Summary: Phenylalanineaminopeptidase was isolated and purified from the culture filtrate of by affinity chromatography on -tert-butyl-l-threonyl-l-phenylalanyl-l-prolyl-glycyl-aminosilochrom and by gel-filtration; a 401-fold purification with a yield of 18% was achieved. The enzyme was a metalloenzyme with a molecular weight of 35000 and a pI of 5.8. It was stable at pH 7–9 and had an activity optimum in the range of pH 8–9.5 with l-phenylalanine -nitroanilide as substrate. Enzyme activity was highest towards the latter compound, substantially lower towards l-leucine -nitroanilide and only marginal towards other -nitroanilides. Besides phenylalanineaminopeptidase, a metalloproteinase and a serine proteinase were also detected in culture filtrate.


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