Abstract
The endoglucanase I (EGI) and the cellobiohydrolase I (CBHI) of the filamentous fungus Trichoderma reesei form a homologous pair of cellulolytic enzymes which nevertheless have different modes of action, We show here that the action of CBHI on bacterial microcrystalline cellulose results in efficient solubilisation but only a slow decrease in its degree of polymerisation. In contrast, the action of EGI results in a rapid decrease of the degree of polymerisation but less efficient overall solubilisation of the substrate. CBHI alone was practically inactive toward cotton which has a high initial degree of polymerisation and a complex morphology. EGI rapidly reduced the degree of polymerisation of cotton, and slowly solubilised part of it Working synergistically, EGI and CBHI solubilised cotton more rapidly and to a greater extent than EGI alone. Our data are consistent with the exoglucanase nature of CBHI and also provide some evidence supporting its processive mode of action.
Original language | English |
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Pages (from-to) | 885-892 |
Number of pages | 8 |
Journal | EUROPEAN JOURNAL OF BIOCHEMISTRY |
Volume | 251 |
Issue number | 3 |
Publication status | Published - 1 Feb 1998 |
MoE publication type | A1 Journal article-refereed |
Keywords
- cellobiohydrolase
- crystalline cellulose
- endoglucanase
- size-exclusion chromatography
- synergy
- CELLOBIOHYDROLASE-I
- CRYSTALLINE CELLULOSE
- BINDING DOMAIN
- ENZYMATIC-HYDROLYSIS
- CELLULASES
- SYNERGISM
- ADSORPTION
- GENES
- MECHANISM
- FIMI