The purification, production and some properties of the intracellular and cell wall associated (1→3)-β-glucanases, (1→6)-β- glucanases and β-glucosidases of Acremonium persicinum have been examined. Anion exchange chromatography revealed the presence of two (1→3)-β-glucanases, one (1→6)-β-glucanase and two β-glucosidases in intracellular extracts of A. persicinum, with further purification by gel filtration chromatography allowing partial characterization of these enzymes. All three intracellular β-glucanases and one of the β-glucosidases appear to be very similar to enzymes found in the extracellular fluid with regard to their molecular masses, hydrolytic action patterns on their substrates, and apparent regulation of syntheses. In contrast, the remaining β-glucosidase appeared to occur only intracellularly and possessed different properties from its extracellular counterpart, most notably being composed of two subunits of 130 and 138 kDa, and its synthesis relatively insensitive to glucose in the medium. Similar anion exchange chromatographic analysis of the cell wall associated enzyme activities extracted by 4 M LiCl revealed the presence of three (1→3)-β-glucanases, one (1→6)-β-glucanase and one β-glucosidase. Except for one (1→3)-β-glucanase all these enzymes appear to be the same as those enzymes found intra- and extracellularly in terms of their action patterns on substrates and their apparent regulation of syntheses. The other apparent cell wall-specific (1→3)-β-glucanase appears to be constitutively produced and is an endo-hydrolase since it displayed no activity toward periodate oxidised laminarin or barley β-glucan. Possible roles for these enzymes are proposed in light of their location, action patterns and apparent regulation of syntheses.