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Synergism of isoenzymes of cellobiohydrolase I and II of trichoderma reesei in hydrolysis of amorphous cellulose

โœ Scribed by H.-J. Heithz; K. Witte; A. Wartenberg

Book ID
102684061
Publisher
John Wiley and Sons
Year
1991
Tongue
English
Weight
524 KB
Volume
11
Category
Article
ISSN
0138-4988

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โœฆ Synopsis

Decompositions of amorphous cellulose induced by cellulases of Trichoderma reesei were evaluated from gradients at zero time of exponential functions which were fitted to nephelometrically measured values of turbidity of incubated solutions of cellulose [turbidity = A x exp ( B x t ) + C [ A , B, C = constant?, t = time]]. Synergistic enhancements of decomposition of amorphous cellulose resulted in the range of 300 p-c. whenever of the two isoenzymes of cellobiohydrolase I of Trichoderma reesei (CBH I, being an exo-glucanase) one was incubatcd together with one of the isoenzymes of CBH I1 (being really an endo-glucanase). Accessibility of amorphous cellulose to enzymatic decomposition being calculated from the fitted function by the term ( A / ( A + C)) x

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Microcrystalline cellulose (10 g/L Avicel) was hydrolysed by two major cellulases, cellobiohydrolase I (CBH I) and endoglucanase II (EG II), of Trichoderma reesei. Two types of experiments were performed, and in both cases the enzymes were added alone and together, in equimolar mixtures. In time cou

Isolation and purification of isoenzymes
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Five cellulases were fractionated from a commercial cellulase preparation (CelluclastTx). Two isoenzymes of cellobiohydrolase I (CBHI) (PI = 4.1) could be proved to be real exo-glucanases due t o their activity towards MU (= methylumbel1iferyl)-lactoside being inhibited b y cellobiose (5 mM) and due