Abstract: The present invention provides methods and compositions for the production of stabilized proteins. In particular, the present invention provides methods and compositions for the generation of combinatorial libraries of consensus mutations and screening for improved protein variants.

Abstract: The present application relates to peptides which bind to a target stain, phenol oxidizing enzyme-binding peptide complexes wherein the binding peptide is attached to the C-terminus of the phenol oxidizing enzyme or is inserted or substituted into the phenol oxidizing enzyme. In a preferred embodiment the phenol oxidizing enzyme is a laccase specifically Stachybotrys oxidase B and variants thereof. The invention provides expression vectors comprising the phenol oxidizing enzyme-binding peptide complex as well as host cells comprising the vectors.

Abstract: The present application relates to peptides which bind to a target stain, phenol oxidizing enzyme-binding peptide complexes wherein the binding peptide is attached to the C-terminus of the phenol oxidizing enzyme or is inserted or substituted into the phenol oxidizing enzyme. In a preferred embodiment the phenol oxidizing enzyme is a laccase specifically Stachybotrys oxidase B and variants thereof. The invention provides expression vectors comprising the phenol oxidizing enzyme-binding peptide complex as well as host cells comprising the vectors.

Abstract: The invention relates to the production by recombinant technology of enzymes having desired activity. The invention provides methods employing display vehicle technology allowing to select enzymes having desired catalytic activity. The invention provides a method for selecting an enzyme mutant with desired catalytic activity comprising displaying each of a multitude of mutants of said enzyme on the surface of a display vehicle comprising a nucleic acid encoding said mutant and selecting for a display vehicle carrying nucleic acid encoding an enzyme mutant having at least a site other than its catalytic site mutated.

Abstract: The present invention relates to novel amylolytic enzymes having improved characteristics for the use in starch degradation, in textile or paper desizing and in household detergent compositions. The disclosed &agr;-amylases show surprisingly improved properties with respect to the activity level and the combination of thermostability and a higher activity level. These improved properties make them more suitable for the use under more acidic or more alkaline conditions. The improved properties allow also the reduction of the Calcium concentration under application conditions without a loss of performance of the enzyme.

Abstract: The present invention provides detergent compositions comprising variants of precursor phenol oxidizing enzymes, said precursor being derived from a Stachybotrys species. The precursor enzymes can be, for example, naturally-occurring or recombinant phenol oxidizing enzymes. The variant enzymes, in general, are obtained by modification of a precursor DNA sequence encoding the naturally-occurring or recombinant phenol oxidizing enzyme to generate the substitution of one or more amino acids in the encoded amino acid sequence. Variant enzymes are disclosed having properties which differ from those of their respective precursor enzymes, e.g., altered pH optima and/or phenol oxidizing activity and/or altered stability. The variant enzymes of the present invention are especially useful in detergent formulations, for example, to modify (bleach) the color associated with colored compounds.

Abstract: A method is provided for producing a coated article comprising: (a) preparing a solution of lignin; (b) mixing the lignin solution with a phenol oxidizing enzyme; (c) incubating the mixture from said step (b) under conditions and for a time sufficient to form a solution of a desired viscosity; (d) contacting or spreading the mixture from the step (c) on an article to be coated; and (e) allowing the coating to set onto the article by subjecting the article to conditions and for a time sufficient to form a coating on the surface of the article.

Abstract: A method is provided for producing a painted article comprising: (a) preparing a lignin solution comprising lignin and a dye or pigment; (b) mixing the lignin solution with a phenol oxidizing enzyme; (c) incubating the mixture from said step (b) under conditions and for a time sufficient to form a solution of a desired viscosity; (d) contacting or spreading the mixture from the step (c) on an article to be painted; and (e) allowing the mixture to set onto the article by subjecting the article to conditions and for a time sufficient to form a paint on the surface of the article.

Abstract: The present invention provides mutant lipases which retain lipase activity, but have improved surfactant resistance and are thus highly advantageous for use in detergent compositions. Preferred lipases of this type include modified functional forms of a lipase of Pseudomonas alcaligenes having one or more amino acid substitutions at or near the surface of the lipase which effect interaction of the hydrophobic portions of surfactant molecules with initiation sites on the enzyme for surfactant denaturation.

Abstract: Enzymes stabilized against the destabilizing effect of ionic surfactants and a method of producing such stabilized enzymes in which DNA sequences which code for the enzymes are modified by directed mutation in defined positions which correlate with defined surface regions of the enzyme, in such a way that the codon in which the mutation is located now codes for an amino acid differing from the original amino acid.

Abstract: Novel, optimized highly alkaline proteases which are suitable for use in detergent formulations are prepared by employing microorganisms transformed by mutated DNA sequences. The mutated sequences are obtained starting from DNA sequences which code for highly alkaline protease usually produced by Bacillus species by altering these DNA sequences in defined positions by directed mutagenesis (point mutation) in such a way that the codon in which the point mutation is located now codes for an amino acid which is more strongly basic than the original amino acid. The result is highly alkaline proteases in which original amino acids have been replaced by more strongly basic amino acids, preferably by the amino acids lysine or arginine. Synthetic oligonucleotides, DNA sequences, vectors and transformed microorganisms which are used for generating and obtaining the optimized highly alkaline protease are also described.