Novel antioxidant and ACE inhibitory peptide identified from Arthrospira platensis protein and stability against thermal/pH treatments and simulated gastrointestinal digestion.

In current study, novel antioxidant and ACE inhibitory peptides were screened from Arthrospira platensis protein hydrolysates (APH) generated by six different proteases, respectively. The purification steps including ultrafiltration membrane and chromatography were guided by ABTS radical scavenging activity (ARSA), hydroxyl radical scavenging activity (HRSA), ferrous ion chelation activity (FICA) and ACE inhibitory activity. A novel antioxidant peptide VTAGLVGGGAGK, which exhibited highest ARSA, HRSA and FICA with EC50 value of 1.08 mg/mL 1.35 mg/mL and 1.24 mg/mL, respectively, was identified from alcalase-APH. Meanwhile, a novel ACE inhibitory peptide PTGNPLSP with the highest ACE inhibitory activity (IC50 = 1.54 mg/mL) was identified from trypsin-APH. Both VTAGLVGGGAGK and PTGNPLSP had strong stability under thermal processing (25-100 °C) and diverse pH conditions (pH 3-11). In addition, the PTGNPLSP was more stable than VTAGLVGGGAGK during in vitro gastrointestinal digestion. Our findings will provide new knowledge for the development of novel natural antioxidants and ACE inhibitors as well as the high-value utilization of Arthrospira platensis protein.