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Eberhart, Bruce (University of North Carolina, Greensboro),David F. Cross, and Lewis R. Chase . β-Glucosidase system ofNeuspora crassa . I. β-Glucosidase and cellulose activities of mutant and wild-type strains. J. Bacteriol.87: 761–770. 1964.—A mutant strain,gluc-1 , ofNeurospora crassa was isolated and characterized by its low level of β-glucosidase activity. The mutant was selected by testing irradiated colonies for extracellular β-glucosidase activity. Strains containing thegluc-1 gene were also visibly detected by their reduced ability to destroy esculin in their growth media. The mutant strain grew at wild-type rates with cellobiose or carboxymethylcellulose as carbon sources. This auxotrophic similarity with wild type is explained by the presence of at least two β-glucosidases (and possibly two cellulases) inNeurospora that act complementarily. The thermolabile β-glucosidase was destroyed after 1 min of incubation at 60 C. This enzyme was present in mycelia but absent in conidial extracts. A second β-glucosidase that is comparatively stable at 60 C was present in both mycelia and conidia. A partial separation of these enzymes was achieved with ammonium fractionation of mycelial extracts ofgluc-1 and wild-type strains. Thermolabile β-glucosidase and cellulase activity appear not to be affected by thegluc-1 mutation, whereas the thermostable glucosidase is greatly reduced ingluc-1 strains.

β-GLUCOSIDASE SYSTEM OF NEUROSPORA CRASSA I. β-