Journal ArticleDOI
Hydrolysis of cellooligosaccharides by Trichoderma reesei cellobiohydrolases: Experimental data and kinetic modeling
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TLDR
A mathematical model based on a reaction-rate-dependent, reversible loss of active enzyme, interpreted in terms of nonproductive substrate binding, was derived and valid to predict concentration-time course data for the hydrolysis of all oligomeric substrates by CBH I and CBH II very well.About:
This article is published in Enzyme and Microbial Technology.The article was published on 1994-01-01. It has received 68 citations till now. The article focuses on the topics: Trichoderma reesei.read more
Citations
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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
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.
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Bioconversion of forest products industry waste cellulosics to fuel ethanol: a review.
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The three-dimensional crystal structure of the catalytic core of cellobiohydrolase I from Trichoderma reesei.
Christina Divne,Jerry Ståhlberg,Tapani Reinikainen,Laura Ruohonen,Göran Pettersson,J. Knowles,TT Teeri,T.A. Jones +7 more
TL;DR: The structure of the major cellobiohydrolase, CBHI, of the potent cellulolytic fungus Trichoderma reesei has been determined and refined and may account for many of the previously poorly understood macroscopic properties of the enzyme and its interaction with solid cellulose.
References
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Journal ArticleDOI
Three-Dimensional Structure of Cellobiohydrolase II from Trichoderma reesei
TL;DR: The three-dimensional structure of a cellulase, the enzymatic core of CBHII from the fungus Trichoderma reesei reveals an alpha-beta protein with a fold similar to but different from the widely occurring barrel topology first observed in triose phosphate isomerase.
Journal ArticleDOI
Studies of the cellulolytic system of Trichoderma reesei QM 9414. Analysis of domain function in two cellobiohydrolases by limited proteolysis.
Peter Tomme,Herman van Tilbeurgh,Göran Pettersson,Jozef Van Damme,Joël Vandekerckhove,Jonathan Knowles,Tuula T. Teeri,Marc Claeyssens +7 more
TL;DR: The specific activities of the intact enzymes and their cores on two forms of insoluble cellulose (crystalline, amorphous) differentiate the CBH I and CBH II in terms of adsorption and catalytic properties.
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Molecular Cloning of Exo–Cellobiohydrolase I Derived from Trichoderma Reesei Strain L27
Sharon P. Shoemaker,Vicky Schweickart,Martha B. Ladner,David Harrow Gelfand,Shirley Kwok,Kenneth B. Myambo,Michael A. Innis +6 more
TL;DR: The molecular cloning and characterization of the gene encoding exo–cellobiohydrolase I of Trichoderma reesei strain L27 is reported and it is found to contain a 10 bp sequence, CAGCT–GACTG, that is homologous to a sequence necessary for splicing of introns in yeast2.
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Homologous domains in Trichoderma reesei cellulolytic enzymes: gene sequence and expression of cellobiohydrolase II.
TL;DR: A short region of extensive homology is found in all Trichoderma cellulases characterized so far, suggesting that this region is important for cellulose hydrolysis.
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Limited proteolysis of the cellobiohydrolase I from Trichoderma reesei: Separation of functional domains
TL;DR: The results lead to the proposal of a bifunctional organisation of the CBH I: one domain, corresponding to the carboxyterminal, acts as a binding site for insoluble cellulose and the other, localised in the core protein, contains the active (hydrolytic) site.