Open AccessFormation of cross‐fractures in cellulose microfibril structure by an endoglucanase‐cellobiohydrolase complex from Trichoderma reesei
Author(s) -
Sprey Benno,
Bochem HansPeter
Publication year - 1993
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1993.tb05970.x
Subject(s) - cellulase , microfibril , trichoderma reesei , cellulose , isoelectric point , chemistry , cell wall , biochemistry , enzyme
An endoglucanase‐cellobiohydrolase from Trichoderma reesei culture fluids was purified by means of preparative isoelectric focusing. The cellulase complex had a common apparent isoelectric point (p I ) of 3.8. Beyond this p I , the electrophoretic mobilities of endoglucanase and cellobiohydrolase were different under conditions of titration curves. The effect of this endoglucanase‐cellobiohydronalase complex on Sinapis cellulose microfibril ultranstructure was observed by transmission electron microscopy after metal shadowing of the specimen. By the action of this cellulase complex, the microfibril structure was converted into an amorphous form of cellulose. Moreover, the hydrolase complex induced visible cross‐fractures within the cellulose microfibril structure. The mean cellulose microfibril lenght of 1.2 μm was reduced to 0.9 μm in the presence (12 h) of this cellulase complex by the formation of shorter microfibril fragments.