Isolation and identification of an antioxidant collagen peptide from skipjack tuna () bone.

To date, many researchers have developed active components that are derived from seafood processing for the purposes of healthcare. Here, an antioxidant collagen peptide was obtained from skipjack tuna () bone by using a combination of trypsin and chymotrypsin as the catalyst. The amino acid sequence of the peptide was identified as Ser-Ser-Gly-Pro-Pro-Val-Pro-Gly-Pro-Met-Gly-Pro-Met-Gly-Pro-Arg (SSGPPVPGPMGPMGPR) by liquid chromatography-electrospray ionization quadrupole time-of-flight mass spectrometry (LC-ESI-QTOF-MS) analysis. We found that the as-prepared collagen peptide can efficiently scavenge DPPH radical (IC 3.149 mM), superoxide anion radical (IC 3.803 mM) and ABTS radical (IC 9.489 mM). In addition, it has been found that the methionine (Met) residue in the collagen peptide could provide a precise active site during the scavenging of DPPH radicals by Fourier transform infrared spectroscopy (FTIR) analysis and matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) mass spectrometry analysis. These results suggest that the peptide can find wide uses in the food, cosmetic and pharmaceutical industries.