The cellulases endoglucanase I and cellobiohydrolase II of Trichoderma reesei act synergistically to solubilize native cotton cellulose but not to decrease its molecular size

Degradation of cotton cellulose by Trichoderma reesei endoglucanase I (EGI) and cellobiohydrolase II (CBHII) was investigated by analyzing the insoluble cellulose fragments remaining after enzymatic hydrolysis. Changes in the molecular-size distribution of cellulose after attack by EGI, alone and in...

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Bibliographic Details
Published in:Applied and Environmental Microbiology 1996-08, Vol.62 (8), p.2883-2887
Main Authors: Kleman-Leyer, K.M. (The Ohio State University, Columbus, OH.), Siika-aho, M, Teeri, T.T, Kirk, T.K
Format: Article
Language:English
Subjects:
ACTIVIDAD ENZIMATICA
ACTIVITE ENZYMATIQUE
Biological and medical sciences
Biology of microorganisms of confirmed or potential industrial interest
Biotechnology
CELLULASE
CELLULOSE
CELULASA
CELULOSA
Enzymes
Fundamental and applied biological sciences. Psychology
Fungi
GOSSYPIUM
HIDROLASAS
HIDROLISIS
HYDROLASE
HYDROLYSE
Microbiology
Miscellaneous
Mission oriented research
PESO MOLECULAR
POIDS MOLECULAIRE
PURIFICACION
PURIFICATION
SINERGISMO
SOLUBILIDAD
SOLUBILITE
SYNERGISME
TRICHODERMA LONGIBRACHIATUM
Trichoderma reesei
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Summary:Degradation of cotton cellulose by Trichoderma reesei endoglucanase I (EGI) and cellobiohydrolase II (CBHII) was investigated by analyzing the insoluble cellulose fragments remaining after enzymatic hydrolysis. Changes in the molecular-size distribution of cellulose after attack by EGI, alone and in combination with CBHII, were determined by size exclusion chromatography of the tricarbanilate derivatives. Cotton cellulose incubated with EGI exhibited a single major peak, which with time shifted to progressively lower degrees of polymerization (DP; number of glucosyl residues per cellulose chain). In the later stages of degradation (8 days), this peak was eventually centered over a DP of 200 to 300 and was accompanied by a second peak (DP, approximately 15); a final weight loss of 34% was observed. Although CBHII solubilized approximately 40% of bacterial microcrystalline cellulose, the cellobiohydrolase did not depolymerize or significantly hydrolyze native cotton cellulose. Furthermore, molecular-size distributions of cellulose incubated with EGI together with CBHII did not differ from those attacked solely by EGI. However, a synergistic effect was observed in the reducing-sugar production by the cellulase mixture. From these results we conclude that EGI of T. reesei degrades cotton cellulose by selectively cleaving through the microfibrils at the amorphous sites, whereas CBHII releases soluble sugars from the EGI-degraded cotton cellulose and from the more crystalline bacterial microcrystalline cellulose
ISSN:0099-2240
1098-5336
DOI:10.1128/AEM.62.8.2883-2887.1996