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Possible adsorption sites of cellulases on crystalline cellulose
Author(s) -
Henrissat Bernard,
Vigny Béatrice,
Buleon Alain,
Perez Serge
Publication year - 1988
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 - 10.1016/0014-5793(88)80726-9
Subject(s) - cellulase , trichoderma reesei , glycosidic bond , cellulose , adsorption , chemistry , hydrolysis , enzymatic hydrolysis , glycoside hydrolase , enzyme , crystallography , chemical engineering , biochemistry , organic chemistry , engineering
The possible adsorption sites of cellulases on crystalline cellulose were investigated by molecular graphic representation of a crystal of cellulose and estimation of the accessibility of the various glycosidic bonds to enzymatic attack. The results show that only certain glycosidic bonds of certain surface cellulose chains are susceptible to enzymatic hydrolysis. These preferential sites correlate well with previous electron microscopy observations of the adsorption sites of 1,4‐β‐D‐glucan cellobiohydrolase I (CBHI) from Trichoderma reesei on Valonia cellulose.