Selenium-Chelating Peptide Derived from Wheat Gluten: In Vitro Functional Properties

Area of Science:

• Food Science and Technology
• Nutritional Biochemistry
• Biotechnology

Background:

• Exogenous selenium supplementation often faces bioavailability challenges.
• Wheat protein hydrolysates (WPH) offer a peptide-rich source for nutrient chelation.
• Developing enhanced selenium delivery systems is crucial for nutritional applications.

Purpose of the Study:

• To synthesize selenium-chelating polypeptides from wheat protein hydrolysate (WPH-Se).
• To evaluate the in vitro antioxidant activity and gastrointestinal stability of WPH-Se.
• To assess the bioavailability and amino acid profile of WPH-Se post-digestion.

Main Methods:

• WPH-Se synthesized using wheat peptide and selenium (2:1 ratio) at pH 8.0, 80 °C.
• In vitro antioxidant activity assessed via DPPH, OH, and ABTS radical scavenging assays.
• In vitro gastrointestinal digestion simulated to evaluate stability and functional properties.

Main Results:

• WPH-Se exhibited significant antioxidant activities (DPPH, OH, ABTS scavenging, reducing capacity) across various conditions.
• High antioxidant efficacy was maintained by WPH-Se during simulated gastrointestinal digestion.
• Post-digestion, WPH-Se showed increased tryptophan, cysteine, and essential amino acids with retained selenium.

Conclusions:

• WPH-Se possesses robust in vitro antioxidant properties and stability during digestion.
• The enhanced amino acid profile and selenium content suggest improved nutritional value.
• WPH-Se is a promising ingredient for selenium and antioxidant dietary supplementation.