The Purification and Characterization of Prolyl Aminopeptidase from Penicillium camemberti

Prolyl aminopeptidase [EC 3.4.11.5] from the cell-free extract of Penicillium camemberti was purified about 2800-fold by chromatographic techniques. The purity of the enzyme was confinned by electrophoretic analysis. The molecular mass of the enzyme was estimated to be 270,000 Da by gel filtration. The enzyme had a maximum activity at pH 7.0 and 45C, and Pro-p-naphthylamide was the substrate; the enzyme was stable up to 50C.