Debranching of soluble wheat arabinoxylan dramatically enhances recalcitrant binding to cellulose

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Debranching of soluble wheat arabinoxylan dramatically enhances recalcitrant binding to cellulose. / Selig, Michael J.; Thygesen, Lisbeth G.; Felby, Claus; Master, Emma R.

In: Biotechnology Letters, Vol. 37, No. 3, 2015, p. 633-641.

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

Harvard

Selig, MJ, Thygesen, LG, Felby, C & Master, ER 2015, 'Debranching of soluble wheat arabinoxylan dramatically enhances recalcitrant binding to cellulose', Biotechnology Letters, vol. 37, no. 3, pp. 633-641. https://doi.org/10.1007/s10529-014-1705-0

APA

Selig, M. J., Thygesen, L. G., Felby, C., & Master, E. R. (2015). Debranching of soluble wheat arabinoxylan dramatically enhances recalcitrant binding to cellulose. Biotechnology Letters, 37(3), 633-641. https://doi.org/10.1007/s10529-014-1705-0

Vancouver

Selig MJ, Thygesen LG, Felby C, Master ER. Debranching of soluble wheat arabinoxylan dramatically enhances recalcitrant binding to cellulose. Biotechnology Letters. 2015;37(3):633-641. https://doi.org/10.1007/s10529-014-1705-0

Author

Selig, Michael J. ; Thygesen, Lisbeth G. ; Felby, Claus ; Master, Emma R. / Debranching of soluble wheat arabinoxylan dramatically enhances recalcitrant binding to cellulose. In: Biotechnology Letters. 2015 ; Vol. 37, No. 3. pp. 633-641.

Bibtex

@article{c9ddff529664480794221ebdf9ed972d,
title = "Debranching of soluble wheat arabinoxylan dramatically enhances recalcitrant binding to cellulose",
abstract = "The presence of xylan is a detriment to the enzymatic saccharification of cellulose in lignocelluloses. The inhibition of the processive cellobiohydrolase Cel7A by soluble wheat arabinoxylan is shown here to increase by 50 % following enzymatic treatment with a commercially-purified α-l-arabinofuranosidase. The enhanced inhibitory effect was shown by T2 relaxation time measurements via low field NMR to coincide with an increasing degree of constraint put on the water in xylan solutions. Furthermore, quartz crystal micro-balance with dissipation experiments showed that α-l-arabinofuranosidase treatment considerably increased the rate and rigidity of arabinoxylan mass association with cellulose. These data also suggest significant xylan–xylan adlayer formation occurs following initial binding of debranched arabinoxylan. From this, we speculate the inhibitory effects of xylan to cellulases may result from reduced enzymatic access via the dense association of xylan with cellulose.",
keywords = "Arabinoxylan, Binding, Cellobiohydrolase, Cellulose, Debranching, QCM-D",
author = "Selig, {Michael J.} and Thygesen, {Lisbeth G.} and Claus Felby and Master, {Emma R.}",
year = "2015",
doi = "10.1007/s10529-014-1705-0",
language = "English",
volume = "37",
pages = "633--641",
journal = "Biotechnology Letters",
issn = "0141-5492",
publisher = "Springer",
number = "3",

}

RIS

TY - JOUR

T1 - Debranching of soluble wheat arabinoxylan dramatically enhances recalcitrant binding to cellulose

AU - Selig, Michael J.

AU - Thygesen, Lisbeth G.

AU - Felby, Claus

AU - Master, Emma R.

PY - 2015

Y1 - 2015

N2 - The presence of xylan is a detriment to the enzymatic saccharification of cellulose in lignocelluloses. The inhibition of the processive cellobiohydrolase Cel7A by soluble wheat arabinoxylan is shown here to increase by 50 % following enzymatic treatment with a commercially-purified α-l-arabinofuranosidase. The enhanced inhibitory effect was shown by T2 relaxation time measurements via low field NMR to coincide with an increasing degree of constraint put on the water in xylan solutions. Furthermore, quartz crystal micro-balance with dissipation experiments showed that α-l-arabinofuranosidase treatment considerably increased the rate and rigidity of arabinoxylan mass association with cellulose. These data also suggest significant xylan–xylan adlayer formation occurs following initial binding of debranched arabinoxylan. From this, we speculate the inhibitory effects of xylan to cellulases may result from reduced enzymatic access via the dense association of xylan with cellulose.

AB - The presence of xylan is a detriment to the enzymatic saccharification of cellulose in lignocelluloses. The inhibition of the processive cellobiohydrolase Cel7A by soluble wheat arabinoxylan is shown here to increase by 50 % following enzymatic treatment with a commercially-purified α-l-arabinofuranosidase. The enhanced inhibitory effect was shown by T2 relaxation time measurements via low field NMR to coincide with an increasing degree of constraint put on the water in xylan solutions. Furthermore, quartz crystal micro-balance with dissipation experiments showed that α-l-arabinofuranosidase treatment considerably increased the rate and rigidity of arabinoxylan mass association with cellulose. These data also suggest significant xylan–xylan adlayer formation occurs following initial binding of debranched arabinoxylan. From this, we speculate the inhibitory effects of xylan to cellulases may result from reduced enzymatic access via the dense association of xylan with cellulose.

KW - Arabinoxylan

KW - Binding

KW - Cellobiohydrolase

KW - Cellulose

KW - Debranching

KW - QCM-D

UR - http://www.scopus.com/inward/record.url?scp=84925543688&partnerID=8YFLogxK

U2 - 10.1007/s10529-014-1705-0

DO - 10.1007/s10529-014-1705-0

M3 - Journal article

C2 - 25335745

AN - SCOPUS:84925543688

VL - 37

SP - 633

EP - 641

JO - Biotechnology Letters

JF - Biotechnology Letters

SN - 0141-5492

IS - 3

ER -

ID: 136770309