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

Bouchier, Paul J²  O'Cuinn, Gerard³  FitzGerald, Richard J¹ 

[1] Life Sciences Department, University of Limerick, Limerick, Ireland;Dairy Products Research Centre, Teagasc, Fermoy, Ireland;Life Sciences Department, Galway-Mayo Institute of Technology, Galway, Ireland

关键词: General aminopeptidase;    Post proline dipeptidyl aminopeptidase;    Aminopeptidase P;    β-Casein derived peptide;    Proline enriched peptide;   

DOI  :  10.1016/S0014-5793(99)00146-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown