1.1.99.B3	A38V	the mutation significantly increases the kcat and catalytic efficiency of the enzyme on oligosaccharides compared to the wild type enzyme	-, 740204	
1.1.99.B3	A38V/S388N	the mutation increases the kcat and catalytic efficiency of the enzyme on oligosaccharides compared to the wild type enzyme	740204	
1.1.99.B3	C130A	FAD binding site, FAD covalently attached	698829	
1.1.99.B3	E247A	the mutation decreases the kcat and catalytic efficiency of the enzyme on oligosaccharides compared to the wild type enzyme	-, 740204	
1.1.99.B3	H70A	FAD binding site, FAD covalently attached	698829	
1.1.99.B3	H70A/C130A	no activity, lack of essential FAD cofactor	698829	
1.1.99.B3	Q353A	the mutation decreases the kcat and catalytic efficiency of the enzyme on oligosaccharides compared to the wild type enzyme	740204	
1.1.99.B3	Q353N	the mutation decreases the kcat and catalytic efficiency of the enzyme on oligosaccharides compared to the wild type enzyme	740204	
1.1.99.B3	Q384A	the mutation decreases the kcat and catalytic efficiency of the enzyme on oligosaccharides compared to the wild type enzyme	-, 740204	
1.1.99.B3	Q384N	the mutation decreases the kcat and catalytic efficiency of the enzyme on oligosaccharides compared to the wild type enzyme	740204	
1.1.99.B3	W351A	the mutation decreases the kcat and catalytic efficiency of the enzyme on oligosaccharides compared to the wild type enzyme	740204	
1.1.99.B3	W351A	the mutation increases Km values by up to 2 orders of magnitude while also increasing kcat up to 3fold on cello- and xylo-oligosaccharides and showing no substrate inhibition compared to the wild type enzyme	740204	
1.1.99.B3	W351F	the mutant shows reduced kcat values for monosaccharide and oligosaccharide substrates	-, 724616	
1.1.99.B3	Y300A	the mutant variant of gluco-oligosaccharide oxidase (GOOX) from Sarocladium strictum shows a broader substrate range and higher H2O2 stability compared to the wild-type enzyme. The mutant Y300A exhibits up to 40times higher activity on all tested sugars except glucose, compared to wild-type. Fusion of the Y300A variant to a family 22 carbohydrate binding module from Clostridium thermocellum (CtCBM22A) nearly doubles its catalytic efficiency on glucose, while retaining significant activity on oligosaccharides. In the presence of 200 mM of H2O2, the recombinant CtCBM22A_Y300A retains 80% of activity on glucose and 100% of activity on cellobiose, the preferred substrate for this enzyme, while the wild-type enzyme retains 60% activity on D-glucose under the same conditions. GOOX variants appear to undergo a different mechanism of inactivation, as a loss of histidine instead of methionine is observed after H2O2 incubation. The addition of CtCBM22A also promotes functional binding of the fusion enzyme to xylan, facilitating its simultaneous purification and immobilization using edible oat spelt xylan, which might benefit the usage of this enzyme preparation in food and baking applications. The presence of CtCBM22A also permits enzyme binding to oat spelt xylans, facilitating simultaneous purification and immobilization of the enzyme, and ancillary fibre enrichment in potential food applications	743824	
1.1.99.B3	Y300A	the mutation doubles kcat values for monosaccharide and oligosaccharide substrates	-, 724616	
1.1.99.B3	Y300A	the variant shows broader substrate range and higher H2O2 stability and specifically exhibits up to 40times higher activity on all tested sugars except D-glucose compared to the wild type enzyme	741429	
1.1.99.B3	Y300N	the mutation doubles kcat values for monosaccharide and oligosaccharide substrates	-, 724616	
1.1.99.B3	Y310A	larger amount of carbohydrates	698829	
1.1.99.B3	Y72A	the mutation decreases the kcat and catalytic efficiency of the enzyme on oligosaccharides compared to the wild type enzyme	-, 740204	
1.1.99.B3	Y72F	the mutation decreases the kcat and catalytic efficiency of the enzyme on oligosaccharides compared to the wild type enzyme	-, 740204