Interaction between cellohexaose and cellulose binding domains from Trichoderma reesei cellulases

Maija-Liisa Mattinen; Markus Linder; Anita Teleman; Arto Annila

doi:10.1016/S0014-5793(97)00356-6

Interaction between cellohexaose and cellulose binding domains from Trichoderma reesei cellulases

Maija-Liisa Mattinen^*
, Markus Linder
, Anita Teleman
, Arto Annila

^*Corresponding author for this work

VTT Technical Research Centre of Finland

VTT (former employee or external)

Research output: Contribution to journal › Article › Scientific › peer-review

51 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 language	English
Pages (from-to)	291-296
Journal	FEBS Letters
Volume	407
Issue number	3
DOIs	https://doi.org/10.1016/S0014-5793(97)00356-6
Publication status	Published - 1997
MoE publication type	A1 Journal article-refereed

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title = "Interaction between cellohexaose and cellulose binding domains from Trichoderma reesei cellulases",

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.",

author = "Maija-Liisa Mattinen and Markus Linder and Anita Teleman and Arto Annila",

note = "Project code: KET3116",

year = "1997",

doi = "10.1016/S0014-5793(97)00356-6",

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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

N1 - Project code: KET3116

PY - 1997

Y1 - 1997

N2 - 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.

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

M3 - Article

SN - 0014-5793

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SP - 291

EP - 296

JO - FEBS Letters

JF - FEBS Letters

IS - 3

ER -

Interaction between cellohexaose and cellulose binding domains from Trichoderma reesei cellulases

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