Purification and Identification of Novel Antioxidant Peptides from Enzymatically Hydrolysed Samia ricini Pupae.

Abstract

The emergence of excessive free radicals leads to the destruction of various systems within the body. These free radicals also affect nutritional values, color, taste, and emit an odor akin to rancid food. Most food industries use synthetic antioxidants, such as BHT (butylated hydroxytoluene) or BHA (butylated hydroxy anisole). However, high doses of these can be harmful to our health. Therefore, an antioxidant compounds, such as bioactive peptides from edible animals or plants, have emerged to be a very promising alternative as they reduce potential side effects. This study focused on the purification and identification of antioxidant peptides from protein hydrolysates of wild silkworm pupae (Samia ricini). Antioxidant peptides were purified from the hydrolysate by ultrafiltration and RP-HPLC. The results showed that protein hydrolysate from S. ricini pupae by trypsin with a molecular weight lower than 3 kDa and highly hydrophobic property, exhibited strong DPPH radical scavenging activity and chelating activity. Further identification of peptides from the fraction with the highest antioxidant activity was carried out using LC-MS/MS. Three novel peptides, i.e., Met-Ley-Ile-Ile-Ile-Met-Arg, Leu-Asn-Lys-Asp-Leu-Met-Arg, and Glu-Asn-Ile-Ile-Leu-Phe-Arg, were identified. The results of this study indicated that the protein hydrolysate from S. ricini pupae possessed potent biological activity, and the novel antioxidant peptides could be utilized to develop health-related antioxidants in food industry.