Effect of side groups on the action of β-xylosidase from Trichoderma reesei against substituted xylo-oligosaccharides

Maija Tenkanen (Corresponding Author), Elina Luonteri, Anita Teleman

Research output: Contribution to journalArticleScientificpeer-review

35 Citations (Scopus)

Abstract

The action of β-xylosidase from Trichoderma reesei against different substituted xylo-oligosaccharides was studied. The enzyme cleaved off all unsubstituted xylose units from the non-reducing end of 1,2-linked uronic acid substituted xylo-oligosaccharides. Surprisingly, an l-arabinofuranosyl group linked α-1,3 to the xylopyranosyl ring was found to protect the β-1,4-xylosidic linkage before the substituted xylose unit from being cleaved by the β-xylosidase. Most probably the 1,3-linked substituent sterically hinders the hydrolysis. According to the results of the present work, β-xylosidase of T. reesei is not able to remove all unsubstituted xylose units from the non-reducing end of substituted xylo-oligosaccharides, as had been believed previously.
Original languageEnglish
Pages (from-to)303-306
JournalFEBS Letters
Volume399
Issue number3
DOIs
Publication statusPublished - 1996
MoE publication typeA1 Journal article-refereed

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