Controlled depolymerization of cellulose by light-driven lytic polysaccharide oxygenases

Bissaro, Bastien; Kommedal, Eirik Garpestad; Røhr, Åsmund K.; Eijsink, Vincent G. H.

doi:10.1038/s41467-020-14744-9

Cited by 79 publications

(138 citation statements)

References 69 publications

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“…The scarcity of kinetic data likely reflects the numerous experimental challenges associated with quantitative characterization of LPMO functionality 12 . The complexity is exemplified by the recent discovery that LPMOs may use H 2 O 2 , rather than, or even instead of, O 2 , as co-substrate [13][14][15][16][17][18][19][20] . Regardless of the mechanism, LPMOs need an external electron donor for catalysis.…”

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confidence: 99%

Kinetic insights into the peroxygenase activity of cellulose-active lytic polysaccharide monooxygenases (LPMOs)

et al. 2020

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Lytic polysaccharide monooxygenases (LPMOs) are widely distributed in Nature, where they catalyze the hydroxylation of glycosidic bonds in polysaccharides. Despite the importance of LPMOs in the global carbon cycle and in industrial biomass conversion, the catalytic properties of these monocopper enzymes remain enigmatic. Strikingly, there is a remarkable lack of kinetic data, likely due to a multitude of experimental challenges related to the insoluble nature of LPMO substrates, like cellulose and chitin, and to the occurrence of multiple side reactions. Here, we employed competition between well characterized reference enzymes and LPMOs for the H2O2 co-substrate to kinetically characterize LPMO-catalyzed cellulose oxidation. LPMOs of both bacterial and fungal origin showed high peroxygenase efficiencies, with kcat/KmH2O2 values in the order of 105–106 M−1 s−1. Besides providing crucial insight into the cellulolytic peroxygenase reaction, these results show that LPMOs belonging to multiple families and active on multiple substrates are true peroxygenases.

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confidence: 99%

Kinetic insights into the peroxygenase activity of cellulose-active lytic polysaccharide monooxygenases (LPMOs)

et al. 2020

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“…In light of the recent publications suggesting H 2 O 2 is a key factor in light-driven LPMO 9 observed. Interestingly, Chl α exposed to a light intensity of 500 µmol m -2 s -1 also showed greatly reduced formation of H 2 O 2 compared to the same experiment with light intensity of 200 µmol m -2 s -1 .…”

Section: Effect Of Light Intensity On H 2 O 2 Productionmentioning

confidence: 85%

“…Besides providing biomass, photosynthetic organisms have also inspired the development of photobiocatalysis, a biomimicry tool, designed to speed up enzymatic reactions using light [3][4][5] . Photobiocatalysis has been shown to increase the activity of cytochrome P450s 6 , methane monooxygenases (pMMO) 7 and fungal lytic polysaccharide monooxygenases (LPMOs) [8][9][10] .…”

Section: Introductionmentioning

confidence: 99%

“…This work proposed that the enhanced light-driven LPMO activity is due to a photoactivated electron transfer from a photosynthetic pigment directly to the LPMO. However, recent evidence indicates the formation of H 2 O 2 by a photosensitizer is involved in the acceleration of light-driven LPMO catalysis 9,10 . Regardless of the exact mechanism, light-driven reactions has the potential to provide more powerful, faster and thus ´greener´ redox reactions 22 .…”

Section: Introductionmentioning

confidence: 99%

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Water-soluble chlorophyll-binding proteins from Brassica oleracea allow for stable photobiocatalytic oxidation of cellulose by a lytic polysaccharide monooxygenase.

Dodge

Russo

Blossom

et al. 2020

Preprint

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Background: Lytic polysaccharide monooxygenases (LPMOs) are indispensable redox enzymes used in industry for the saccharification of plant biomass. LPMO-driven cellulose oxidation can be enhanced considerably through photobiocatalysis using chlorophyll derivatives and light. Water soluble chlorophyll binding proteins (WSCPs) make it is possible to stabilize and solubilize chlorophyll in aqueous solution, allowing for in vitro studies on photostability and ROS production. Here we aim apply a WSCP-Chl α as a photosensitizing complex for photobiocatalysis with the LPMO, TtAA9. Results: We have in this study demonstrated how WSCP reconstituted with chlorophyll a (WSCP-Chl α) can create a stable photosensitizing complex which produces controlled amounts of H2O2 in the presence of ascorbic acid and light. WSCP-Chl α is highly reactive and allows for tightly controlled formation of H2O2 by regulating light intensity. TtAA9 together with WSCP-Chl α shows increased cellulose oxidation under low light conditions, and the WSCP-Chl α complex remains stable after 24 hours of light exposure. Additionally, the WSCP-Chl α complex demonstrates stability over a range of temperatures and pH conditions relevant for enzyme activity in industrial settings.Conclusion: With WSCP-Chl α as the photosensitizer, the need to replenish Chl is greatly reduced, enhancing the catalytic lifetime of light-driven LPMOs and increasing the efficiency of cellulose depolymerization. WSCP-Chl α allows for stable photobiocatalysis providing a sustainable solution for biomass processing.

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“…This work proposed that the enhanced light-driven LPMO activity is due to a photoactivated electron transfer from a photosynthetic pigment directly to the LPMO. However, recent evidence indicates the formation of H 2 O 2 by a photosensitizer is involved in the acceleration of light-driven LPMO catalysis 9,10 . Regardless of the exact mechanism, it is certain that photobiocatalysis has the potential to provide more powerful, faster and thus ´greener´ redox reactions 20 .…”

Section: Introductionmentioning

confidence: 99%

Water-soluble chlorophyll-binding proteins from Brassica oleracea allow for stable photobiocatalytic oxidation of cellulose by a lytic polysaccharide monooxygenase

Dodge

Russo

Blossom

et al. 2020

Preprint

View full text Add to dashboard Cite

Abstract Background Lytic polysaccharide monooxygenases (LPMOs) are indispensable redox enzymes used in industry for the saccharification of plant biomass. LPMO-driven cellulose oxidation can be enhanced considerably through photobiocatalysis using chlorophyll derivatives and light. Water soluble chlorophyll binding proteins (WSCPs) make it is possible to stabilize and solubilize chlorophyll in aqueous solution, allowing for in vitro studies on photostability and ROS production. Here we aim apply a WSCP-Chl a as a photosensitizing complex for photobiocatalysis with the LPMO, TtAA9. Results We have in this study demonstrated how WSCP reconstituted with chlorophyll a (WSCP-Chl a) can create a stable photosensitizing complex which produces controlled amounts of H2O2 in the presence of ascorbic acid and light. WSCP-Chl a is highly reactive and allows for tightly controlled formation of H2O2 by regulating light intensity. TtAA9 together with WSCP-Chl a shows increased cellulose oxidation under low light conditions, and the WSCP-Chl a complex remains stable after 24 hours of light exposure. Additionally, the WSCP-Chl a complex demonstrates stability over a range of temperatures and pH conditions relevant for enzyme activity in industrial settings. Conclusion With WSCP-Chl a as the photosensitizer, the need to replenish Chl is greatly reduced, enhancing the catalytic lifetime of light-driven LPMOs and increasing the efficiency of cellulose depolymerization. WSCP-Chl a allows for stable photobiocatalysis providing a sustainable solution for biomass processing.

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Controlled depolymerization of cellulose by light-driven lytic polysaccharide oxygenases

Cited by 79 publications

References 69 publications

Kinetic insights into the peroxygenase activity of cellulose-active lytic polysaccharide monooxygenases (LPMOs)

Kinetic insights into the peroxygenase activity of cellulose-active lytic polysaccharide monooxygenases (LPMOs)

Water-soluble chlorophyll-binding proteins from Brassica oleracea allow for stable photobiocatalytic oxidation of cellulose by a lytic polysaccharide monooxygenase.

Water-soluble chlorophyll-binding proteins from Brassica oleracea allow for stable photobiocatalytic oxidation of cellulose by a lytic polysaccharide monooxygenase

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