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Hydrolysis of α s1 ‐ and β‐casein‐derived peptides with a broad specificity aminopeptidase and proline specific aminopeptidases from Lactococcus lactis subsp. cremoris AM2
Author(s) -
Bouchier Paul J,
FitzGerald Richard J,
O'Cuinn Gerard
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)00146-5
Subject(s) - lactococcus lactis , proline , aminopeptidase , biochemistry , casein , hydrolysis , chemistry , peptide , enzyme , lysine , amino acid , biology , bacteria , leucine , lactic acid , genetics
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.