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Separation and characterization of the complexes constituting the cellulolytic enzyme system of Clostridium thermocellum (1986)

Hon-nami, Koyu ; Coughlan, Michael P. ; Hon-nami, Hiromi ; [et al.]

Springer

Archives of microbiology 145 (1986), S. 13-19

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ISSN: 1432-072X

Keywords: Clostridium thermocellum ; Cellulose ; Cellobiose ; Cellulase ; Cellulolytic enzyme complex ; Endo-β-glucanase

Source: Springer Online Journal Archives 1860-2000

Topics: Biology

Notes: Abstract Clostridium thermocellum, strain JW20 (ATCC 31449) when growing in cellulose produces a cellulolytic enzyme system, that at the early stage of the fermentation is largely bound to the substrate. As cellulose is consumed the bound enzyme is released as free enzyme to the culture fluid. The bound enzyme fraction extracted with distilled water from the cellulose contains two major components, a large complex (Mr≃100×106) and a small complex Mr≃4.5×106) which were separated by gel filtration and sucrose solved by affinity chromatography into a complex that binds to the column and into a non-bindable mixture of proteins. All four fractions have endo-β-glucanase activity but only the two bound complexes and the free bindable complex hydrolyze crystalline cellulose with cellobiose as the main product. These three complexes are qualitatively similar in that they each contain about 20 different polypeptides (Mr values from 45,000 to 200,000) of which about ten are major components. However, the relative amounts of some of the peptides in the complexes differ. At least four polypeptides of the complexes have endo-β-glucanase activity.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/BF00413021

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Sorption of Talaromyces emersonii cellulase on cellulosic substrates (1983)

Moloney, Aidan ; Coughlan, Michael P.

New York, NY [u.a.] : Wiley-Blackwell

Biotechnology and Bioengineering 25 (1983), S. 271-280

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ISSN: 0006-3592

Keywords: Chemistry ; Biochemistry and Biotechnology

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology

Notes: The sorption characteristics of the cellulase system of Talaromyces emersonii on various cellulosic substrates were examined. Analysis of reaction mixture supernatants by electrophoresis and enzyme assay showed that all components of the cellulase system were rapidly adsorbed by cellulose and then gradually returned to the liquid phase as the hydrolysis of the substrate progressed. The extent of adsorption in the rapid phase was influenced by pH, temperature, the nature of the substrate, and its concentration.

Additional Material: 5 Ill.