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
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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