Nanostructure of cellulose microfibrils in spruce wood

The structure of cellulose microfibrils in wood is not known in detail, despite the abundance of cellulose in woody biomass and its importance for biology, energy, and engineering. The structure of the microfibrils of spruce wood cellulose was investigated using a range of spectroscopic methods coup...

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Published inProceedings of the National Academy of Sciences - PNAS Vol. 108; no. 47; pp. E1195 - E1203
Main Authors Fernandes, Anwesha N, Thomas, Lynne H, Altaner, Clemens M, Callow, Philip, Forsyth, V. Trevor, Apperley, David C, Kennedy, Craig J, Jarvis, Michael C
Format Journal Article
LanguageEnglish
Published United States National Academy of Sciences 22.11.2011
National Acad Sciences
SeriesPNAS Plus
Subjects
Biological Sciences
Biomass
Biosynthesis
Cellulose
Cellulose - ultrastructure
energy
engineering
Hydrogen
hydrogen bonding
Hydrogen bonds
hydrophobicity
Magnetic Resonance Spectroscopy
Microfibrils - ultrastructure
Models, Molecular
nanomaterials
Nanostructured materials
Neutron Diffraction
Physical Sciences
Picea
PNAS Plus
Scattering, Small Angle
spectroscopy
Spectroscopy, Fourier Transform Infrared
Spectrum analysis
wood
Wood - ultrastructure
X-radiation
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Summary:The structure of cellulose microfibrils in wood is not known in detail, despite the abundance of cellulose in woody biomass and its importance for biology, energy, and engineering. The structure of the microfibrils of spruce wood cellulose was investigated using a range of spectroscopic methods coupled to small-angle neutron and wide-angle X-ray scattering. The scattering data were consistent with 24-chain microfibrils and favored a "rectangular" model with both hydrophobic and hydrophilic surfaces exposed. Disorder in chain packing and hydrogen bonding was shown to increase outwards from the microfibril center. The extent of disorder blurred the distinction between the I alpha and I beta allomorphs. Chains at the surface were distinct in conformation, with high levels of conformational disorder at C-6, less intramolecular hydrogen bonding and more outward-directed hydrogen bonding. Axial disorder could be explained in terms of twisting of the microfibrils, with implications for their biosynthesis.
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Edited* by Chris R. Somerville, University of California, Berkeley, CA, and approved September 19, 2011 (received for review June 6, 2011)
Author contributions: A.N.F., L.H.T., C.M.A., P.C., V.T.F., D.C.A., and M.C.J. designed research; A.N.F., L.H.T., C.M.A., P.C., V.T.F., D.C.A., and M.C.J. performed research; C.M.A. contributed new reagents/analytic tools; A.N.F., L.H.T., C.M.A., P.C., V.T.F., D.C.A., C.J.K., and M.C.J. analyzed data; and M.C.J. wrote the paper.
ISSN:0027-8424
1091-6490
1091-6490
DOI:10.1073/pnas.1108942108