Crickets contain high protein content that can be used to improve nutrition but are less exploited. This study was conducted to isolate different Cricket Protein Fractions including albumin, globulin, glutelin, and prolamin. All fractions were characterized and hydrolyzed by commercial enzymes. The results showed that the glutelin fractions had the highest extraction yields with 53.9 ± 2.12% (p < 0.05). Moreover, glutelin hydrolysate fraction prepared by Alcalase with a 16.35 ±0.29% hydrolysis degree was selected for further purification because of their high antioxidant activities, including ABTS radical-scavenging activity (0.44-0.55 µmol Trolox eq./g) and metal chelating activity (1721.99-1751.71 µmol EDTA eq./g). Two active fractions, GA-1 (<3 kDa) and GA-2 (<3 kDa), were collected from the consecutive purification of glutelin hydrolysates, which included processes such as membrane ultrafiltration and gel filtration. The fractions were analyzed by LC-MS/MS to obtain 10 peptides with 3-13 amino acids identified as TEAPLNPK, EVGA, KLL, TGNLPGAAHPLLL, AHLLT, LSPLYE, AGVL, VAAV, VAGL, and QLL with a molecular weight range of 359.23-721.37 Da in the two fractions. The amino acid sequence shows a prevalence of hydrophobic amino acids (50-100%) such as valine and leucine in the peptide chains, accounting for its high antioxidant activity. In conclusion, cricket glutelin hydrolysate prepared by Alcalase can serve as an alternative source of potent edible bioactive peptides in functional food products.
Keywords: antioxidant peptides; bioactive peptide; cricket protein fraction (CPF); fractionation; protein hydrolysate.