Affiliation:
1. 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-β-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).
Publisher
American Society for Microbiology
Subject
Ecology,Applied Microbiology and Biotechnology,Food Science,Biotechnology
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