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Separation and identification of ACE inhibitory peptides from defatted walnut meal
Ist Teil von
European food research & technology, 2020-10, Vol.246 (10), p.2029-2038
Ort / Verlag
Berlin/Heidelberg: Springer Berlin Heidelberg
Erscheinungsjahr
2020
Link zum Volltext
Quelle
Alma/SFX Local Collection
Beschreibungen/Notizen
The peptide obtained from walnut protein enzymatic hydrolysate had high ACE inhibitory activity. Through centrifugation, ultrafiltration, gel chromatography and high performance liquid chromatography (HPLC), the walnut oligo-peptide, which was denoted as P4-c with high ACE inhibitory activity was obtained. Three novel ACE inhibitory peptides, GVVPHN, EHSLDPLK and KTLLNFGPN, were identified from P4-c by high-resolution ion mobility mass spectrometry (IM-MS). The three novel ACE inhibitory peptides possessed good ACE inhibitory activity and the fraction GVVPHN had high ACE inhibitory activity with 27.3 µmol L
−1
of IC
50
. The molar percentage of hydrophobic amino acids in the peptide GVVPHN was 50% while the hydrophobic amino acid contents of EHSLDPLK and KTLLNFGPN were 37.5% and 44.4%, respectively, which indicates ACE inhibitory activities were hydrophobicity of amino acid-dependent.