title: Proteolytic inactivation of an extracellular (1-->3)-beta-glucanase from the fungus Acremonium persicinum is associated with growth at neutral or alkaline medium pH.
abstract: The filamentous fungus Acremonium persicinum released high levels of proteolytic enzyme activity into the culture fluid during growth at pH 7 or above. Almost total inhibition of this crude activity by phenylmethylsulfonyl fluoride suggested that it was mainly due to the presence of a serine protease. This protease inactivated one of three extracellular (1-->3)-beta-glucanases produced by this fungus, although the activities of the remaining two (1-->3)-beta-glucanases did not appear to be affected. Growth of A. persicinum in acidic conditions resulted in the presence of much lower extracellular proteolytic activity and no apparent (1-->3)-beta-glucanase inactivation.
authors.affiliation: Biotechnology Research Centre, La Trobe University, Bendigo, Australia.
authors.forename: S M
authors.initials: SM
authors.lastname: Pitson
authors.forename: R J
authors.initials: RJ
authors.lastname: Seviour
authors.forename: B M
authors.initials: BM
authors.lastname: McDougall
mesh_terms: D000164:Acremonium / Q000201:enzymology* / Q000254:growth & development*; D000468:Alkalies; D001431:Bacteriological Techniques; D010450:Endopeptidases / Q000378:metabolism; D005656:Fungal Proteins / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D009584:Nitrogen / Q000378:metabolism; D001617:beta-Glucosidase / Q000378:metabolism*
chemical_list: D000468:Alkalies; D005656:Fungal Proteins; D001617:beta-Glucosidase; D010450:Endopeptidases; D009584:Nitrogen