a peptide recognition sequence for the first transpeptidase enzyme, C) linking the first block to the second block by means of the first transpeptidase enzyme, wherein the first and second blocks are independently selected from nanoparticles, non-peptide polymers, and recombinant proteins. Such a production method makes it possible to build block polymers from identical or different blocks in a particularly simple and controlled manner.

Abstract: The invention relates to a plant protection and/or plant growth promotion system, comprising at least one anchor peptide for increased binding to a plant part, a support function, which is indirectly or directly bound to the anchor peptide, and an active substance for protecting the plant and/or promoting plant growth and yield.

Abstract: The invention relates to novel variants of fungal endoglucanases. The invention further relates to enzyme preparations and detergent compositions comprising the variant as well as to processes for treating cellulosic material with the variant. The variants have depilling, antipilling and/or antigreying performance, and improved stability in the presence of proteases.

Abstract: An agent, such as a detergent or cleaning agent, may include a polyesterase, as defined herein. A method for cleaning textiles may include applying the agent to a textile for removing soiling. The polyesterase may also help to reduce pilling effects in the agent.

Abstract: An agent, such as a detergent or cleaning agent, may include a polyesterase. A method for cleaning textiles may include applying the agent to a textile for removing soiling. The polyesterase may also help to reduce pilling effects in the agent.

Abstract: The present invention pertains to a novel fusion protein and/or fusion peptide, preferably for use in the separation from and/or detection in an environment of one or more target polymers or plastics, e.g., one or more target polymer fragments and/M or particles or target plastic fragments and/or particles, preferably wherein the one or more target polymer particles or target plastic particles are microplastics; a method of preparing such novel fusion protein and/or fusion peptide, a system and kit comprising the novel fusion protein and/or fusion peptide and a (polymer or non-polymer) carrier or carrier system, a use of the novel fusion protein and/or fusion peptide or of a system and kit as mentioned in the separation from and/or detection in an environment of one or more target polymers or plastics, e.g.

Abstract: The invention is used in the field of enzyme technology. The invention relates to lipases and to the production thereof, the amino acid sequence of which has been modified in particular with regard to the use thereof in detergents and cleaning agents, all sufficiently similar lipases having a corresponding modification and nucleic acids coding for them. The invention further relates to methods and uses of said lipases and to agents containing them, in particular detergents and cleaning agents.

Abstract: The present invention relates to a hydantoinase having an amino acid sequence selected from (i) or (ii), with (i) amino acid sequence selected from SEQ ID NO: 6-20 and SEQ ID NO: 73-119 (ii) amino acid sequence wherein in the amino acid sequence of SEQ ID NO: 6-20 and SEQ ID NO: 73-119, 1 to 75 amino acid residues have been substituted, deleted, inserted and/or added, and wherein further the catalytic activity of the hydantoinase is higher by a factor of at least 1.2 than the catalytic activity of the hydantoinase having amino acid sequence SEQ ID NO: 1. The present invention further relates to a process for preparing amino acids, wherein said hydantoinase is used.

Abstract: The present invention relates to polypeptides having cellulase activity, in particular to variants derived from the 20K-cellulase enzyme. The invention discloses a number of amino acid residue positions important for the properties of the cellulase enzyme and thereby for the stability and/or performance thereof. The novel variants have improved stability compared to the parental cellulase. In particular, the novel variants have good performance in an antigreying application and excellent stability in the presence of a protease in several detergent compositions even in long-term experiments.

Abstract: The present invention relates to polypeptides having cellulase activity, in particular to variants derived from the 20K-cellulase enzyme. The invention discloses a number of amino acid residue positions important for the properties of the cellulase enzyme and thereby for the stability and/or performance thereof. The novel variants have improved stability compared to the parental cellulase. In particular, the novel variants have good performance in an antigreying application and excellent stability in the presence of a protease in several detergent compositions even in long-term experiments.

Abstract: The subject of the invention is new membranes in which tailor-made membrane transport proteins (such as e.g. TCDB classified proteins) act as pore-forming proteins (e.g. FhuA) or peptides which act as pores in the membrane. The membranes can preferably be produced both by linking synthesised protein-polymer conjugates and by direct linking of the pore-forming proteins and peptides. Such membranes are distinguished by many outstanding features which existing membranes have not been able to offer to date.

Abstract: The invention relates to lipases comprising an amino acid sequence having a sequence that is at least about 70% identical to the amino acid sequence specified in SEQ ID NO:1 over the entire length and an amino acid substitution of at least one of the positions K142, I149, S195, K204, N218, E287, P292, Q294, I302, P308, Q309, E335 or S364, corresponding to the numbering in accordance with SEQ ID NO:1. Such lipases have very good stability, particularly temperature stability, while providing good cleaning performance.

Abstract: The present invention relates to it hydantoinase having an amino acid sequence selected from (i) or (ii), with (i) amino acid sequence selected from SEQ ID NO: 6-20 and SEQ ID NO: 73-119 (ii) amino acid sequence wherein in the amino acid sequence of SEQ ID NO: 6-20 and SEQ ID NO: 73-119, 1 to 75 amino acid residues have been substituted, deleted, inserted and/or added, and wherein further the catalytic activity of the hydantoinase is higher by a factor of at least 1.2 than the catalytic activity of the hydantoinase having amino acid sequence SEQ ID NO: 1. The present invention further relates to a process for preparing amino acids, wherein said hydantoinase is used.

Abstract: The present invention relates to a hydantoinase having an amino acid sequence selected from (i) or (ii), with (i) amino acid sequence selected from SEQ ID NO: 6-20 and SEQ ID NO: 73-119 (ii) amino acid sequence wherein in the amino acid sequence of SEQ ID NO: 6-20 and SEQ ID NO: 73-119, 1 to 75 amino acid residues have been substituted, deleted, inserted and/or added, and wherein further the catalytic activity of the hydantoinase is higher by a factor of at least 1.2 than the catalytic activity of the hydantoinase having amino acid sequence SEQ ID NO: 1, The present invention further relates to a process for preparing amino acids, wherein said hydantoinase is used.

Abstract: Novel glucose oxidase (GOx) variants are disclosed that have the substitutions of T30V and I94V set forth in SEQ ID NO:1, and additionally at least one further amino acid substitution in the enzyme sequence in any of the positions S53; A137; A173; A332; F414 and V560. The GOx variants herein exhibit specificity for glucose and significantly reduced oxygen consumption rates and/or increased enzyme activity for electron mediators other than oxygen. Also provided are assay devices incorporating at least one of the GOx variants herein for improved blood glucose measurements.

Abstract: The invention relates to a plant protection and/or plant growth promotion system, comprising at least one anchor peptide for increased binding to a plant part, a support function, which is indirectly or directly bound to the anchor peptide, and an active substance for protecting the plant and/or promoting plant growth and yield.

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 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: Nucleic acids encoding cytochrome P450 variants are provided. The cytochrome P450 variants of have a higher alkane-oxidation capability, alkene-oxidation capability, and/or a higher organic-solvent resistance than the corresponding wild-type or parent cytochrome P450 enzyme. A preferred wild-type cytochrome P450 is cytochrome P450 BM-3. Preferred cytochrome P450 variants include those having an improved capability to hydroxylate alkanes and epoxidate alkenes comprising less than 8 carbons, and have amino acid substitutions corresponding to V78A, H236Q, and E252G of cytochrome P450 BM-3. Preferred cytochrome P450 variants also include those having an improved hydroxylation activity in solutions comprising co-solvents such as DMSO and THF, and have amino acid substitutions corresponding to T235A, R471A, E494K, and S1024E of cytochrome P450 BM-3.