Purification and Characterization of a Novel Calcium-Binding Heptapeptide from the Hydrolysate of Tilapia Bone with Its Osteogenic Activity

• Published in: Foods Vol. 11; no. 3; p. 468
• Main Authors: He, Jinlun, Guo, Hao, Zhang, Mei, Wang, Meng, Sun, Liping, Zhuang, Yongliang
• Format: Journal Article
• Language: English
• Published: Switzerland MDPI AG 04.02.2022; MDPI
• Subjects: Amino acids; Amino groups; animals; Binding; Binding sites; Biomedical materials; bone formation; Calcium; calcium-binding capacity; Carbonyl compounds; Carbonyl groups; Carbonyls; Chelation; Collagen; Differentiation; electrostatic interactions; Electrostatic properties; Enzymes; Food science; Fourier transform infrared spectroscopy; Fourier transforms; High performance liquid chromatography; hydrogen; Hydrogen bonding; Hydrolysates; Hydrophobicity; Infrared spectroscopy; Integrins; Liquid chromatography; Mass spectrometry; Mass spectroscopy; Mineralization; Molecular docking; molecular dynamics; Osteoblastogenesis; osteoblasts; Osteoclastogenesis; osteoclasts; Osteoporosis; peptide; Peptides; proteinases; Proteins; Residues; Scanning electron microscopy; Skin; structural characteristics; Tilapia; tilapia bone; X-ray diffraction; peptide; molecular docking; structural characteristics; calcium-binding capacity; mass spectrometry; tilapia bone; osteoblast

In this study, a calcium-binding peptide was obtained by hydrolyzing tilapia bone and its osteogenic activity was evaluated. Animal protease was selected from nine enzymes, and its hydrolysate was purified through preparative and semi-preparative reverse phase high-performance liquid chromatography....