Action of acetylxylan esterase from Trichoderma reesei on acetylated methyl glycosides

Peter Biely (Corresponding Author), G. Cote, L. Kremnicky, R. Greene, Maija Tenkanen

Research output: Contribution to journalArticleScientificpeer-review

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Abstract

Substrate specificity of purified acetylxylan esterase (AcXE) from Trichoderma reesei was investigated on partially and fully acetylated methyl glycopyranosides. Methyl 2,3,4-tri-O-acetyl-β-d-xylopyranoside was deacetylated at positions 2 and 3, yielding methyl 4-O-acetyl-β-d-xylopyranoside in almost 90% yield. Methyl 2,3-di-O-acetyl β-d-xylopyranoside was deacetylated at a rate similar to the fully acetylated derivative. The other two diacetates (2,4- and 3,4-), which have a free hydroxyl group at either position 3 or 2, were deacetylated one order of magnitude more rapidly. Thus the second acetyl group is rapidly released from position 3 or 2 after the first acetyl group is removed from position 2 or 3. The results strongly imply that in degradation of partially acetylated β-1,4-linked xylans, the enzyme deacetylates monoacetylated xylopyranosyl residues more readily than di-O-acetylated residues. The T. reesei AcXE attacked acetylated methyl β-d-glucopyranosides and β-d-mannopyranosides in a manner similar to the xylopyranosides.

Original languageEnglish
Pages (from-to)121 - 124
Number of pages4
JournalFEBS Letters
Volume420
Issue number2-3
DOIs
Publication statusPublished - 1997
MoE publication typeA1 Journal article-refereed

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acetylxylan esterase
Trichoderma
Glycosides
Xylans
Mannose
Substrate Specificity
Hydroxyl Radical
Derivatives
Degradation
Substrates
Enzymes

Cite this

Biely, P., Cote, G., Kremnicky, L., Greene, R., & Tenkanen, M. (1997). Action of acetylxylan esterase from Trichoderma reesei on acetylated methyl glycosides. FEBS Letters, 420(2-3), 121 - 124. https://doi.org/10.1016/S0014-5793(97)01500-7
Biely, Peter ; Cote, G. ; Kremnicky, L. ; Greene, R. ; Tenkanen, Maija. / Action of acetylxylan esterase from Trichoderma reesei on acetylated methyl glycosides. In: FEBS Letters. 1997 ; Vol. 420, No. 2-3. pp. 121 - 124.
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abstract = "Substrate specificity of purified acetylxylan esterase (AcXE) from Trichoderma reesei was investigated on partially and fully acetylated methyl glycopyranosides. Methyl 2,3,4-tri-O-acetyl-β-d-xylopyranoside was deacetylated at positions 2 and 3, yielding methyl 4-O-acetyl-β-d-xylopyranoside in almost 90{\%} yield. Methyl 2,3-di-O-acetyl β-d-xylopyranoside was deacetylated at a rate similar to the fully acetylated derivative. The other two diacetates (2,4- and 3,4-), which have a free hydroxyl group at either position 3 or 2, were deacetylated one order of magnitude more rapidly. Thus the second acetyl group is rapidly released from position 3 or 2 after the first acetyl group is removed from position 2 or 3. The results strongly imply that in degradation of partially acetylated β-1,4-linked xylans, the enzyme deacetylates monoacetylated xylopyranosyl residues more readily than di-O-acetylated residues. The T. reesei AcXE attacked acetylated methyl β-d-glucopyranosides and β-d-mannopyranosides in a manner similar to the xylopyranosides.",
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Biely, P, Cote, G, Kremnicky, L, Greene, R & Tenkanen, M 1997, 'Action of acetylxylan esterase from Trichoderma reesei on acetylated methyl glycosides', FEBS Letters, vol. 420, no. 2-3, pp. 121 - 124. https://doi.org/10.1016/S0014-5793(97)01500-7

Action of acetylxylan esterase from Trichoderma reesei on acetylated methyl glycosides. / Biely, Peter (Corresponding Author); Cote, G.; Kremnicky, L.; Greene, R.; Tenkanen, Maija.

In: FEBS Letters, Vol. 420, No. 2-3, 1997, p. 121 - 124.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Action of acetylxylan esterase from Trichoderma reesei on acetylated methyl glycosides

AU - Biely, Peter

AU - Cote, G.

AU - Kremnicky, L.

AU - Greene, R.

AU - Tenkanen, Maija

PY - 1997

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N2 - Substrate specificity of purified acetylxylan esterase (AcXE) from Trichoderma reesei was investigated on partially and fully acetylated methyl glycopyranosides. Methyl 2,3,4-tri-O-acetyl-β-d-xylopyranoside was deacetylated at positions 2 and 3, yielding methyl 4-O-acetyl-β-d-xylopyranoside in almost 90% yield. Methyl 2,3-di-O-acetyl β-d-xylopyranoside was deacetylated at a rate similar to the fully acetylated derivative. The other two diacetates (2,4- and 3,4-), which have a free hydroxyl group at either position 3 or 2, were deacetylated one order of magnitude more rapidly. Thus the second acetyl group is rapidly released from position 3 or 2 after the first acetyl group is removed from position 2 or 3. The results strongly imply that in degradation of partially acetylated β-1,4-linked xylans, the enzyme deacetylates monoacetylated xylopyranosyl residues more readily than di-O-acetylated residues. The T. reesei AcXE attacked acetylated methyl β-d-glucopyranosides and β-d-mannopyranosides in a manner similar to the xylopyranosides.

AB - Substrate specificity of purified acetylxylan esterase (AcXE) from Trichoderma reesei was investigated on partially and fully acetylated methyl glycopyranosides. Methyl 2,3,4-tri-O-acetyl-β-d-xylopyranoside was deacetylated at positions 2 and 3, yielding methyl 4-O-acetyl-β-d-xylopyranoside in almost 90% yield. Methyl 2,3-di-O-acetyl β-d-xylopyranoside was deacetylated at a rate similar to the fully acetylated derivative. The other two diacetates (2,4- and 3,4-), which have a free hydroxyl group at either position 3 or 2, were deacetylated one order of magnitude more rapidly. Thus the second acetyl group is rapidly released from position 3 or 2 after the first acetyl group is removed from position 2 or 3. The results strongly imply that in degradation of partially acetylated β-1,4-linked xylans, the enzyme deacetylates monoacetylated xylopyranosyl residues more readily than di-O-acetylated residues. The T. reesei AcXE attacked acetylated methyl β-d-glucopyranosides and β-d-mannopyranosides in a manner similar to the xylopyranosides.

U2 - 10.1016/S0014-5793(97)01500-7

DO - 10.1016/S0014-5793(97)01500-7

M3 - Article

VL - 420

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SN - 0014-5793

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