Hydrolysis of alphas1- and beta-casein-derived peptides with a broad specificity aminopeptidase and proline specific aminopeptidases from Lactococcus lactis subsp. cremoris AM2.
Aminopeptidase hydrolysis of alpha(s)1 - and beta-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.
Bouchier
P J
PJ
Dairy Products Research Centre, Teagasc, Fermoy, Ireland.
FitzGerald
R J
RJ
O'Cuinn
G
G
D000626:Aminopeptidases / Q000378:metabolism*; D002364:Caseins / Q000378:metabolism*; D018819:Dipeptidyl Peptidase 4 / Q000378:metabolism*; D006868:Hydrolysis; D013294:Lactococcus lactis / Q000201:enzymology*; D007931:Leucyl Aminopeptidase / Q000378:metabolism*; D010455:Peptides / Q000378:metabolism*; D013379:Substrate Specificity
D002364:Caseins; D010455:Peptides; D000626:Aminopeptidases; D007931:Leucyl Aminopeptidase; C022750:X-Pro aminopeptidase; D018819:Dipeptidyl Peptidase 4