Comparison of catalytic properties of acetyl xylan esterases from three carbohydrate esterase families

Maija Tenkanen, Jaime Eyzaguirre, Riitta Isoniemi, Craig B. Faulds, Peter Biely

Research output: Chapter in Book/Report/Conference proceedingChapter or book articleProfessional

Abstract

Most natural hemicelluloses are acetylated. Some xylans carryalso esterified phenolic acid side groups. Carbohydrate-actingesterases (CE) have been recently classified according tostructural similarities into several CE families. However, thisclassification does not necessarily predict the substrate specificity of these enzymes. In this work eight different hemicellulose-acting esterases from three different esterase families were studied. The substrate specificities and the modes of action of esterases from different families varied significantly. Some esterases acted on a wide range of substrates, i.e. on acetyl and on feruloyl groups in xylan and on acetyl groups in glucomannan, while others were strictly specific for one substrate. The CE family 1 and 5 esterases deacetylated first at the position 3 and 2, respectively, whereas the CE family 4 esterase performed a fast double deacetylation at both positions in methyl per-O-acetyl-β-D-xylopyranoside.
Original languageEnglish
Title of host publicationApplications of Enzymes to Lignocellulosics
EditorsShawn D. Mansfield, John N. Saddler
Place of PublicationWashington, DC
PublisherAmerican Chemical Society
Chapter13
Pages211-229
ISBN (Electronic)9780841219601
ISBN (Print)0-8412-3831-6
DOIs
Publication statusPublished - 2003
MoE publication typeNot Eligible

Publication series

NameACS Symposium Series
PublisherACS
Volume855

Fingerprint

xylan
esterases
carbohydrates
substrate specificity
hemicellulose
phenolic acids
mechanism of action
enzymes

Cite this

Tenkanen, M., Eyzaguirre, J., Isoniemi, R., Faulds, C. B., & Biely, P. (2003). Comparison of catalytic properties of acetyl xylan esterases from three carbohydrate esterase families. In S. D. Mansfield, & J. N. Saddler (Eds.), Applications of Enzymes to Lignocellulosics (pp. 211-229). Washington, DC: American Chemical Society. ACS Symposium Series, Vol.. 855 https://doi.org/10.1021/bk-2003-0855.ch013
Tenkanen, Maija ; Eyzaguirre, Jaime ; Isoniemi, Riitta ; Faulds, Craig B. ; Biely, Peter. / Comparison of catalytic properties of acetyl xylan esterases from three carbohydrate esterase families. Applications of Enzymes to Lignocellulosics. editor / Shawn D. Mansfield ; John N. Saddler. Washington, DC : American Chemical Society, 2003. pp. 211-229 (ACS Symposium Series, Vol. 855).
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Tenkanen, M, Eyzaguirre, J, Isoniemi, R, Faulds, CB & Biely, P 2003, Comparison of catalytic properties of acetyl xylan esterases from three carbohydrate esterase families. in SD Mansfield & JN Saddler (eds), Applications of Enzymes to Lignocellulosics. American Chemical Society, Washington, DC, ACS Symposium Series, vol. 855, pp. 211-229. https://doi.org/10.1021/bk-2003-0855.ch013

Comparison of catalytic properties of acetyl xylan esterases from three carbohydrate esterase families. / Tenkanen, Maija; Eyzaguirre, Jaime; Isoniemi, Riitta; Faulds, Craig B.; Biely, Peter.

Applications of Enzymes to Lignocellulosics. ed. / Shawn D. Mansfield; John N. Saddler. Washington, DC : American Chemical Society, 2003. p. 211-229 (ACS Symposium Series, Vol. 855).

Research output: Chapter in Book/Report/Conference proceedingChapter or book articleProfessional

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AU - Biely, Peter

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AB - Most natural hemicelluloses are acetylated. Some xylans carryalso esterified phenolic acid side groups. Carbohydrate-actingesterases (CE) have been recently classified according tostructural similarities into several CE families. However, thisclassification does not necessarily predict the substrate specificity of these enzymes. In this work eight different hemicellulose-acting esterases from three different esterase families were studied. The substrate specificities and the modes of action of esterases from different families varied significantly. Some esterases acted on a wide range of substrates, i.e. on acetyl and on feruloyl groups in xylan and on acetyl groups in glucomannan, while others were strictly specific for one substrate. The CE family 1 and 5 esterases deacetylated first at the position 3 and 2, respectively, whereas the CE family 4 esterase performed a fast double deacetylation at both positions in methyl per-O-acetyl-β-D-xylopyranoside.

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BT - Applications of Enzymes to Lignocellulosics

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Tenkanen M, Eyzaguirre J, Isoniemi R, Faulds CB, Biely P. Comparison of catalytic properties of acetyl xylan esterases from three carbohydrate esterase families. In Mansfield SD, Saddler JN, editors, Applications of Enzymes to Lignocellulosics. Washington, DC: American Chemical Society. 2003. p. 211-229. (ACS Symposium Series, Vol. 855). https://doi.org/10.1021/bk-2003-0855.ch013