Abstract
A new X-prolyl dipeptidyl-aminopeptidase was discovered and purified from Aspergillus oryzae grown on solid bran culture medium. The purified enzyme was homogeneous on polyacrylamide gel electrophoresis (PAGE) at pH 9.4 and on isoelectric focussing, and its M r was 280 000 by gel filtration. On SDS-PAGE, the purified enzyme gave a single band with a M r of 145 000 indicating that the enzyme was composed of two homogeneous monomers. The p I was 4.2. The enzyme was inhibited by diisopropylphosphorofluoridate. It has a pH optimum at 7.0–7.5 for glycol- pL -proline- p-nitroanilide (Gly-Pro- pNA). The K m value of the enzyme for Gly-Pro- pNA at pH 7.5 and 30° was 0.55 mM.
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