Proteolytic inactivation of an extracellular (1 → 3)-β-glucanase from the fungus Acremonium persicinum is associated with growth at neutral or alkaline medium pH |
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Authors: | Stuart M. Pitson Robert J. Seviour Barbara M. Mcdougall |
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Affiliation: | Biotechnology Research Centre, La Trobe University, Bendigo, P.O. Box 199, Bendigo, Vie. 3550, Australia |
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Abstract: | 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)- β -glucanases produced by this fungus, although the activities of the remaining two (1 → 3)- β -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)- β -glucanase inactivation. |
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Keywords: | Protease (1 → 3)-β-Glucanase Proteolytic inactivation Acremonium persicinum |
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