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Our comparative studies reveal that the two lytic polysaccharide monooxygenases  Hi LPMO9B and  Hi LPMO9I from the white-rot conifer pathogen  Heterobasidion irregulare  display clear difference with respect to their activity against crystalline cellulose and glucomannan.  Hi LPMO9I produced very little soluble sugar on bacterial microcrystalline cellulose (BMCC). In contrast,  Hi LPMO9B was much more active against BMCC and even released more soluble sugar than the  H .  irregulare  cellobiohydrolase I,  Hi Cel7A. Furthermore,  Hi LPMO9B was shown to cooperate with and stimulate the activity of  Hi Cel7A, both when the BMCC was first pretreated with  Hi LPMO9B, as well as when  Hi LPMO9B and  Hi Cel7A were added together. No such stimulation was shown by  Hi LPMO9I. On the other hand,  Hi LPMO9I was shown to degrade glucomannan, using a C4-oxidizing mechanism, whereas no oxidative cleavage activity of glucomannan was detected for  Hi LPMO9B. Structural modeling and comparison with other glucomannan-active LPMOs suggest that conserved sugar-interacting residues on the L2, L3 and LC loops may be essential for glucomannan binding, where 4 out of 7 residues are shared by  Hi LPMO9I, but only one is found in  Hi LPMO9B. The difference shown between these two  H .  irregulare  LPMOs may reflect distinct biological roles of these enzymes within deconstruction of different plant cell wall polysaccharides during fungal colonization of softwood.

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Side-by-side biochemical comparison of two lytic polysaccharide monooxygenases from the white-rot fungus Heterobasidion irregulare on their activity against crystalline cellulose and glucomannan