Lipase variant

Certain variants of Lipolase (wild-type Humicolalanuginosa lipase) have a particularly good first-wash performance in a detergent solution. The variants should comprise one or more substitutions with positive amino acids near the N-terminal in the three-dimensional structure. The variants should fur...

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Bibliographische Detailangaben
Hauptverfasser:	ALLAN SVENDSEN, KIM VILBOUR ANDERSEN, JESPER VIND, SHAMKANT ANANT PATKAR, KIRSTEN BOJSEN, DORTE AABY HALKIER
Format:	Patent
Sprache:	eng
Schlagworte:	ANIMAL AND VEGETABLE OILS, FATS, FATTY SUBSTANCES AND WAXES BEER BIOCHEMISTRY CANDLES CHEMISTRY COMPOSITIONS THEREOF CULTURE MEDIA DERIVATIVES THEREOF DETERGENT COMPOSITIONS DETERGENTS ENZYMOLOGY FATTY ACIDS THEREFROM METALLURGY MICROBIOLOGY MICROORGANISMS OR ENZYMES MUTATION OR GENETIC ENGINEERING NUCLEIC ACIDS NUCLEOSIDES NUCLEOTIDES ORGANIC CHEMISTRY PROPAGATING, PRESERVING OR MAINTAINING MICROORGANISMS RECOVERY OF GLYCEROL RESIN SOAPS SOAP OR SOAP-MAKING SPIRITS SUGARS USE OF SINGLE SUBSTANCES AS DETERGENTS VINEGAR WINE
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Beschreibung
Zusammenfassung:	Certain variants of Lipolase (wild-type Humicolalanuginosa lipase) have a particularly good first-wash performance in a detergent solution. The variants should comprise one or more substitutions with positive amino acids near the N-terminal in the three-dimensional structure. The variants should further comprise a peptide addition at the C-terminal and/or should meet certain limitations on electrically charged amino acids at positions 90-101 and 210.