Modified xylanases exhibiting improved expression

A modified Family (11) xylanase enzyme comprising a sequence that introduces a functional consensus glycosylation site is provided. Non-limiting examples o f introduced glycosylation sites include mutation of the amino acid at positio n (34, 131, 180, 182), or a combination thereof, to an asparagine...

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Bibliographische Detailangaben
1. Verfasser:	WHITE THERESA,GIROUX GENEVIEVE R.,WALLACE KATIE E. A
Format:	Patent
Sprache:	eng
Schlagworte:	BAKERY PRODUCTS BAKING BEER BIOCHEMISTRY CHEMISTRY COMPOSITIONS THEREOF CULTURE MEDIA EDIBLE DOUGHS ENZYMOLOGY FODDER FOODS OR FOODSTUFFS FOODS, FOODSTUFFS, OR NON-ALCOHOLIC BEVERAGES, NOT COVERED BYSUBCLASSES A23B - A23J HUMAN NECESSITIES IMPREGNATING OR COATING OF PAPER METALLURGY MICROBIOLOGY MICROORGANISMS OR ENZYMES MUTATION OR GENETIC ENGINEERING PAPER NOT OTHERWISE PROVIDED FOR PAPER-MAKING PREPARATION THEREOF NOT COVERED BY SUBCLASSES D21C OR D21D PRESERVATION OF FOODS OR FOODSTUFFS, IN GENERAL PRESERVATION THEREOF PRODUCTION OF CELLULOSE PROPAGATING, PRESERVING OR MAINTAINING MICROORGANISMS PULP COMPOSITIONS SPIRITS TEXTILES THEIR PREPARATION OR TREATMENT, e.g. COOKING, MODIFICATION OFNUTRITIVE QUALITIES, PHYSICAL TREATMENT THEIR TREATMENT, NOT COVERED BY OTHER CLASSES TREATMENT OF FINISHED PAPER NOT COVERED BY CLASS B31 OR SUBCLASS D21G TREATMENT, e.g. PRESERVATION, OF FLOUR OR DOUGH, e.g. BYADDITION OF MATERIALS VINEGAR WINE
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Beschreibung
Zusammenfassung:	A modified Family (11) xylanase enzyme comprising a sequence that introduces a functional consensus glycosylation site is provided. Non-limiting examples o f introduced glycosylation sites include mutation of the amino acid at positio n (34, 131, 180, 182), or a combination thereof, to an asparagine. The indicat ed amino acid position in the Family (11) xylanase is determined from sequence alignment of the xylanase of interest with that of a Trichoderma reesei xylanase II amino acid sequence. The introduced consensus glycosylation site facilitates increased expression efficiency of the modified xylanase when compared to the expression efficiency of a corresponding xylanase from which the modified xylanase was derived, using similar host strains and growth conditions.