Interaction between cellohexaose and cellulose binding domains from Trichoderma reesei cellulases

Maija-Liisa Mattinen (Corresponding Author), Markus Linder, Anita Teleman, Arto Annila

Research output: Contribution to journalArticleScientificpeer-review

45 Citations (Scopus)


Most Trichoderma reesei cellulases consist of a catalytic and a cellulose binding domain (CBD) joined by a linker. We have used cellohexaose as a model compound for the glucose chain to investigate the interaction between the soluble enzyme and cellulose. The binding of cellohexaose to family I CBDs was studied by NMR spectroscopy. CBDs cause line broadening effects and decreasing T2 relaxation times for certain cellohexaose resonances, whereas there are no effects in the presence of a mutant which binds weakly to cellulose. Yet it remains uncertain how well the soluble cellooligosaccharide mimics the binding of CBD to the cellulose.

Original languageEnglish
Pages (from-to)291-296
JournalFEBS Letters
Issue number3
Publication statusPublished - 1997
MoE publication typeA1 Journal article-refereed


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