Open Accessβ‐Glucosidase from Trichoderma reesei
Author(s) -
CHIRICO William J.,
BROWN Ross D.
Publication year - 1987
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1987.tb11447.x
Subject(s) - trichoderma reesei , cello , chemistry , substrate (aquarium) , oligosaccharide , stereochemistry , enzyme , biochemistry , biology , physics , cellulase , ecology , piano , acoustics
To determine the mode of action of the β‐glucosidase from Trichoderma reesei a method was developed for synthesizing [1‐ 3 H]cello‐oligosaccharides with specific radioactivities of approximately 3000 Ci/mol. The β‐glucosidase removed glucosyl residues from the non‐reducing end of the [1‐ 3 H]cello‐oligosaccharides in a multiple attack mode with little tendency to attack the substrates repetitively. Values of K m were lower for longer cello‐oligosaccharides, whereas values of V remained essentially constant. A subsite map, constructed using values of V/K m for the cello‐oligosaccharides, showed that the substrate‐binding region comprises primarily three subsites.