Large-scale preparation and some properties of penicillopepsin, the acid proteinase of Penicillium janthinellum

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Abstract
The acid proteinase penicillopepsin has been isolated from the culture filtrate of the mould Penicillium janthinellum, grown in submerged culture in a 1500 l fermentor. After concentrating the enzyme by adsorption on diethylaminoethylcellulose, it was purified by chromatography on aminoethylcellulose and phosphocellulose. The yield of the purified enzyme was about 2.6 g (37% recovery). It was shown to be homogeneous on acrylamide gel. Crystals suitable for X-ray analysis were prepared from the pure enzyme. Both the N- and the C-terminal amino acids appear to be alanine, although N-terminal serine has also been found in varying amounts. The purified enzyme is stable to prolonged exposure in the pH range 2.2–6.0, and at pH 4.9 retains 100% activity for 1 h at 55°. The crystals retain full activity at room temperature for many weeks.

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