Separation of the cellulolytic system of Trichoderma viride-reesei mutant using medium pressure liquid chromatography and characterization of a new exo-cellobiohydrolase*
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1399-3011.1984.tb02738.x/fullpdf
Reference31 articles.
1. The Mechanism of Enzymatic Cellulose Degradation. Purification of a Cellulolytic Enzyme from Trichoderma viride Active on Highly Ordered Cellulose
2. Enzymatic Studies on a Cellulase System of Trichoderma viride
3. The Mechanism of Enzymatic Cellulose Degradation. Purification and Some Properties of Two Different 1,4-beta-Glucan Glucanohydrolases from Trichoderma viride
4. Structural characterization of a glycoprotein cellulase, 1,4-β-d-glucan cellobiohydrolase C from Trichoderma viride
5. Characterization of endo-1,4-β-d-glucanases purified from Trichoderma viride
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1. Microbial Cellulases: Protein Architecture, Molecular Properties, and Biosynthesis;Advances in Applied Microbiology;1995
2. Isolation, purification, and properties of the exocellulase from Sporotrichum (Chrysosporium) thermophile;Enzyme and Microbial Technology;1989-04
3. Ion-exchange derivatives of spheron;Journal of Chromatography A;1988-05
4. Chapter 15 Bibliography;Journal of Chromatography Library;1988
5. Chapter 8 Enzymes;Journal of Chromatography Library;1988
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