Identification of peptides from edible silkworm pupae (Bombyx mori) protein hydrolysates with antioxidant activity

• Silkworm protein hydrolysates were generated with a range of proteolytic enzymes. The resulting physicochemical properties the enzyme dependent. demonstrated in vitro and situ antioxidant activity. In total, 8 peptides synthetised examined for cellular SWFVTPF NDVLFF showed highest activity HepG2 cells. ( Bombyx mori ) pupae is by-product from silk industry which rich protein. Hydrolysates silkworm using Alcalase®, Prolyve®, Flavourzyme® Brewers Clarex® preparations characterised. was investigated assays an assay reactive oxygen species (ROS) reduction hepatic HepG2. Overall, Alcalase Prolyve had scavenging activities, however, Flavourzyme Clarex enhanced ferric reducing power (FRAP) compared to other samples. Furthermore, hydrolysate significantly reduced ROS by 40% untreated control Peptides identified LC-MS/MS then tested their (ROS reduction, superoxide dismutase (SOD) expression glutathione (GSH) production activity) cells, therefore may have potential as natural antioxidants.