Characterization, in vitro antioxidant activity and stability of cattle bone collagen peptides‑selenium chelate
Jianming Li, Wenjun Wang, Hui Chen, Su-Yun Lin, X. Y. Mao, Jun-Min Yu, Lingli Chen
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 intestinal selenium permeability of CCP-Se was significantly better than sodium selenite ( p < 0.05). This study provides reference for the high-value application of cattle bone and suggests the potential of CCP-Se as a new effective selenium supplement. • The CCP-Se was prepared and selenium binding capacity was 33.65 mg/g. • CCP-Se had a compact structure with good thermal and pH stability. • CCP-Se showed excellent antioxidant activity. • CCP-Se exhibited better intestinal permeability than sodium selenite.