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Full-Text Articles in Chemical Engineering
Structural And Functional Characterization Of A Lytic Polysaccharide Monooxygenase With Broad Substrate Specificity, Anna S. Borisova, Trine Isaksen, Maria Dimarogona, Abhishek A. Kognole, Geir Mathiesen, Anikó Várnai, Åsmund K. Røhr, Christina M. Payne, Morten Sørlie, Mats Sandgren, Vincent G. H. Eijsink
Structural And Functional Characterization Of A Lytic Polysaccharide Monooxygenase With Broad Substrate Specificity, Anna S. Borisova, Trine Isaksen, Maria Dimarogona, Abhishek A. Kognole, Geir Mathiesen, Anikó Várnai, Åsmund K. Røhr, Christina M. Payne, Morten Sørlie, Mats Sandgren, Vincent G. H. Eijsink
Chemical and Materials Engineering Faculty Publications
The recently discovered lytic polysaccharide monooxygenases (LPMOs) carry out oxidative cleavage of polysaccharides and are of major importance for efficient processing of biomass. NcLPMO9C from Neurospora crassa acts both on cellulose and on non-cellulose β-glucans, including cellodextrins and xyloglucan. The crystal structure of the catalytic domain of NcLPMO9C revealed an extended, highly polar substrate-binding surface well suited to interact with a variety of sugar substrates. The ability of NcLPMO9C to act on soluble substrates was exploited to study enzyme-substrate interactions. EPR studies demonstrated that the Cu2+ center environment is altered upon substrate binding, whereas isothermal titration …