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Light-driven oxidation of polysaccharides by photosynthetic pigments and a metalloenzyme.

ABSTRACT: Oxidative processes are essential for the degradation of plant biomass. A class of powerful and widely distributed oxidative enzymes, the lytic polysaccharide monooxygenases (LPMOs), oxidize the most recalcitrant polysaccharides and require extracellular electron donors. Here we investigated the effect of using excited photosynthetic pigments as electron donors. LPMOs combined with pigments and reducing agents were exposed to light, which resulted in a never before seen 100-fold increase in catalytic activity. In addition, LPMO substrate specificity was broadened to include both cellulose and hemicellulose. LPMO enzymes and pigment derivatives common in the environment of plant-degrading organisms thus form a highly reactive and stable light-driven system increasing the turnover rate and versatility of LPMOs. This light-driven system may find applications in biotechnology and chemical processing.

SUBMITTER: Cannella D

PROVIDER: S-EPMC4822002 | biostudies-literature | 2016 Apr

REPOSITORIES: biostudies-literature

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Light-driven oxidation of polysaccharides by photosynthetic pigments and a metalloenzyme.

Cannella D D Möllers K B KB Frigaard N-U NU Jensen P E PE Bjerrum M J MJ Johansen K S KS Felby C C

Nature communications 20160404

Oxidative processes are essential for the degradation of plant biomass. A class of powerful and widely distributed oxidative enzymes, the lytic polysaccharide monooxygenases (LPMOs), oxidize the most recalcitrant polysaccharides and require extracellular electron donors. Here we investigated the effect of using excited photosynthetic pigments as electron donors. LPMOs combined with pigments and reducing agents were exposed to light, which resulted in a never before seen 100-fold increase in cata ...[more]

PMID: 27041218

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Dataset Information

Light-driven oxidation of polysaccharides by photosynthetic pigments and a metalloenzyme.

Publications

Light-driven oxidation of polysaccharides by photosynthetic pigments and a metalloenzyme.

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