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Fig. 3 | Biotechnology for Biofuels

Fig. 3

From: Structure of a Thermobifida fusca lytic polysaccharide monooxygenase and mutagenesis of key residues

Fig. 3

Binding and activity of T. fusca AA10A binding surface mutants. Digestion of 0.5 μM TfAA10A incubated 2 h on 5.0 mg/mL BC, with total monosaccharide release compared with WT value. Extent of binding compared to WT as fraction of 1.0 μM enzyme lost from solution after binding equilibrium established after 16 h. Binding was measured in the absence of reducing agent. Samples were measured in triplicate, with error bars representing the replicate standard deviation

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