Amaranth peptides with antithrombotic activity released by simulated gastrointestinal digestion. (January 2016)

• Record Type: Journal Article
• Authors: Sabbione, Ana Clara; Nardo, Agustina Estefanía; Añón, María Cristina; Scilingo, Adriana
• Is Part Of: Journal of functional foods. Volume 20(2016)
• Page Start: 204
• Page End: 214
• Publication Date: 2016-01
• Subjects: Amaranth protein isolate -- Gastrointestinal digestion -- Antithrombotic activity -- Absorption by Caco 2 cell culture -- Bioactive peptides; TEER transepithelial electrical resistance -- DH% degree of hydrolysis -- MTT methyl tetrazolium assay -- AF active fraction -- SEC size-exclusion chromatography; Functional foods -- Analysis -- Periodicals; Food -- Biotechnology -- Periodicals; Nutrition -- Periodicals; 613.2
• DOI: 10.1016/j.jff.2015.10.015
• Languages: English
• ISSNs: 1756-4646

Abstract

Highlights: Potential antithrombotic peptides are released by gastrointestinal digestion. A protein active fraction was obtained using gel permeation chromatography. The peptides absorption through a Caco2-TC7 monolayer was studied. Potential thrombin inhibitors were identified and located in their native molecules. Abstract: Amaranth protein isolate was obtained and subjected to simulated gastrointestinal digestion to evaluate its potential antithrombotic activity. The protein isolate did not present fibrin clotting inhibition at the concentrations studied, whereas the hydrolysate (DH% = 51.1 ± 3.8%) exhibited inhibition of fibrin coagulation, showing a dose–response behaviour (IC50 = 0.23 ± 0.02 mg/mL), confirming that the enzymatic treatment was able to release bioactive peptides from amaranth proteins. A fraction with high antithrombotic activity was obtained from this hydrolysate, and resulted to be three times more potent than its original sample (IC50 = 0.07 ± 0.01 mg/mL). The absorption of this active fraction was studied with an in vitro peptides transport assay through intestinal epithelium and it was observed that some peptides are able to cross the Caco2-TC7 cell monolayer. Potentially bioactive peptides were found after sequencing them, and informatics tools allowed us to select and locate in their native molecules those peptides prone to inhibit thrombin activity.