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. 1997 May 5;407(3):291-6.
doi: 10.1016/s0014-5793(97)00356-6.

Interaction between cellohexaose and cellulose binding domains from Trichoderma reesei cellulases

M L Mattinen  1 , M Linder, A Teleman, A Annila
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Free article

Interaction between cellohexaose and cellulose binding domains from Trichoderma reesei cellulases

M L Mattinen et al. FEBS Lett. .
Free article

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.

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