Hydrolysis of α s1- and β-casein-derived peptides with a broad specificity aminopeptidase and proline specific aminopeptidases from Lactococcus lactis subsp. cremoris AM2

Aminopeptidase hydrolysis of α s1- 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...

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Bibliographic Details
Published in:FEBS letters 1999-02, Vol.445 (2), p.321-324
Main Authors: Bouchier, Paul J, FitzGerald, Richard J, O'Cuinn, Gerard
Format: Article
Language:English
Subjects:
Aminopeptidase P
General aminopeptidase
Post proline dipeptidyl aminopeptidase
Proline enriched peptide
β-Casein derived peptide
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Summary:Aminopeptidase hydrolysis of α s1- 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.
ISSN:0014-5793
1873-3468
DOI:10.1016/S0014-5793(99)00146-5