Olive Pomace Extract Contains Low Molecular Weight Peptides and Possesses ACE Inhibitory Activity
peer-reviewed · International Journal of Molecular Sciences · 2024
| Date | 2024-04-02 |
| Type | peer-reviewed |
| Venue | International Journal of Molecular Sciences |
| Publisher | MDPI AG |
| Contribution | downstream-application |
| DOI | 10.3390/ijms25073962 |
| Citations (OpenAlex) | 23 |
Abstract
The aim of the present study was to determine the ACE inhibitory activity of aqueous extracts of olive pomace and to understand whether they represent a good source of bioactive LMW peptides for nutritional and pharmacological applications. We produced a water extract from olive pomace (var. Picual) and obtained its low molecular weight (LMW) fraction (50 = 3.57 ± 0.22 µg prot/mL). The LMW fraction (Olea europaea (cv. Farga) genome database. Ten new peptides were also identified by Peaks de novo sequencing. The protein sources of twelve peptides detected in the database by Peaks DB were identified by BLAST search. The ACE inhibitory activity of the identified peptides was predicted by BIOPEP software. We conclude that olive pomace possesses ACE inhibitory activity and contains low molecular weight peptides with (predicted) biological activity. Olive pomace may represent a good source of peptides for nutritional and pharmaceutical applications. In our study, it has been shown that olive pomace possesses ACE inhibitory activity and contains low molecular weight peptides with (predicted) biological activity. Olive pomace may represent a good source of peptides for nutritional and pharmaceutical applications. More research is needed in order to identify the in vivo effects of olive pomace bioactive peptides.
Methods and tools
- Olive pomace ACE-inhibitory peptides: Finds low molecular weight peptides with predicted ACE-inhibitory activity in olive pomace, several of them sequenced de novo by PEAKS.
Methods it uses
- PEAKS: Commercial DP-based de novo