Single-molecule study of oxidative enzymaticdeconstruction of cellulose

Research output: Contribution to journalArticleResearch

Abstract

LPMO (lytic polysaccharide monooxygenase) represents a unique paradigm of cellulosicbiomass degradation by an oxidative mechanism. Understanding the role of LPMO indeconstructing crystalline cellulose is fundamental to the enzyme’s biological function andwill help to specify the use of LPMO in biorefinery applications. Here we show with real-timeatomic force microscopy that C1 and C4 oxidizing types of LPMO from Neurospora crassa(NcLPMO9F, NcLPMO9C) bind to nanocrystalline cellulose with high preference for the verysame substrate surfaces that are also used by a processive cellulase (Trichoderma reeseiCBH I) to move along during hydrolytic cellulose degradation. The bound LPMOs, however,are immobile during their adsorbed residence time ( ~ 1.0 min for NcLPMO9F) on cellulose.Treatment with LPMO resulted in fibrillation of crystalline cellulose and strongly ( ≥ 2-fold)enhanced the cellulase adsorption. It also increased enzyme turnover on the cellulose surface,thus boosting the hydrolytic conversion.
Original languageEnglish
Pages (from-to)8:894
Number of pages7
JournalNature Communications
DOIs
Publication statusPublished - 2017

ASJC Scopus subject areas

  • Materials Science(all)

Fields of Expertise

  • Advanced Materials Science

Cite this

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title = "Single-molecule study of oxidative enzymaticdeconstruction of cellulose",
abstract = "LPMO (lytic polysaccharide monooxygenase) represents a unique paradigm of cellulosicbiomass degradation by an oxidative mechanism. Understanding the role of LPMO indeconstructing crystalline cellulose is fundamental to the enzyme’s biological function andwill help to specify the use of LPMO in biorefinery applications. Here we show with real-timeatomic force microscopy that C1 and C4 oxidizing types of LPMO from Neurospora crassa(NcLPMO9F, NcLPMO9C) bind to nanocrystalline cellulose with high preference for the verysame substrate surfaces that are also used by a processive cellulase (Trichoderma reeseiCBH I) to move along during hydrolytic cellulose degradation. The bound LPMOs, however,are immobile during their adsorbed residence time ( ~ 1.0 min for NcLPMO9F) on cellulose.Treatment with LPMO resulted in fibrillation of crystalline cellulose and strongly ( ≥ 2-fold)enhanced the cellulase adsorption. It also increased enzyme turnover on the cellulose surface,thus boosting the hydrolytic conversion.",
author = "Manuel Eibinger and J{\"u}rgen Sattelkow and Thomas Ganner and Harald Plank and Bernd Nidetzky",
year = "2017",
doi = "DOI: 10.1038/s41467-017-01028-y",
language = "English",
pages = "8:894",
journal = "Nature Communications",
issn = "2041-1723",
publisher = "Nature Publishing Group",

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TY - JOUR

T1 - Single-molecule study of oxidative enzymaticdeconstruction of cellulose

AU - Eibinger, Manuel

AU - Sattelkow, Jürgen

AU - Ganner, Thomas

AU - Plank, Harald

AU - Nidetzky, Bernd

PY - 2017

Y1 - 2017

N2 - LPMO (lytic polysaccharide monooxygenase) represents a unique paradigm of cellulosicbiomass degradation by an oxidative mechanism. Understanding the role of LPMO indeconstructing crystalline cellulose is fundamental to the enzyme’s biological function andwill help to specify the use of LPMO in biorefinery applications. Here we show with real-timeatomic force microscopy that C1 and C4 oxidizing types of LPMO from Neurospora crassa(NcLPMO9F, NcLPMO9C) bind to nanocrystalline cellulose with high preference for the verysame substrate surfaces that are also used by a processive cellulase (Trichoderma reeseiCBH I) to move along during hydrolytic cellulose degradation. The bound LPMOs, however,are immobile during their adsorbed residence time ( ~ 1.0 min for NcLPMO9F) on cellulose.Treatment with LPMO resulted in fibrillation of crystalline cellulose and strongly ( ≥ 2-fold)enhanced the cellulase adsorption. It also increased enzyme turnover on the cellulose surface,thus boosting the hydrolytic conversion.

AB - LPMO (lytic polysaccharide monooxygenase) represents a unique paradigm of cellulosicbiomass degradation by an oxidative mechanism. Understanding the role of LPMO indeconstructing crystalline cellulose is fundamental to the enzyme’s biological function andwill help to specify the use of LPMO in biorefinery applications. Here we show with real-timeatomic force microscopy that C1 and C4 oxidizing types of LPMO from Neurospora crassa(NcLPMO9F, NcLPMO9C) bind to nanocrystalline cellulose with high preference for the verysame substrate surfaces that are also used by a processive cellulase (Trichoderma reeseiCBH I) to move along during hydrolytic cellulose degradation. The bound LPMOs, however,are immobile during their adsorbed residence time ( ~ 1.0 min for NcLPMO9F) on cellulose.Treatment with LPMO resulted in fibrillation of crystalline cellulose and strongly ( ≥ 2-fold)enhanced the cellulase adsorption. It also increased enzyme turnover on the cellulose surface,thus boosting the hydrolytic conversion.

U2 - DOI: 10.1038/s41467-017-01028-y

DO - DOI: 10.1038/s41467-017-01028-y

M3 - Article

SP - 8:894

JO - Nature Communications

JF - Nature Communications

SN - 2041-1723

ER -