Discovery of LPMO activity on hemicelluloses shows the importance of oxidative processes in plant cell wall degradation

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Discovery of LPMO activity on hemicelluloses shows the importance of oxidative processes in plant cell wall degradation. / Agger, Jane W.; Isaksen, Trine; Várnai, Anikó; Vidal Melgosa, Silvia; Willats, William George Tycho; Ludwig, Roland; Horn, Svein J.; Eijsink, Vincent G.H.; Westereng, Bjørge.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 111, No. 17, 2014, p. 6287-6292.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Agger, JW, Isaksen, T, Várnai, A, Vidal Melgosa, S, Willats, WGT, Ludwig, R, Horn, SJ, Eijsink, VGH & Westereng, B 2014, 'Discovery of LPMO activity on hemicelluloses shows the importance of oxidative processes in plant cell wall degradation', Proceedings of the National Academy of Sciences of the United States of America, vol. 111, no. 17, pp. 6287-6292. https://doi.org/10.1073/pnas.1323629111

APA

Agger, J. W., Isaksen, T., Várnai, A., Vidal Melgosa, S., Willats, W. G. T., Ludwig, R., Horn, S. J., Eijsink, V. G. H., & Westereng, B. (2014). Discovery of LPMO activity on hemicelluloses shows the importance of oxidative processes in plant cell wall degradation. Proceedings of the National Academy of Sciences of the United States of America, 111(17), 6287-6292. https://doi.org/10.1073/pnas.1323629111

Vancouver

Agger JW, Isaksen T, Várnai A, Vidal Melgosa S, Willats WGT, Ludwig R et al. Discovery of LPMO activity on hemicelluloses shows the importance of oxidative processes in plant cell wall degradation. Proceedings of the National Academy of Sciences of the United States of America. 2014;111(17):6287-6292. https://doi.org/10.1073/pnas.1323629111

Author

Agger, Jane W. ; Isaksen, Trine ; Várnai, Anikó ; Vidal Melgosa, Silvia ; Willats, William George Tycho ; Ludwig, Roland ; Horn, Svein J. ; Eijsink, Vincent G.H. ; Westereng, Bjørge. / Discovery of LPMO activity on hemicelluloses shows the importance of oxidative processes in plant cell wall degradation. In: Proceedings of the National Academy of Sciences of the United States of America. 2014 ; Vol. 111, No. 17. pp. 6287-6292.

Bibtex

@article{a939ce45ef024b128c6ad40fa1d7b6cc,
title = "Discovery of LPMO activity on hemicelluloses shows the importance of oxidative processes in plant cell wall degradation",
abstract = "The recently discovered lytic polysaccharide monooxygenases (LPMOs) are known to carry out oxidative cleavage of glycoside bonds in chitin and cellulose, thus boosting the activity ofwell-known hydrolytic depolymerizing enzymes. Because biomass-degrading microorganisms tend to produce a plethora of LPMOs, and considering the complexity and copolymeric nature of the plant cell wall, it has been speculated that some LPMOs may act on other substrates, in particular the hemicelluloses that tether to cellulose microfibrils. We demonstrate that an LPMO from Neurospora crassa, NcLPMO9C, indeed degrades various hemicelluloses, in particular xyloglucan. This activity was discovered using a glycan microarray-based screening method for detection of substrate specificities of carbohydrate-active enzymes, and further explored using defined oligomeric hemicelluloses, isolated polymeric hemicelluloses and cell walls. Products generated by NcLPMO9C were analyzed using high performance anion exchange chromatography and multidimensional mass spectrometry. We show that NcLPMO9C generates oxidized products from a variety of substrates and that its product profile differs from those of hydrolytic enzymes acting on the same substrates. The enzyme particularly acts on the glucose backbone of xyloglucan, accepting various substitutions (xylose, galactose) in almost all positions. Because the attachment of xyloglucan to cellulose hampers depolymerization of the latter, it is possible that the beneficial effect of the LPMOs that are present in current commercial cellulase mixtures in part is due to hitherto undetected LPMO activities on recalcitrant hemicellulose structures.",
keywords = "Biorefinery, CBM33, GH61, Metallo enzymes",
author = "Agger, {Jane W.} and Trine Isaksen and Anik{\'o} V{\'a}rnai and {Vidal Melgosa}, Silvia and Willats, {William George Tycho} and Roland Ludwig and Horn, {Svein J.} and Eijsink, {Vincent G.H.} and Bj{\o}rge Westereng",
year = "2014",
doi = "10.1073/pnas.1323629111",
language = "English",
volume = "111",
pages = "6287--6292",
journal = "Proceedings of the National Academy of Sciences of the United States of America",
issn = "0027-8424",
publisher = "The National Academy of Sciences of the United States of America",
number = "17",

}

RIS

TY - JOUR

T1 - Discovery of LPMO activity on hemicelluloses shows the importance of oxidative processes in plant cell wall degradation

AU - Agger, Jane W.

AU - Isaksen, Trine

AU - Várnai, Anikó

AU - Vidal Melgosa, Silvia

AU - Willats, William George Tycho

AU - Ludwig, Roland

AU - Horn, Svein J.

AU - Eijsink, Vincent G.H.

AU - Westereng, Bjørge

PY - 2014

Y1 - 2014

N2 - The recently discovered lytic polysaccharide monooxygenases (LPMOs) are known to carry out oxidative cleavage of glycoside bonds in chitin and cellulose, thus boosting the activity ofwell-known hydrolytic depolymerizing enzymes. Because biomass-degrading microorganisms tend to produce a plethora of LPMOs, and considering the complexity and copolymeric nature of the plant cell wall, it has been speculated that some LPMOs may act on other substrates, in particular the hemicelluloses that tether to cellulose microfibrils. We demonstrate that an LPMO from Neurospora crassa, NcLPMO9C, indeed degrades various hemicelluloses, in particular xyloglucan. This activity was discovered using a glycan microarray-based screening method for detection of substrate specificities of carbohydrate-active enzymes, and further explored using defined oligomeric hemicelluloses, isolated polymeric hemicelluloses and cell walls. Products generated by NcLPMO9C were analyzed using high performance anion exchange chromatography and multidimensional mass spectrometry. We show that NcLPMO9C generates oxidized products from a variety of substrates and that its product profile differs from those of hydrolytic enzymes acting on the same substrates. The enzyme particularly acts on the glucose backbone of xyloglucan, accepting various substitutions (xylose, galactose) in almost all positions. Because the attachment of xyloglucan to cellulose hampers depolymerization of the latter, it is possible that the beneficial effect of the LPMOs that are present in current commercial cellulase mixtures in part is due to hitherto undetected LPMO activities on recalcitrant hemicellulose structures.

AB - The recently discovered lytic polysaccharide monooxygenases (LPMOs) are known to carry out oxidative cleavage of glycoside bonds in chitin and cellulose, thus boosting the activity ofwell-known hydrolytic depolymerizing enzymes. Because biomass-degrading microorganisms tend to produce a plethora of LPMOs, and considering the complexity and copolymeric nature of the plant cell wall, it has been speculated that some LPMOs may act on other substrates, in particular the hemicelluloses that tether to cellulose microfibrils. We demonstrate that an LPMO from Neurospora crassa, NcLPMO9C, indeed degrades various hemicelluloses, in particular xyloglucan. This activity was discovered using a glycan microarray-based screening method for detection of substrate specificities of carbohydrate-active enzymes, and further explored using defined oligomeric hemicelluloses, isolated polymeric hemicelluloses and cell walls. Products generated by NcLPMO9C were analyzed using high performance anion exchange chromatography and multidimensional mass spectrometry. We show that NcLPMO9C generates oxidized products from a variety of substrates and that its product profile differs from those of hydrolytic enzymes acting on the same substrates. The enzyme particularly acts on the glucose backbone of xyloglucan, accepting various substitutions (xylose, galactose) in almost all positions. Because the attachment of xyloglucan to cellulose hampers depolymerization of the latter, it is possible that the beneficial effect of the LPMOs that are present in current commercial cellulase mixtures in part is due to hitherto undetected LPMO activities on recalcitrant hemicellulose structures.

KW - Biorefinery

KW - CBM33

KW - GH61

KW - Metallo enzymes

U2 - 10.1073/pnas.1323629111

DO - 10.1073/pnas.1323629111

M3 - Journal article

C2 - 24733907

AN - SCOPUS:84899647519

VL - 111

SP - 6287

EP - 6292

JO - Proceedings of the National Academy of Sciences of the United States of America

JF - Proceedings of the National Academy of Sciences of the United States of America

SN - 0027-8424

IS - 17

ER -

ID: 117494089