Structure characterization and antioxidant activity of abalone visceral peptides-selenium in vitro

Abstract

Peptide-selenium chelate is widely regarded as one of the best selenium supplements for relieving selenium deficiency. In this study, abalone visceral peptides (AVP) was used to prepare a new type of peptides-selenium chelate to develop an organic selenium supplement with antioxidant activity. AVP prepared by alcalase exhibited the highest selenium-chelating ability. UV–visible spectroscopy, fluorescence spectroscopy, Fourier transform infrared spectroscopy and other structural analysis showed that selenium was mainly bound to the functional groups of –NH, –OH, –CH, CC, CO, and CN bonds on AVP. The formation of AVP-selenium chelate enhanced thermal stability and generated a new crystal structure. The ABTS•+ and •OH scavenging activities of AVP-selenium chelate were increased after in vitro digestion than that of AVP. Conclusively, this study analyzed the chelating mechanism of AVP and selenium from a structural perspective, which would provide a theoretical basis for the development of new selenium supplements.