Preparation, Characterization, and In Vitro Bioactivity of Artemisia capillaris Thunb. Leaf Protein Peptide Selenium Chelates.

This study aimed to prepare Artemisia capillaris Thunb. leaf protein peptide selenium chelates (AP-Se) employing sodium selenite as a selenium (Se) source, with a focus on their structure and biological activities. Artemisia capillaris Thunb. leaf protein (AP) was extracted from Artemisia capillaris Thunb. leaf (AC) and enzymatically digested to obtain AP peptide (AP-P). The results exhibited that the maximum Se chelating capacity of 52.78 ± 0.74 (mg/g) was obtained at a peptide-Se mass ratio of 1:3.3, pH 9, and temperature of 49°C condition. The N-terminal amino group and C-terminal carboxyl group of AP-P were the main binding sites of selenium ions. The chelation reaction caused folding and curling of the peptide chain in AP-P, which produced folds and crystal in AP-Se microstructure. Furthermore, at certain dosages, AP-Se demonstrated an ABTS+ clearance rate comparable with that of Vitamin C (VC), along with outstanding gastrointestinal permeability. Furthermore, AP-Se was proven to be less hazardous to cells than sodium selenite. Overall, the study indicated that AP-Se may have a promising usage as an effective natural selenium supplement in the medical and food industries.