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Identification of essential cellulase components in the hydrolysis of a steam‐exploded birch substrate 1
Author(s) -
Yu Alex H. C,
Saddler John N.
Publication year - 1995
Publication title -
biotechnology and applied biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.468
H-Index - 70
eISSN - 1470-8744
pISSN - 0885-4513
DOI - 10.1111/j.1470-8744.1995.tb00305.x
Subject(s) - cellulase , hydrolysis , cellulose , chemistry , substrate (aquarium) , chromatofocusing , chromatography , enzymatic hydrolysis , enzyme , biochemistry , organic chemistry , size exclusion chromatography , biology , ecology
To Identify the essential cellulase components responsible for the emdent hydrolysis of crystalline cellulose, cellulase mJxtures reconstituted from purified fractions of cellulase components were used in the hydrolysis of a steamexploded birch substrate. Celluclast, a commerdal cellulase mixture, was fractionated into seven groups according to their pI values by chromatofocusing. Two of the seven groups when acting together were shown to have the same spedfic activity on the birch substrate as the original Celluclast. Furthermore, the synergistic interaction of these two enzyme groups were observed in the hydrolysis of the birch substrate. These two groups of cellulase components were further separated into eight subgroups based on their hydrophobidty by hydrophobic‐ interaction chromatography. From hydrolysis experiments using reconstituted mixtures of these eight subgroups, the high spectfic activity of Celluclast on crystalline substrate was suggested to be the result of the interaction of more than two of these eight component groups. These eight subgroups of cellulase components were shown to include celloblohydrolase I, cellobiohydrolase II and as yet, unidentified endoglucanases.