Department of Microbiology and Public Health, Michigan State University, East Lansing, Michigan 48824.
Appl Environ Microbiol. 1985 Mar;49(3):622-6. doi: 10.1128/aem.49.3.622-626.1985.
Crude extracts of the anaerobic, cellulolytic protozoan Trichomitopsis termopsidis possessed endo-beta-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 degrees 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).
厌氧纤维素分解原生动物 Trichomitopsis termopsidis 的粗提取物具有内切-β-1,4-葡聚糖酶和纤维二糖酶活性，这分别通过对羧甲基纤维素和纤维二糖的水解作用得到证明。细胞提取物还水解微晶纤维素。微晶纤维素的水解显示在 pH 5 和 30°C 时具有最佳活性，释放的唯一产物是葡萄糖。T. termopsidis 的纤维素酶活性似乎完全与细胞相关。还检测到针对花旗松木粉、木聚糖、淀粉和蛋白质的水解活性，但对几丁质没有活性。根据这种原生动物（食木白蚁的后肠）的自然栖息地，讨论了这些酶在 T. termopsidis 营养中的重要性。
