SUMMARY: Conidia of QM 9414 are able to degrade crystalline cellulose to glucose in the absence of protein synthesis, indicating the presence of a cellulase enzyme system. Measurement of enzyme activities revealed the presence of several glycanases and glycosidases. The cellulase enzyme system appeared irrespective of the conditions applied to induce conidiation. Removal of the endo-1,4-β-glucanase from the cellulase system could be achieved by treatment of conidia with β-octylglucoside or Triton X-100. Conidia treated in this way grew poorly on cellulose but well on glycerol. The endo-1,4-β-glucanase released from conidia by β-octylglucoside appeared as a single enzyme upon SDS-PAGE/immunoblotting with an apparent molecular mass of 68 kDa, an isoelectric point of 4.8-5.3, and a pH optimum between pH 4-6. These properties were similar to endo-1,4-β-glucanase I purified from culture filtrates of cellulose-grown Thermostability of the released enzyme was, however, lower than that of endo-1,4-β-glucanase I. Germination of conidia in a medium containing glycerol as a carbon source led to a loss of endo-1,4-β-glucanase activity which paralleled the decrease in the number of ungerminated conidia.


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