Hydrolysis of Ks1- and L-casein-derived peptides with a broad specifcity aminopeptidase and proline specific aminopeptidases from Lactococcus lactis subsp. cremoris AM2
Name:
Hydrolysis-of--s1--and---casei ...
Size:
76.84Kb
Format:
PDF
Description:
main article
Keyword
General aminopeptidasePost proline dipeptidyl aminopeptidase
Aminopeptidase P
β-Casein derived peptide
Proline enriched peptide
Date
1999-03-29
Metadata
Show full item recordStatistics
Display Item StatisticsCitation
Bouchier, P., FitzGerald, R. and O'Cuinn, G. Hydrolysis of αs1- and β-casein-derived peptides with a broad specificity aminopeptidase and proline specific aminopeptidases from Lactococcus lactis subsp. cremoris AM2. FEBS Letters, 1999, 445(2-3), 321-324. doi: https://doi.org/10.1016/S0014-5793(99)00146-5Abstract
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.Funder
Forbairt; IRish Dairy LEvy; European UnionGrant Number
AIR2-CT94-1560ae974a485f413a2113503eed53cd6c53
https://doi.org/10.1016/S0014-5793(99)00146-5
Scopus Count
Collections
The following license files are associated with this item:
- Creative Commons
Except where otherwise noted, this item's license is described as Attribution-NonCommercial-ShareAlike 3.0 United States