Intracellular and cell wall associated beta-glucanases and beta-glucosidases of Acremonium persicinum

The purification, production and some properties of the intracellular and c ell wall associated (1 --> 3)-beta-glucanases, (1 --> 6)-beta-glucanases an d beta-glucosidases of Acremonium persicinum have been examined. Anion exch ange chromatography revealed the presence of two (1 --> 3)-beta-glucanases, one (1 --> 6)-beta-glucanase and two beta-glucosidases in intracellular ex tracts of A: persicinum, with further purification by gel filtration chroma tography allowing partial characterization of these enzymes. All three intr acellular beta-glucanases and one of the beta-glucosidases appear to be ver y similar to enzymes found in the extracellular fluid with regard to their molecular masses, hydrolytic action patterns on their substrates, and appar ent regulation of syntheses. In contrast, the remaining beta-glucosidase ap peared to occur only intracellularly and possessed different properties fro m its extracellular counterpart, most notably being composed of two subunit s of 130 and 138 kDa, and its synthesis relatively insensitive to glucose i n the medium. Similar anion exchange chromatographic analysis of the cell w all associated enzyme activities extracted by 4 M LiCl revealed the presenc e of three (1 --> 3)-beta-glucanases, one (1 --> 6)-beta-glucanase and one beta-glucosidase. Except for one (1 --> 3)-beta-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)-beta-glucana se appears to be constitutively produced and is an endo-hydrolase since it displayed no activity toward periodate oxidised laminarin or barley beta-gl ucan. Possible roles for these enzymes are proposed in light of their locat ion, action patterns and apparent regulation of syntheses.