Title : Action of acetylxylan esterase from Trichoderma reesei on acetylated methyl glycosides - Biely_1997_FEBS.Lett_420_121 |
Author(s) : Biely P , Cote GL , Kremnicky L , Greene RV , Tenkanen M |
Ref : FEBS Letters , 420 :121 , 1997 |
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-beta-D-xylopyranoside was deacetylated at positions 2 and 3, yielding methyl 4-O-acetyl-beta-D-xylopyranoside in almost 90% yield. Methyl 2,3-di-O-acetyl beta-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 beta-1,4-linked xylans, the enzyme deacetylates monoacetylated xylopyranosyl residues more readily than di-O-acetylated residues. The T. reesei AcXE attacked acetylated methyl beta-D-glucopyranosides and beta-D-mannopyranosides in a manner similar to the xylopyranosides. |
PubMedSearch : Biely_1997_FEBS.Lett_420_121 |
PubMedID: 9459293 |
Substrate | 2,3,4-tri-O-Ac-Me-beta-Xylp |
Biely P, Cote GL, Kremnicky L, Greene RV, Tenkanen M (1997)
Action of acetylxylan esterase from Trichoderma reesei on acetylated methyl glycosides
FEBS Letters
420 :121
Biely P, Cote GL, Kremnicky L, Greene RV, Tenkanen M (1997)
FEBS Letters
420 :121