Isolation and identification of anti‐proliferative peptides from Spirulina platensis using three‐step hydrolysis

Abstract BACKGROUND Spirulina platensis is an excellent source of proteins (>60%) that can be hydrolyzed into bioactive peptides. RESULTS In this study, whole proteins of Spirulina platensis were extracted and hydrolyzed using three gastrointestinal endopeptidases (pepsin, trypsin and chymotrypsin). Subsequently, gel filtration chromatography was employed to separate hydrolysates, and four fractions (Tr1–Tr4) were obtained. Among them, Tr2 showed the strongest anti‐proliferation activities on three cancer cells (MCF‐7, HepG‐2 and SGC‐7901), with IC50 values of <31.25, 36.42 and 48.25 µg mL−1, respectively. Furthermore, a new peptide, HVLSRAPR, was identified from fraction Tr1. This peptide exhibited strong inhibition on HT‐29 cancer cells with an IC50 value of 99.88 µg mL−1. CONCLUSION Taken together, these peptides possessed anti‐proliferation activities on cancer cells and low cytotoxicity on normal cells, suggesting that they might serve as a natural anticancer agent for nutraceutical and pharmaceutical industries. © 2016 Society of Chemical Industry