Details

Autor(en) / Beteiligte

• Yesmine, Ben Henda
• Antoine, Bonnet
• da Silva Ortência Leocádia, Nunes Gonzalez
• Rogério, Boscolo Wilson
• Ingrid, Arnaudin
• Nicolas, Bridiau
• Thierry, Maugard
• Jean-Marie, Piot
• Frédéric, Sannier
• Stéphanie, Bordenave-Juchereau

Titel

Identification of ace inhibitory cryptides in Tilapia protein hydrolysate by UPLC–MS/MS coupled to database analysis

Ist Teil von

• Journal of chromatography. B, Analytical technologies in the biomedical and life sciences, 2017-05, Vol.1052, p.43-50

Ort / Verlag

Netherlands: Elsevier B.V

Erscheinungsjahr

2017

Quelle

MEDLINE

Beschreibungen/Notizen

• An ultra-performance liquid chromatography-quadrupole-time of flight mass spectrometry method was developed and applied to identify short angiotensin-I-converting enzyme (ACE) inhibitory cryptides in Tilapia (Oreochromis Niloticus) protein hydrolyzate. A database was created with previously identified ACE-inhibitory di- and tripeptides and the lowest molecular weight fraction of Tilapia hydrolysate was analysed for coincidences. Only VW and VY were identified. Further analysis of collected fractions conducted to the identification of 51 different peptides in major fractions. 19 peptides selected were synthesised and tested for their ACE inhibitory potential. TL, TI, IK, LR, LD, IQ, DI, AILE, ALLE, ALIE and AIIE were identified as new ACE inhibitors. The findings from this study point UPLC–MS/MS combined with the creation of a database as an efficient technique to identify specific short peptides within a complex hydrolysate, in addition with de novo sequencing. This efficient characterisation of bioactive factors like cryptides in protein hydrolysates will extend their use as functional foods.