Peptide identification and angiotensin converting enzyme (ACE) inhibitory activity in prolyl endoproteinase digests of bovine αs-casein

Roseanne Norris, Martina B. O'Keeffe, Alexey Poyarkov, Richard J. Fitzgerald

Research output: Contribution to journalArticlepeer-review

Abstract

Incubation of sodium caseinate (NaCN) and purified α-casein (αs-CN) with an Aspergillus niger derived prolyl endoproteinase (An-PEP) for 1, 2, 3, 4, 8 and 24 h resulted in the generation of potent angiotensin converting enzyme (ACE) inhibitory hydrolysates. An ACE IC50 of 21.1 ± 5.1 μg/ml was obtained on incubation of An-PEP with NaCN for 4 h. Fractionation of the NaCN hydrolysates using 3 kDa centrifugal filters resulted in highly active permeate fractions, the most potent being obtained from the 3 h hydrolysate (ACE IC50 = 2.9 ± 0.3 μg/ml). The hydrolytic specificity of An-PEP for purified α-CN was assessed using UPLC ESI MS/MS. The analysis confirmed An-PEP's cleavage preference for the C-terminal side of Pro and also confirmed that An-PEP has the ability to cleave at the C-terminal of Ala, Leu, Arg and His residues.

Original languageEnglish
Pages (from-to)210-217
Number of pages8
JournalFood Chemistry
Volume188
DOIs
Publication statusPublished - 29 Apr 2015

Keywords

  • ACE inhibition
  • Aspergillus niger derived prolyl
  • endoproteinase
  • LC-MS
  • Simulated gastrointestinal digestion
  • Sodium caseinate
  • Substrate specificity
  • α-Casein

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