• Hydrolysis of Ks1- and L-casein-derived peptides with a broad specifcity aminopeptidase and proline specific aminopeptidases from Lactococcus lactis subsp. cremoris AM2

      Bouchier, Paul J.; Fitzgerald, Richard J.; O'Cuinn, Gerard; Forbairt; IRish Dairy LEvy; European Union; AIR2-CT94-1560 (Wiley, 1999-03-29)
      Aminopeptidase hydrolysis of αs1- and β-casein-derived synthetic peptides containing non-consecutive and consecutive proline residues was characterised. Aminopeptidase P (Pep P) (EC 3.4.11.9) or post-proline dipeptidyl aminopeptidase (PPDA) (EC 3.4.14.5) along with lysine-paranitroanilide hydrolase (KpNA-H) (EC 3.4.11.1) activities are required in the degradation of peptides containing non-consecutive proline residues. However, both Pep P and PPDA along with KpNA-H are required for hydrolysis of peptides containing consecutive proline residues. The results demonstrate the mechanism by which combinations of purified general and proline specific aminopeptidases from Lactococcus lactis subsp. cremoris AM2 hydrolyse peptides containing proline residues.