Open AccessProteolytic inactivation of an extracellular (1 → 3)‐ β ‐glucanase from the fungus Acremonium persicinum is associated with growth at neutral or alkaline medium pH
Author(s) -
Pitson Stuart M.,
Seviour Robert J.,
Mcdougall Barbara M.
Publication year - 1996
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1996.tb08591.x
Subject(s) - phenylmethylsulfonyl fluoride , extracellular , glucanase , biochemistry , fungus , protease , proteases , serine protease , acremonium , biology , proteolytic enzymes , enzyme , microbiology and biotechnology , chemistry , botany
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.