Surface Studies of Lytic Polysaccharide Monooxygenase Action on Polysaccharides
Lytic polysaccharide monooxygenases are enzymes which were discovered in 2010/11 have been heralded as a breakthrough in biomass degradation and in the future of sustainable biofuels. The enzymes work by oxidising the polysaccharide chains in what otherwise would be highly recalcitrant materials (e.g. cellulose, chitin) and, as such, make the substrate susceptible to further degradation by normal enzymatic or chemical methods. The mode of action of LPMOs is poorly understood, in particular the need for LPMOs to act in concert with other proteins, many of which are simple electron-transfer proteins. It is possible that these electron-transfer proteins form "super-complexes" with LPMOs on the surface of polysaccharide substrates. We aim to use neutron reflectometry to establish the nature of this super-complex interaction. Dynamic measurements of deuterated LMPOs (supplied as discussed by the D-Lab) both with and without hydrogenous electronic transfer proteins will be carried out by exploiting the high flux of FIGARO in combination with isotopic contrast variation. The structure of the binding combined with the kinetics of film breakup will be resolved.
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Paul H Walton; Richard A. Campbell; CIANO Luisa; FORSYTH Victor Trevor; FRAGNETO Giovanna; HAERTLEIN Michael and Esther M. Johnston. (2015). Surface Studies of Lytic Polysaccharide Monooxygenase Action on Polysaccharides. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.8-02-741
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