Modularity impacts cellulose surface oxidation by a lytic polysaccharide monooxygenase from Streptomyces coelicolor

Lytic polysaccharide monooxygenases (LPMOs) catalyze the oxidation of β-(1,4)-linked polysaccharides, such as cellulose, in a reaction that requires an electron donor and H 2 O 2 as co-substrate. Several LPMOs include a carbohydrate-binding module (CBM), which promotes action on insoluble substrates...

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Bibliographic Details
Published in:Cellulose (London) 2023-11, Vol.30 (17), p.10783-10794
Main Authors: Raji, Olanrewaju, Eijsink, Vincent G. H., Master, Emma, Forsberg, Zarah
Format: Article
Language:English
Subjects:
Acids
Bioorganic Chemistry
Carbohydrates
Cellulose fibers
Ceramics
Chemistry
Chemistry and Materials Science
Chromatography
Cloning
Composites
Copper
Crystalline cellulose
Dispersion
Enzymes
Fluorescence
Glass
Hydrogen peroxide
Labeling
Modularity
Natural Materials
Organic Chemistry
Original Research
Oxidation
Physical Chemistry
Polymer Sciences
Polysaccharides
Reaction products
Substrates
Sustainable Development
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Summary:Lytic polysaccharide monooxygenases (LPMOs) catalyze the oxidation of β-(1,4)-linked polysaccharides, such as cellulose, in a reaction that requires an electron donor and H 2 O 2 as co-substrate. Several LPMOs include a carbohydrate-binding module (CBM), which promotes action on insoluble substrates. Herein, a fluorescent labeling technique was used to track LPMO action on microcrystalline cellulose and evaluate the impact of CBMs on the distribution of LPMO activity across the fiber surface. Confocal microscopic images revealed that the distribution of oxidized positions on the cellulose surface was CBM-dependent: fluorescent spots were concentrated in reactions with a CBM-containing LPMO whereas they were more dispersed for a CBM-deficient LPMO variant. The more dispersed oxidation pattern for the CBM-free LPMO coincided with the release of fewer soluble reaction products.
ISSN:0969-0239
1572-882X
DOI:10.1007/s10570-023-05551-8