Trichoderma reesei CE16 acetyl esterase and its role in enzymatic degradation of acetylated hemicellulose

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Standard

Trichoderma reesei CE16 acetyl esterase and its role in enzymatic degradation of acetylated hemicellulose. / Biely, Peter; Cziszarava, Maria; Agger, Jane W.; Li, Xin-Liang; Puchart, Vladimir; Vranska, Maria; Eijsink, Vincent G.H.; Westereng, Bjørge.

In: BBA General Subjects, Vol. 1840, No. 1, 2014, p. 516-525.

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

Harvard

Biely, P, Cziszarava, M, Agger, JW, Li, X-L, Puchart, V, Vranska, M, Eijsink, VGH & Westereng, B 2014, 'Trichoderma reesei CE16 acetyl esterase and its role in enzymatic degradation of acetylated hemicellulose', BBA General Subjects, vol. 1840, no. 1, pp. 516-525. https://doi.org/10.1016/j.bbagen.2013.10.008

APA

Biely, P., Cziszarava, M., Agger, J. W., Li, X-L., Puchart, V., Vranska, M., Eijsink, V. G. H., & Westereng, B. (2014). Trichoderma reesei CE16 acetyl esterase and its role in enzymatic degradation of acetylated hemicellulose. BBA General Subjects, 1840(1), 516-525. https://doi.org/10.1016/j.bbagen.2013.10.008

Vancouver

Biely P, Cziszarava M, Agger JW, Li X-L, Puchart V, Vranska M et al. Trichoderma reesei CE16 acetyl esterase and its role in enzymatic degradation of acetylated hemicellulose. BBA General Subjects. 2014;1840(1):516-525. https://doi.org/10.1016/j.bbagen.2013.10.008

Author

Biely, Peter ; Cziszarava, Maria ; Agger, Jane W. ; Li, Xin-Liang ; Puchart, Vladimir ; Vranska, Maria ; Eijsink, Vincent G.H. ; Westereng, Bjørge. / Trichoderma reesei CE16 acetyl esterase and its role in enzymatic degradation of acetylated hemicellulose. In: BBA General Subjects. 2014 ; Vol. 1840, No. 1. pp. 516-525.

Bibtex

@article{ccb8a3c6e9f44ac2a0695bf32c3a1b4b,
title = "Trichoderma reesei CE16 acetyl esterase and its role in enzymatic degradation of acetylated hemicellulose",
abstract = "ResultsThe combined action of GH10 xylanase and acetylxylan esterases (AcXEs) leads to formation of neutral and acidic xylooligosaccharides with a few resistant acetyl groups mainly at their non-reducing ends. We show here that these acetyl groups serve as targets for TrCE16 AcE. The most prominent target is the 3-O-acetyl group at the non-reducing terminal Xylp residues of linear neutral xylooligosaccharides or on aldouronic acids carrying MeGlcA at the non-reducing terminus. Deacetylation of the non-reducing end sugar may involve migration of acetyl groups to position 4, which also serves as substrate of the TrCE16 esterase.ConclusionConcerted action of CtGH10 xylanase, an AcXE and TrCE16 AcE resulted in close to complete deacetylation of neutral xylooligosaccharides, whereas substitution with MeGlcA prevents removal of acetyl groups from only a small fraction of the aldouronic acids. Experiments with diacetyl derivatives of methyl β-d-xylopyranoside confirmed that the best substrate of TrCE16 AcE is 3-O-acetylated Xylp residue followed by 4-O-acetylated Xylp residue with a free vicinal hydroxyl group.General significanceThis study shows that CE16 acetyl esterases are crucial enzymes to achieve complete deacetylation and, consequently, complete the saccharification of acetylated xylans by xylanases, which is an important task of current biotechnology.",
author = "Peter Biely and Maria Cziszarava and Agger, {Jane W.} and Xin-Liang Li and Vladimir Puchart and Maria Vranska and Eijsink, {Vincent G.H.} and Bj{\o}rge Westereng",
year = "2014",
doi = "10.1016/j.bbagen.2013.10.008",
language = "English",
volume = "1840",
pages = "516--525",
journal = "B B A - General Subjects",
issn = "0304-4165",
publisher = "Elsevier",
number = "1",

}

RIS

TY - JOUR

T1 - Trichoderma reesei CE16 acetyl esterase and its role in enzymatic degradation of acetylated hemicellulose

AU - Biely, Peter

AU - Cziszarava, Maria

AU - Agger, Jane W.

AU - Li, Xin-Liang

AU - Puchart, Vladimir

AU - Vranska, Maria

AU - Eijsink, Vincent G.H.

AU - Westereng, Bjørge

PY - 2014

Y1 - 2014

N2 - ResultsThe combined action of GH10 xylanase and acetylxylan esterases (AcXEs) leads to formation of neutral and acidic xylooligosaccharides with a few resistant acetyl groups mainly at their non-reducing ends. We show here that these acetyl groups serve as targets for TrCE16 AcE. The most prominent target is the 3-O-acetyl group at the non-reducing terminal Xylp residues of linear neutral xylooligosaccharides or on aldouronic acids carrying MeGlcA at the non-reducing terminus. Deacetylation of the non-reducing end sugar may involve migration of acetyl groups to position 4, which also serves as substrate of the TrCE16 esterase.ConclusionConcerted action of CtGH10 xylanase, an AcXE and TrCE16 AcE resulted in close to complete deacetylation of neutral xylooligosaccharides, whereas substitution with MeGlcA prevents removal of acetyl groups from only a small fraction of the aldouronic acids. Experiments with diacetyl derivatives of methyl β-d-xylopyranoside confirmed that the best substrate of TrCE16 AcE is 3-O-acetylated Xylp residue followed by 4-O-acetylated Xylp residue with a free vicinal hydroxyl group.General significanceThis study shows that CE16 acetyl esterases are crucial enzymes to achieve complete deacetylation and, consequently, complete the saccharification of acetylated xylans by xylanases, which is an important task of current biotechnology.

AB - ResultsThe combined action of GH10 xylanase and acetylxylan esterases (AcXEs) leads to formation of neutral and acidic xylooligosaccharides with a few resistant acetyl groups mainly at their non-reducing ends. We show here that these acetyl groups serve as targets for TrCE16 AcE. The most prominent target is the 3-O-acetyl group at the non-reducing terminal Xylp residues of linear neutral xylooligosaccharides or on aldouronic acids carrying MeGlcA at the non-reducing terminus. Deacetylation of the non-reducing end sugar may involve migration of acetyl groups to position 4, which also serves as substrate of the TrCE16 esterase.ConclusionConcerted action of CtGH10 xylanase, an AcXE and TrCE16 AcE resulted in close to complete deacetylation of neutral xylooligosaccharides, whereas substitution with MeGlcA prevents removal of acetyl groups from only a small fraction of the aldouronic acids. Experiments with diacetyl derivatives of methyl β-d-xylopyranoside confirmed that the best substrate of TrCE16 AcE is 3-O-acetylated Xylp residue followed by 4-O-acetylated Xylp residue with a free vicinal hydroxyl group.General significanceThis study shows that CE16 acetyl esterases are crucial enzymes to achieve complete deacetylation and, consequently, complete the saccharification of acetylated xylans by xylanases, which is an important task of current biotechnology.

U2 - 10.1016/j.bbagen.2013.10.008

DO - 10.1016/j.bbagen.2013.10.008

M3 - Journal article

VL - 1840

SP - 516

EP - 525

JO - B B A - General Subjects

JF - B B A - General Subjects

SN - 0304-4165

IS - 1

ER -

ID: 91954035