| Literature DB >> 9175871 |
M L Mattinen1, M Linder, A Teleman, A Annila.
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.Entities:
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Year: 1997 PMID: 9175871 DOI: 10.1016/s0014-5793(97)00356-6
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124