Abstract: The present invention relates to a method for improving the properties of a cellulolytic enzyme by amino acid substitution, deletion or insertion, the method comprising the steps of: a. constructing a multiple alignment of at least two amino acid sequences known to have three-dimensional structures similar to endoglucanase V (EGV) from Humicola insolens known from Protein Data Bank entry 4ENG; b. constructing a homology-built three-dimensional structure of the cellulolytic enzyme based on the structure of the EGV; c. identifying amino acid residue positions present in a distance from the substrate binding cleft of not more than 5 ?; d. identifying surface-exposed amino acid residues of the enzyme; e. identifying all charged or potentially charged amino acid residue positions of the enzyme; f. choosing one or more positions wherein the amino acid residue is to be substituted, deleted or where an insertion is to be provided; and g.

Abstract: The present invention relates to novel subtilase variants exhibiting alterations relative to the parent subtilase in one or more properties including: Wash performance, thermal stability, storage stability or catalytic activity. The variants of the invention are suitable for use in e.g. cleaning or detergent compositions, such as laundry detergent compositions and dishwash compositions, including automatic dishwash compositions.

Abstract: The present invention relates to variants (mutants) of parent Termamyl-like alpha-amylases, which variant has alpha-amylase activity and exhibits altered properties relative to the parent alpha-amylase.

Abstract: The present invention relates to enzymes produced by mutating the genes for a number of subtilases and expressing the mutated genes in suitable hosts are presented. The enzymes exhibit improved stability and/or improved wash performance in any detergent in comparison to their wild type parent enzymes. The enzymes are well-suited for use in any detergent and for some in especially liquid or solid shaped detergent compositions.

Abstract: The present invention relates to enzymes produced by mutating the genes for a number of subtilases and expressing the mutated genes in suitable hosts are presented. The enzymes exhibit improved stability and/or improved wash performance in any detergent in comparison to their wild type parent enzymes. The enzymes are well-suited for use in any detergent and for some in especially liquid or solid shaped detergent compositions.

Abstract: The present invention relates to polypeptide-polymer conjugates having added and/or removed one or more attachment groups for coupling polymeric molecules on the surface of the polypeptide structure, a method for preparing polypeptide-polymer conjugates of the invention, the use of said conjugates for reducing the immunogenicity and allergenicity and compositions comprising said conjugate.

Abstract: Described is a method for improving the properties of a cellulolytic enzyme by amino acid substitution, deletion or insertion, the method comprising the steps of:

Abstract: The present invention relates to polypeptides with reduced immune response including reduced allergenicity having one or more amino acid residues being substituted with other amino acid residues and/or having coupled one or more polymeric molecules in the vicinity of the polypeptides metal binding site, a method for preparing modified polypeptides of the invention, the use of the polypeptide for reducing the immunogenicity and allergenicity and compositions comprising the polypeptide.

Abstract: The present invention relates to polypeptides with reduced immune response including reduced allergenicity having one or more amino acid residues being substituted with other amino acid residues and/or having coupled one or more polymeric molecules in the vicinity of the polypeptides metal binding site, a method for preparing modified polypeptides of the invention, the use of the polypeptide for reducing the immunogenicity and allergenicity and compositions comprising the polypeptide.

Abstract: The present invention relates to enzymes produced by mutating the genes for a number of subtilases and expressing the mutated genes in suitable hosts are presented. The enzymes exhibit improved autoproteolytic stability in comparison to their wild type parent enzymes.

Abstract: The present invention relates to enzymes produced by mutating the genes for a number of subtilases and expressing the mutated genes in suitable hosts are presented. The enzymes exhibit improved autoproteolytic stability in comparison to their wild type parent enzymes.

Abstract: The present invention relates to polypeptide-polymer conjugates having added and/or removed one or more attachment groups for coupling polymeric molecules on the surface of the polypeptide structure, a method for preparing polypeptide-polymer conjugates of the invention, the use of said conjugated for reducing the immunogenicity and allergenicity and compositions comprising said conjugate.

Abstract: The present invention relates to enzymes produced by mutating the genes for a number of subtilases and expressing the mutated genes in suitable hosts are presented. The enzymes exhibit improved stability and/or improved wash performance in any detergent in comparison to their wild type parent enzymes. The enzymes are well-suited for use in any detergent and for some in especially liquid or solid shaped detergent compositions.

Abstract: The present invention relates to variants of a Family 7 cellulase comprising one or more mutations of the amino acid sequence of the cellulase in which each mutation is independently a substitution of an amino acid residue with another amino acid or an insertion of at least one amino acid residues, wherein the variant has a modified H-bonding potential and hydrophobic interaction relative to the cellulase. The present invention also relates to the use of the cellulase variants in detergent compositions, especially for soil removal or color clarification or preventing backstaining; in fabric softeners; for bio-polishing of textiles; for drainage improvement of paper pulp; for deinking of old paper; for plant degradation.

Abstract: Cellulose-containing fabric is desized by treating with an enzyme hybrid having a catalytically active amino acid sequence of an enzyme such as a lipase or an amylase linked to an amino acid sequence containing a cellulose-binding domain. The enzyme amino acid sequence may be of an .alpha.-amylase obtainable from a species of Bacillus such as Bacillus licheniformis, or of a lipase obtainable from a species of Humicola, Candida, Pseudomonas or Bacillus. The cellulose-binding domain may be from a cellulase, a xylanase, a mannanase, an arabinofuranosidase, an acetylesterase or a chitinase. The enzyme hybrid is obtained from a transformed host cell containing an expression cassette having a DNA sequence encoding the enzyme hybrid. A desizing composition is formed containing the enzyme hybrid and a wetting agent.

Abstract: The present invention relates to a process for removal or bleaching of soiling or stains present on cellulosic fabric, wherein the fabric is contacted in aqueous medium with a modified enzyme (enzyme hybrid) which comprises a catalytically active amino acid sequence of a non-cellulolytic enzyme linked to an amino acid sequence comprising a cellulose-binding domain. The invention further relates to a detergent composition comprising an enzyme hybrid of the type in question and a surfactant, and to a process for washing soiled or stained cellulosic fabric, wherein the fabric is washed in an aqueous medium to which is added such a detergent composition.

Abstract: The present invention relates to variants of cyclomaltodextrin glucanotransferase. More specifically the invention relates to a method of modifying the substrate binding and/or product selectivity of a precursor CGTase enzyme, and CGTase variants derived from a precursor CGTase enzyme by substitution, insertion and/or deletion of one or more amino acid residue(s), which amino acid residue(s) holds a position close to the substrate. Moreover, the invention relates to DNA constructs encoding the CGTase variants, expression vectors, host cells and methods of producing the CGTase variants of the invention.

Abstract: This invention relates to novel stabilized enzymes. More specifically the invention relates to novel stabilized enzymes, in which a naturally occurring amino acid residue (other than proline) has been substituted with a proline residue at one or more positions; at which position(s) the dihedral angles .phi. (phi) constitute values within the interval ?-90.degree.<.phi.<-40.degree.!; preferably the dihedral angles .phi. (phi) and .psi. (psi) constitute values within the intervals ?-90.degree.<.psi.<-40.degree.! and ?-180.degree.<.psi.<-150.degree. or -80<$g c)<10 or 100<.psi.<180!; and which positions(s) is/are not located in regions in which the enzyme is characterized by possessing .alpha.-helical or .beta.-sheet structure. The invention also relates to nucleotide sequences encoding the novel stabilized enzymes, and expression vectors and host organisms containing the nucleotide sequences. This invention also relates to detergent compositions comprising the stabilized enzymes.

Abstract: The present invention relates to cellulases derived from the strain Myceliophthora thermophila and variants thereof comprising a core and optionally a C-terminal link consisting of 10 amino acids at the most, especially cellulases having a substrate binding cleft of a depth of at least 12 .ANG., exhibit enhanced enzyme activity in the alkaline pH range while exerting a moderate cellulolytic action on the cellulosic substrate and are, for example, useful in detergent compositions, especially for soil removal or color clarification or preventing backstaining; in fabric softeners; for bio-polishing of textiles; for drainage improvement of paper pulp; for deinking of old paper; for plant degradation.

Abstract: The invention relates to stabilized subtilisin proteases wherein one or more prolines is substituted for a native amino acid at stabilizing positions defined both by the range of the dihedral angles in the primary structure present at the substitution site and by selected characteristics of the protease secondary structure in the vicinity of the substitution site, to nucleotide sequences that encode the stabilized proteases, and to host organisms that contain the nucleotide sequences encoding the stabilized proteases.