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Appl Environ Microbiol. 1985 March; 49(3): 622-626
Copyright © 1985, American Society for Microbiology. All Rights Reserved.
Department of Microbiology and Public Health, Michigan State University, East Lansing, Michigan 48824
ABSTRACT
Crude extracts of the anaerobic, cellulolytic protozoan Trichomitopsis termopsidis possessed endo-ß-1,4-glucanase and cellobiase activities, as evidenced by hydrolytic action on carboxymethyl cellulose and cellobiose, respectively. Cell extracts also hydrolyzed microcrystalline cellulose. Hydrolysis of microcrystalline cellulose displayed optima at pH 5 and at 30°C, and glucose was the sole product liberated. Cellulolytic activities of T. termopsidis appeared to be entirely cell associated. Hydrolytic activity was also detected against Douglas fir wood powder, xylan, starch, and protein, but not chitin. The importance of these enzymes in the nutrition of T. termopsidis is discussed in terms of the natural habitat of this protozoan (the hindgut of wood-eating termites).
This is journal article no. 11412 from the Michigan Agricultural Experiment Station.
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