Phycobiliproteins from <i>Arthrospira Platensis</i> (Spirulina): A New Source of Peptides with Dipeptidyl Peptidase-IV Inhibitory Activity

• Main Authors: Yuchen Li, Gilda Aiello, Carlotta Bollati, Martina Bartolomei, Anna Arnoldi, Carmen Lammi
• Format: Article
• Language: English
• Published: MDPI AG 2020-03-01
• Series: Nutrients
• Subjects: allophycocyanin; bioactive peptides; c-phycocyanin; dpp-iv; lc-ms/ms; <i>spirulina platensis</i>
• Online Access: https://www.mdpi.com/2072-6643/12/3/794

<i>Arthrospira platensis</i> (spirulina) is a cyanobacterium, which contains mainly two phycobiliproteins (PBP), i.e., C-phycocyanin (C-PC) and allophycocyanin (APC). In this study, PBP were hydrolyzed using trypsin, and the composition of the hydrolysate was characterized by HPLC-ESI-MS/MS. Furthermore, the potential anti-diabetic activity was assessed by using either biochemical or cellular techniques. Findings suggest that PBP peptides inhibit DPP-IV activity in vitro with a dose-response trend and an IC₅₀ value falling in the range between 0.5 and 1.0 mg/mL. A lower inhibition of the DPP-IV activity expressed by Caco-2 cells was observed, which was explained by a secondary metabolic degradation exerted by the same cells.