Abstract

Arthrospira platensis (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.

Highlights

  • Arthrospira platensis is a cyanobacterium, which contains mainly two phycobiliproteins (PBP), namely C-phycocyanin (C-PC) and allophycocyanin (APC) [1]

  • This study provides new evidence regarding the ability of tryptic PBP to modulate Dipeptidyl peptidase IV (DPP-IV) activity in vitro on human recombinant enzyme and in situ on the cellular intestinal modulate DPP-IV activity in vitro on human recombinant enzyme and in situ on the cellular intestinal membrane level

  • We reported the DPP-IV inhibitory activity of a tryptic hydrolysate membrane level

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Summary

Introduction

Arthrospira platensis (spirulina) is a cyanobacterium, which contains mainly two phycobiliproteins (PBP), namely C-phycocyanin (C-PC) and allophycocyanin (APC) [1]. Considering that there is an increasing interest in underexploited sustainable sources of proteins, such as microalgae, in a preceding paper, we investigated the inhibitory activity of a peptic and a tryptic hydrolysate from a total protein extract from spirulina and observed that, in vitro, the tryptic hydrolysate is a much better inhibitor of DPP-IV activity (IC50 = 0.1 mg/mL) than the peptic hydrolysate (IC50 = 3.4 mg/mL) [18]. In view of these results, the present study was aimed at investigating the potential ability of a tryptic PBP hydrolysate to modulate DPP-IV activity. The second objective was the evaluation of the potential anti-diabetic activity, which was carried out by measuring the effects on in vitro DPP-IV activity, as well as by performing experiments on Caco-2 cells, in order to measure the reduction of the enzymatic activity expressed on the cellular membranes of human enterocytes [19]

Reagents
Microalgae Biomass
Enzymatic Hydrolysis of PBP
In Vitro DPP-IV Activity of Tryptic PBP Peptides
Cell Culture
MTT Assay
Statistical Analysis
Results
Discussion
Full Text
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