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The xylan-binding module  Clostridium thermocellum  CBM22A was successfully fused to a gluco-oligosaccharide oxidase, GOOX-VN, from  Sarocladium strictum  via a short TP linker, allowing the fused protein to effectively bind different xylans. The presence of the  Ct CBM22A at the N-terminal of GOOX-VN increased catalytic activity on mono- and oligo-saccharides by 2-3 fold while not affecting binding affinity to these substrates. Notably, both GOOX-VN and its CBM fusion also showed oxidation of xylo-oligosaccharides with degrees of polymerization greater than six. Whereas fusion to  Ct CBM22A did not alter the thermostability of GOOX-VN or reduce substrate inhibition,  Ct CBM22A_GOOX-VN could be immobilized to insoluble oat spelt xylan while retaining wild-type activity. QCM-D analysis showed that the fused enzyme remained bound during oxidation. These features could be harnessed to generate hemicellulose-based biosensors that detect and quantify the presence of different oligosaccharides.

Fusion of a Xylan-Binding Module to Gluco-Oligosaccharide Oxidase Increases Activity and Promotes Stable Immobilization