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Journal ArticleDOI

Synergism of Cellulases from Trichoderma reesei in the Degradation of Cellulose

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TLDR
In this article, the action of cellobiohydrolases I and II (CBHI and CBHII) and EGI and EGII were evaluated against various substrates, including cellulose microcrystals and carboxy-methyl cellulose derivative.
Abstract
The action of cellobiohydrolases I and II (CBHI and CBHII) and endoglucanases I and II (EGI and EGII) purified from Tri-choderma reesei was evaluated against various substrates. CBHI degraded the β-D-glucan from barley in a typical endo pattern. With cellulose substrates, the synergism between CBHI and endoglucanase I or II depended on the structural and ultrastructural features of the substrate. This effect, unrelated to endo-exo cooperation, was found with substrates of intermediate crystallinity whereas weak or no synergism was recorded with cellulose microcrystals or the soluble carboxy-methyl cellulose derivative. Synergistic degradation of cellulose was also recorded with mixtures of CBHI and CBHII. On the other hand, synergism between endoglucanases and CBHII followed the pattern expected for an endo-exo cooperation. These results presented support evidence for multiple types of cooperation between the cellulolytic enzymes.

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Journal ArticleDOI

Microbial cellulose utilization: fundamentals and biotechnology.

TL;DR: A concluding discussion identifies unresolved issues pertaining to microbial cellulose utilization, suggests approaches by which such issues might be resolved, and contrasts a microbially oriented cellulose hydrolysis paradigm to the more conventional enzymatically oriented paradigm in both fundamental and applied contexts.
Journal ArticleDOI

Toward an aggregated understanding of enzymatic hydrolysis of cellulose: noncomplexed cellulase systems.

TL;DR: It is suggested that it is timely to revisit and reinvigorate functional modeling of cellulose hydrolysis and that this would be highly beneficial if not necessary in order to bring to bear the large volume of information available on cellulase components on the primary applications that motivate interest in the subject.
Journal ArticleDOI

Outlook for cellulase improvement: screening and selection strategies.

TL;DR: In this paper, the authors review quantitative cellulase activity assays using soluble and insoluble substrates, and focus on their advantages and limitations, and hypothesize that continuous culture using insoluble cellulosic substrates could be a powerful selection tool for enriching beneficial cellulase mutants from the large library displayed on the cell surface.
Journal ArticleDOI

Substrate and Enzyme Characteristics that Limit Cellulose Hydrolysis

TL;DR: This present review is not intended to conclusively answer what factors control polysaccharide biodegradation, but to serve as an overview illustrating some of the potential enzymatic and structural limitations that invariably influence the complete hydrolysis of lignocellulosicpolysaccharides.
References
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Journal ArticleDOI

The structure of native cellulose

TL;DR: In this paper, the X-ray diffraction data for specimens from the sea alga Valonia ventricosa was used to show a preference for a parallel chain structure with specific chain polarity with respect to the c axis.
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The Effect of Pore Size Distribution on the Rate of Enzymatic Hydrolysis of Cellulosic Substrates

TL;DR: Hard and softwoods were pretreated by mild acid hydrolysis and their pore size distribution determined, finding that the initial rate of Hydrolysis using cellulase from Trichoderma reesei is linearly correlated with the pore volume of the substrate accessible to a nominal diameter representative of the size of the cellulase.
Journal ArticleDOI

Process considerations in the enzymatic hydrolysis of biomass

TL;DR: The processes by which cellulases hydrolyse cellulose are a function of substrate reactivity as well as enzyme activity, and the two must be considered together if an accurate description of biomass saccharification is to be developed as discussed by the authors.
Journal ArticleDOI

The Mechanism of Enzymatic Cellulose Degradation

TL;DR: Two enzymes isolated from a commercial cellulase preparation derived from culture filtrates of the fungus Trichoderma viride were active in releasing free fibers from filter-paper and indicated a homogeneous protein.
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