Novel structures and functions of lytic polysaccharide monooxygenases
Tuesday, April 29, 2014: 3:10 PM
Grand Ballroom F-G, lobby level (Hilton Clearwater Beach)
Svein Jarle Horn1, Jane W. Agger1, Trine Isaksen1, Zarah Forsberg1, Roland Ludwig2, Al MacKenzie1, Gustav Vaarje-Kolstad1, Aniko Varnai1, Bjorge Westereng1 and Vincent G. H. Eijsink1, (1)Department of Chemistry, Biotechnology and Food Science, Norwegian University of Life Sciences, Aas, Norway, (2)Department of Food Science and Technology, BOKU, University of Natural Resources and Life Sciences, Vienna, Australia
Saccharification of lignocellulosic biomass to fermentable sugars will be a key technology in future biorefineries. Traditionally, biomass degradation was thought to be accomplished by mixtures of hydrolytic enzymes. However, recently it has been shown that lytic polysaccharide monooxygenases (LPMOs) take part in this process by catalyzing cleavage of insoluble polysaccharides utilizing a mechanism involving molecular oxygen and an electron donor (1-6). So far, LPMOs have been demonstrated to cleave the beta 1,4 glycosidic bonds in chitin or cellulose, generating products that are oxidized in the C1 position (“downstream end”) or the C4 position (“upstream end”) (1, 2, 5, 7). We have recently characterized the structures and functions of several LPMOs belonging to the AA9 (formerly GH61) and AA10 (formerly CBM33) families. This has revealed novel structural and functional features of these enzymes, which will be presented.


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