Characterization, <i>in vitro</i> antioxidant activity and stability of cattle bone collagen peptides‑selenium chelate.

ABSTRACT: In this study, cattle bone collagen peptides-selenium chelate (CCP-Se) was prepared and its structure, oxidation resistance and stability were characterized. The selenium binding capacity was 33.65 ± 0.13 mg/g by optimized preparation conditions. Structural analysis showed that selenium ions bound mainly to the amino nitrogen, carboxyl oxygen and hydroxyl oxygen atoms of the cattle bone collagen peptide (CCP). The microstructure and particle size analyses showed that the particle size of CCP-Se was increased and formed a regular and compact crystal structure compared with CCP. Additionally, CCP-Se exhibited excellent antioxidant activity. Stability analysis showed that CCP-Se was stable in thermal processing, simulated in vitro digestion and acid/alkali tolerance tests. The intestin

SUBMITTER: Li JM 

PROVIDER: S-EPMC11639323 | biostudies-literature | 2024 Oct

REPOSITORIES: biostudies-literature