Entrapment of glucose oxidase (GOx) within metallic gold converts this widely used enzyme into a general saccharide oxidase. The following sugar molecules were oxidized by the entrapped enzyme (in addition to D-glucose): L-glucose, fructose, xylose,, glucose-6-phosphate, sucrose, lactose, methylglucoside, and the tri-saccharide raffinose. None of these sugars except raffinose has a natural specific oxidase. The origin of this generalization of activity is attributed to the strong protein-gold 3D interactions and to the strong interactions of co-entrapped cetyltrimethylammonium bromide (CTAB) with gold on one hand, and with the protein on the other hand. It is proposed that these interactions induce conformational changes in the channel leading to the active site, which is located at the interface between the two units of the dimeric GOx protein. The observations are compatible with affecting the specific conformation change of pulling apart and opening this gate-keeper, rendering the active site accessible to a variety of substrates. In addition to converting a common enzyme to an oxidase for common sugars which lack it, the entrapment methodology was found to be beneficial in increasing the thermal stability of GOx up to 100 oC and in allowing its convenient recyclability, two features of practical importance.