The relationship between thermal stability and pH optimum studied with wild-type and mutant Trichoderma reesei cellobiohydrolase Cel7A
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1046/j.1432-1033.2003.03431.x/fullpdf
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3. Engineering of a glycosidase Family 7 cellobiohydrolase to more alkaline pH optimum: the pH behaviour of Trichoderma reesei Cel7A and its E223S/A224H/L225V/T226A/D262G mutant;Becker;Biochem. J.,2001
4. The three-dimensional crystal structure of the catalytic core of cellobiohydrolase I from Trichoderma reesei;Divne;Science,1994
5. High-resolution crystal structures reveal how a cellulose chain is bound in the 50 �� long tunnel of cellobiohydrolase I from Trichoderma reesei;Divne;J. Mol. Biol.,1998
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