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 language | English |
|---|---|
| Pages (from-to) | 121 - 124 |
| Number of pages | 4 |
| Journal | FEBS Letters |
| Volume | 420 |
| Issue number | 2-3 |
| DOIs | |
| Publication status | Published - 1997 |
| MoE publication type | A1 Journal article-refereed |
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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 journal › Article › Scientific › peer-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
Y1 - 1997
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
SP - 121
EP - 124
JO - FEBS Letters
JF - FEBS Letters
SN - 0014-5793
IS - 2-3
ER -