PMID: 8961569Dec 1, 1996Paper

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 Microbiology Letters
S M PitsonB M McDougall

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.

References

Jun 1, 1975·Journal of Bacteriology·B Friebe, A W Holldorf
Jan 1, 1987·Annual Review of Biochemistry·J S Bond, P E Butler
Oct 1, 1985·The Biochemical Journal·M L Niku-PaavolaM Nummi
Jun 1, 1994·Applied Microbiology and Biotechnology·M J Rollins, G M Gaucher
Apr 1, 1993·Analytical Biochemistry·G F Bickerstaff, H Zhou

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