Proteolytic inactivation of an extracellular (1-->3)-beta-glucanase from the fungus Acremonium persicinum is associated with growth at neutral or alkaline medium pH.
FEMS Microbiol Lett
; 145(2): 287-93, 1996 Dec 01.
Article
em En
| MEDLINE
| ID: mdl-8961569
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.
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Base de dados:
MEDLINE
Assunto principal:
Acremonium
/
Beta-Glucosidase
Tipo de estudo:
Risk_factors_studies
Idioma:
En
Ano de publicação:
1996
Tipo de documento:
Article