RESUMEN

This study was aimed to analyze the major protein composition of centipedes (Scolopendra subspinipes mutilans L.Koch.), and the ACE inhibitory activity of its hydrolysis. Albumins, gulbulins, coixins and glutelins were sequentially extracted from centipedes flour with corresponding buffer and then quantified by Kjeldahl method and Brandford. Hydrolysation of four kinds of proteins of centipedes and the residues were conducted with pepsin. The hydrolysis was ultrafiltrated (MWCO=3 000) and lyophilized. The peptides (≤3 kD) were obtained to evalu-ate the ACE inhibitory activity by RP-HPLC. The results showed that the total protein content of centipedes was (62.69±1.41)%. Among which the contents of albumins, globulins, coixins, glutelins and residual were account-ing for (6.42±0.31)%, (7.94±0.24)%, (4.31±0.34)%, (40.66±0.56)% and (25.78±0.60)%, respectively. The inhibition rate of hydrolysis of four kinds of protein and residual were 50.28%, 57.37%, 31.15%, 58.99%, 80.81%, respectively. It was concluded that centipedes were rich in protein and the hydrolyzate of all proteins manifested ACE inhibitory activity at different extent. The residual and glutelins indicated strong ACE inhibitory potential by hydrolysis. This research provided valuable sights for exploring hypotensive activity and functional food from centi-pedes.