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

40 Citations (Scopus)

Abstract

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
Number of pages6
JournalFEBS Letters
Volume407
Issue number3
DOIs
Publication statusPublished - 1997
MoE publication typeA1 Journal article-refereed

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Cellulases
Trichoderma
Cellulose
Relaxation time
Nuclear magnetic resonance spectroscopy
Magnetic Resonance Spectroscopy
cellohexaose
Glucose
Enzymes

Cite this

Mattinen, Maija-Liisa ; Linder, Markus ; Teleman, Anita ; Annila, Arto. / Interaction between cellohexaose and cellulose binding domains from Trichoderma reesei cellulases. In: FEBS Letters. 1997 ; Vol. 407, No. 3. pp. 291 - 296.
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Interaction between cellohexaose and cellulose binding domains from Trichoderma reesei cellulases. / Mattinen, Maija-Liisa (Corresponding Author); Linder, Markus; Teleman, Anita; Annila, Arto.

In: FEBS Letters, Vol. 407, No. 3, 1997, p. 291 - 296.

Research output: Contribution to journalArticleScientificpeer-review

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T1 - Interaction between cellohexaose and cellulose binding domains from Trichoderma reesei cellulases

AU - Mattinen, Maija-Liisa

AU - Linder, Markus

AU - Teleman, Anita

AU - Annila, Arto

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AB - 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.

U2 - 10.1016/S0014-5793(97)00356-6

DO - 10.1016/S0014-5793(97)00356-6

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JF - FEBS Letters

SN - 0014-5793

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