Abstract: The present invention relates to a novel variant of peroxidase with improved stability at alkaline conditions, and a bleaching or detergent composition comprising the peroxidase variant.

Abstract: An L-amino oxidase isolated from Trichoderma harzianumi is disclosed. The enzyme exhibits activity on L-arginine, L-lysine, L-methionine, L-asparagine, L phenylalanine, and L-leucine. The pH optimium of the enzyme is alkaline.

Abstract: The present invention relates to isolated nucleic acid constructs containing a sequence encoding a Myceliophthora laccase, and the laccase proteins encoded thereby.

Abstract: This invention relates to methods of oxidizing a substrate in the presence of a laccase or a laccase related enzyme and an enhancing agent. More specifically, the invention relates to a method of bleaching of dye in solutions, to a method of inhibiting the transfer of a textile dye from a dyed fabric to another fabric when said fabrics are washed together in a wash liquor, to a method of bleaching of lignin-containing material, in particular bleaching of pulp for paper production, to a method of treatment of waste water from pulp manufacturing, and to a method of enzymatic polymerization and/or modification of lignin or lignin containing material.

Abstract: The present invention relates to isolated nucleic acid constructs containing a sequence encoding a Polyporus laccase, and the laccase proteins encoded thereby.

Abstract: The transfer of a textile dye from a dyed fabric to another fabric during washing or rinsing is inhibited by adding an enzyme exhibiting peroxidase activity or an enzyme exhibiting a suitable oxidase activity to the wash liquor in which said fabrics are washed and/or rinsed. Peroxidase is produced extracellularly by some strains of Bacillus pumilus. The novel peroxidase preparation from B. pumilus is a microperoxidase, i.e. it contains hemopeptide as an active component. The preparation has improved stability at high temperature, at high pH and at high concentrations of hydrogen peroxide. It can be produced without undesired catalase activity.

Abstract: This invention relates to activation of enzymes. More specifically, the invention relates to peroxidase enhancing agents. The invention also relates to methods of oxidizing a substrate with a source of hydrogen peroxide in the presence of a peroxidase enzyme and a peroxidase enhancing agent More specifically, the invention relates to a method of bleaching of dye in solutions, to a method of inhibiting the transfer of a textile dye from a dyed fabric to another fabric when said fabrics are washed together in a wash liquor, to a method of bleaching of lignin-containing material in particular bleaching of pulp for paper production, to a method of treatment of waste water from pulp manufacturing, and to a method of enzymatic polymerization and/or modification of lignin or lignin containing material.

Abstract: The present invention relates to isolated nucleic acid constructs containing a sequence encoding a polyporus laccase, and the laccase proteins encoded thereby.

Abstract: The transfer of a textile dye from a dyed fabric to another fabric during washing or rinsing is inhibited by adding an enzyme exhibiting peroxidase activity or an enzyme exhibiting a suitable oxidase activity to the wash liquor in which said fabrics are washed and/or rinsed. Peroxidase is produced extracellularly by some strains of Bacillus pumilus. The novel peroxidase preparation from B. pumilus is a microperoxidase, i.e. it contains hemopeptide as an active component. The preparation has improved stability at high temperature, at high pH and at high concentrations of hydrogen peroxide. It can be produced without undesired catalase activity.

Abstract: The present invention relates to isolated nucleic acid fragments containing a sequence encoding a Rhizoctonia solani laccase having optimum activity at a neutral or basic pH. and the laccase proteins encoded thereby.

Abstract: An endoprotease preparation, comprising an isolated endoprotease is disclosed. The endoprotease is a serine protease, shows immunochemical idenity to a protease derived from Fusarium oxysporum DSM 2672, hydrolyzes the oxidized beta-chain of bovine insulin at the peptide bonds Arg (22)-Gly (23) and Lys (29)-Ala(30), has optimum activity towards casein in the pH range of 8.5-11.0 with nearly constant activity in the pH range, has optimum activity at a temperature of about 45.degree. C., and has an isolectric point of about 9.0-10.0. The preferred microorganism that the enzyme is isolated from is Fusarium oxysporum DSM 2672.

Abstract: The transfer of a textile dye from a dyed fabric to another fabric during washing or rinsing is inhibited by adding an enzyme exhibiting peroxidase activity or an enzyme exhibiting a suitable oxidase activity to the wash liquor in which said fabrics are washed and/or rinsed. Peroxidase is produced extracellularly by some strains of Bacillus pumilus. The novel peroxidase preparation from B. pumilus is a microperoxidase, i.e. it contains hemopeptide as an active component. The preparation has improved stability at high temperature, at high pH and at high concentrations of hydrogen peroxide. It can be produced without undesired catalase activity.

Abstract: Combinations of alkaline Bacillus protease with alkaline fungal or actinomycete protease show improved detergency. Proteases obtainable from Fusarium sp. or Paecilomyces sp. (fungal) and Nocardiopsis sp. (actinomycete) are preferred.

Abstract: Thermal stability of microbial rennet is reduced by treatment of the rennet in aqueous medium with aliphatic or inorganic peroxy acids or salts thereof. Preferably, the microbial rennet is Mucor Miehei rennet and the peroxy acid is a lower aliphatic peroxy acid such as peracetic acid. The thermally destabilized microbial rennet is inactivated when whey containing the rennet is pasteurized.

Abstract: A stabilized solution of rennet; the stabilizing agent being methionine. The stabilizing agent is added in an amount corresponding to a concentration of between 0.1% (w/w) and saturation calculated on the total weight of the solution.

Abstract: Microbial rennet such as from Mucor miehei is thermally destabilized by treatment of the rennet in an aqueous medium with oxidizing agents containing active chlorine such as hypochlorites. The thermally destabilized rennet is advantageous for cheese making where absence of rennet activity in pasteurized whey is desired.