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. 1970 Feb;101(2):408–417. doi: 10.1128/jb.101.2.408-417.1970

Localization of the β-Glucosidases in Neurospora crassa

Bruce M Eberhart 1, Reta S Beck 1
PMCID: PMC284921  PMID: 5413819

Abstract

The β-glucosidases (EC 3.2.1.21) of Neurospora crassa were studied with respect to their location in conidia and young mycelia. Aryl-β-glucosidase of conidia was nearly equally divided between extracellular and bound activity. Bound aryl-β-glucosidase was almost all available to substrate. An induction procedure was used to maximize both β-glucosidases in 4 to 6-hr cells. Aryl-β-glucosidase was entirely bound but still mostly (90%) detectable, whereas cellobiase was mostly internal and cryptic. A freeze-thaw cycle or treatment with phenethyl alcohol or deoxycholic acid made the cellobiase detectable without releasing it from the cell. A 10 to 20% increase in cell-bound aryl-β-glucosidase could be obtained by this treatment. Dilute HCl (0.1 n) destroyed the patent aryl-β-glucosidase but not the cryptic aryl-β-glucosidase or the cryptic cellobiase activity in intact cells. This suggested that most aryl-β-glucosidase activity was exterior to the cell membrane but still within the mural space. The thermal stability of patent aryl-β-glucosidase and released cellobiase was found to be higher than in corresponding cell-free extracts. Measurements of Km suggested a slightly lower affinity for substrate p-nitrophenyl-β-d-glucopyranoside by the enzymes in intact cells compared to enzymes in extracts.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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