Isolation, purification, and properties of the exocellulase from Sporotrichum (Chrysosporium) thermophile
Fracheboud, D.; Canevascini, G.
Enzyme and Microbial Technology 11(4): 220-229
1989
ISSN/ISBN: 0141-0229 DOI: 10.1016/0141-0229(89)90096-3
Accession: 001872303
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The principle exocellulase component produced by S. thermophile [Myceliophthora thermophila] during growth on cellulose was isolated by ammonium sulfate precipitation, ion exchange chromatography, and adsorption-desorption on hydroxylapatite. The purified enzyme was homogeneous, very heat-resistant, and had a low pH opt. (3.5) on amorphous cellulose. Its activity was not affected by various cations and was only slightly inhibited by sulfhydryl reagents, though it was inhibited by ferric ions. The evidence of reactivity and mode of action on various substrates suggested that the isolated enzyme was a cellobiohydrolase.