Release of antidiabetic peptides during simulated gastrointestinal digestion of quinoa (Chenopodium quinoa Willd) proteins

Abstract:

[Introduction]: The amino acids, peptides and proteins derived from foods stand out among the most studied natural compounds in virtue of their modulating properties of glucose levels in diabetic individuals. Quinoa has been recognized as one of the >grains of the 21st century> due to its high nutritional and functional value. However, no data on its potential as source of peptides with the ability to control glycemia have been reported. [Methods]: Quinoa proteins were subjected to gastrointestinal digestion simulating physiological conditions. In vitro anti-diabetic activity was measured in gastric and gastroduodenal digests and peptidic fractions obtained from them, evaluating their ability to inhibit dipeptidyl peptidase IV (DPP-IV), α-amylase, and α-glucosidase. The most active digest was analyzed by HPLC-MS/MS to identify the peptides potentially responsible for the observed effects. [Results]: Pepsin partially hydrolyzed quinoa proteins that were completely degraded by the action of pancreatin. Gastroduodenal digests obtained after 60 and 120 min-incubation with pancreatin showed inhibition values for the three enzymes between 2.5 and 7 times higher than those shown by the gastric digest. The IC50 values determined in the 60 mingastroduodenal digest were 0.23 mg protein/mL (DPP-IV), 0.53 mg protein/mL (α-amylase), and 1.75 mg protein/mL (α-glucosidase). The fraction containing the smallest peptides was mainly responsible for the inhibitory effects shown by the gastroduodenal digests. Three novel in vitro antidiabetic peptides, which sequences were IQAEGGLT, DKDYPK, and GEHGSDGNV, were identified. [Conclusions]: This is the …

Año de publicación:

2018

Keywords:

Fuente:

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