Proteolytic inactivation of an extracellular (1 → 3)-β-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.

Isolation of Acremonium species producing cephalosporine C (CPC) from forest soil in Gilan province, Iran

“…Cellulose hydrolysis is an out-standing characteristic of this fungus (Piston et al, 1996). So its isolation in the soil of an old forest is expectable due to suitable ecologic conditions of the investigated area.…”

Purification and characterization of the (1→3)-β-glucanases fromAcremoniumsp. IMI 383068

“…Why multiple forms of these enzymes are found may be either because each is encoded by a separate gene or a single gene encodes one enzyme that then undergoes some post‐translational modification. This may involve protease modification, and protease activity is common in fungal culture media where multiple enzyme production occurs [11,12]. The high homology between the N‐terminal primary amino acid sequences of CG I and CG II, where they are identical for the first 11 amino acids (the only ones obtained for CG II), raises the possibility that these two are encoded by a single gene.…”