Polysaccharide degradation by lytic polysaccharide monooxygenases

Forsberg, Zarah; Sørlie, Morten; Petrović, Dejan M.; Courtade, Gastón; Aachmann, Finn Lillelund; Vaaje‐Kolstad, Gustav; Bissaro, Bastien; Røhr, Åsmund K.; Eijsink, Vincent G. H.

doi:10.1016/j.sbi.2019.02.015

Cited by 124 publications

(104 citation statements)

References 66 publications

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“…C1 oxidation leads to the formation of sugar lactones, which undergo conversion into aldonic acids. The acidic products are then preferentially detected in the form of salt (sodium or potassium), charged by an additional alkali metal cation (Na + or K + ) [27,34]. On the other hand, C4 oxidizing LPMOs create keto/gemdiol forms, which are not forming salts and are present only as single alkali metal cation charged masses.…”

Section: Interaction Of Nclpmo9c With Nccdhiiamentioning

confidence: 99%

“…Reduced LPMOs are reported to utilize either O 2 [3,25] or H 2 O 2 [26] as a cosubstrate, resulting in a monooxygenase or peroxygenase reaction, respectively. The outcome of both reactions is the regioselective insertion of an oxygen atom at the C1 [4] or C4 [9] carbon of the glycosidic linkage, which destabilizes and breaks the bond [17,27]. Recent kinetic studies of bacterial [26,28] and fungal LPMOs [29] showed that turnover numbers with H 2 O 2 as cosubstrate exceeded those obtained with O 2 by two orders of magnitude.…”

Section: Introductionmentioning

confidence: 99%

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The H2O2-dependent activity of a fungal lytic polysaccharide monooxygenase investigated with a turbidimetric assay

Filandr

Man

Halada

et al. 2020

Biotechnol Biofuels

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Background: Lytic polysaccharide monooxygenases (LPMOs) are copper-dependent redox enzymes that cleave recalcitrant biopolymers such as cellulose, chitin, starch and hemicelluloses. Although LPMOs receive ample interest in industry and academia, their reaction mechanism is not yet fully understood. Recent studies showed that H 2 O 2 is a more efficient cosubstrate for the enzyme than O 2 , which could greatly affect the utilization of LPMOs in industrial settings. Results:We probe the reactivity of LPMO9C from the cellulose-degrading fungus Neurospora crassa with a turbidimetric assay using phosphoric acid-swollen cellulose (PASC) as substrate and H 2 O 2 as a cosubstrate. The measurements were also followed by continuous electrochemical H 2 O 2 detection and LPMO reaction products were analysed by mass spectrometry. Different systems for the in situ generation of H 2 O 2 and for the reduction of LPMO's active-site copper were employed, including glucose oxidase, cellobiose dehydrogenase, and the routinely used reductant ascorbate. Conclusions:We found for all systems that the supply of H 2 O 2 limited LPMO's cellulose depolymerization activity, which supports the function of H 2 O 2 as the relevant cosubstrate. The turbidimetric assay allowed rapid determination of LPMO activity on a cellulosic substrate without the need for time-consuming and instrumentally elaborate analysis methods.

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Section: Interaction Of Nclpmo9c With Nccdhiiamentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

The H2O2-dependent activity of a fungal lytic polysaccharide monooxygenase investigated with a turbidimetric assay

Filandr

Man

Halada

et al. 2020

Biotechnol Biofuels

View full text Add to dashboard Cite

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“…The reaction was shown to be dependent on the presence of O 2 and reductant 3 . Ten years of intensive research has revealed the presence of LPMOs in most kingdoms of life [3][4][5][6][7] and today, these enzymes are classified within seven families of auxiliary activities (AA) 8 in the database of carbohydrate-active enzymes 9 , with families AA9, from fungal origin, and AA10, primarily from bacterial origin, being the best studied. To date, many LPMOs, acting on various oligo-and polysaccharides, and using different regioselectivities of oxidation, have been identified 10 .…”

mentioning

confidence: 99%

“…While structurally and functionally well characterized 7,11 , kinetic studies of LPMOs are scarce. The scarcity of kinetic data likely reflects the numerous experimental challenges associated with quantitative characterization of LPMO functionality 12 .…”

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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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“…Für Letzteres wäre eine molekulare Architektur notwendig, die es über möglichst breite und flache Häm-Zugangskanäle erlaubt, aromatische Polymerstrukturen oberflächlich anzugreifen. In diesem Zusammenhang sei darauf verwiesen, dass die erst vor wenigen Jahren entdeckten, kristalline Cellulose spaltenden LPMOs (lyticpolysaccharidemonooxygenases) jüngsten Publikationen zufolge ebenfalls oberflächenwirksame, extrazelluläre Peroxygenasen sind (wenn auch auf Basis einer kupferabhängigen Katalyse) [13].…”

Section: Verbreitung Im Pilzreich Und Phylogenieunclassified

Unspezifische Peroxygenasen — Oxyfunktionalisierung außerhalb der Pilzhyphe

et al. 2020

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Polysaccharide degradation by lytic polysaccharide monooxygenases

Cited by 124 publications

References 66 publications

The H2O2-dependent activity of a fungal lytic polysaccharide monooxygenase investigated with a turbidimetric assay

The H2O2-dependent activity of a fungal lytic polysaccharide monooxygenase investigated with a turbidimetric assay

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

Unspezifische Peroxygenasen — Oxyfunktionalisierung außerhalb der Pilzhyphe

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