Abstract
The anaerobic rumen fungus Piromonas communis, when cultured on cotton fibre as the carbon source, produces an extracellular cellulase that is capable of solubilizing “crystalline” hydrogen-bond-ordered cellulose, in the form of the cotton fibre, at a rate that is greater than that of any other cellulases reported in the literature hitherto. The cell-free culture fluid is also very rich in xylan-degrading enzymes. The activity towards crystalline cellulose resides in a high-molecular-mass (approximately 700–1000 kDa) component (so-called crystalline-cellulose-solubilizing component, CCSC) that comprises endo (1 → 4)-β-D-gluconase (carboxymethylcellulase), β-D-glucosidase and another enzyme that appears to be important for the breakdown of hydrogen-bond-ordered cellulose. The CCSC is associated with only a small amount of the endo-(1 → 4)-β-D-glucanase (1.9%), β-D-glucosidase (0.7%) and protein (0.5%) found in the crude cell-free cellulase preparation. The CCSC, unlike the bulk of the endo-(1 → 4)-β-D-glucanase and β-D-glucosidase, is very strongly absorbed on the microcrystalline cellulose, Avicel.
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Wood, T.M., Wilson, C.A. Studies on the capacity of the cellulase of the anaerobic rumen fungus Piromonas communis P to degrade hydrogen bond-ordered cellulose. Appl Microbiol Biotechnol 43, 572–578 (1995). https://doi.org/10.1007/BF00218468
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DOI: https://doi.org/10.1007/BF00218468