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Interaction between cellohexaose and cellulose binding domains from Trichoderma reesei cellulases
Author(s) -
Mattinen Maija-Liisa,
Linder Markus,
Teleman Anita,
Annila Arto
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)00356-6
Subject(s) - trichoderma reesei , cellulase , cellulose , chemistry , trichoderma , biochemistry , microbiology and biotechnology , botany , biology
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 T 2 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.