Phosphorylation of porcine bone collagen peptide to improve its calcium chelating capacity and its effect on promoting the proliferation, differentiation and mineralization of osteoblastic MC3T3-E1 cells

Journal of Functional Foods

Meihu Ma¹  Chengliang Li²  Guofeng Jin²  Shilin Zhao²  Min Zhang²  Fang Yang²  Yanhui Liang²  Wenmin Wu²  Lichao He³ 

[1] Corresponding author at: National R&D Center for Egg Processing, Huazhong Agricultural University, 1 Shizishan Street, Wuhan, Hubei 430070, China.;College of Food Science and Technology, Huazhong Agricultural University, Wuhan 430070, China;College of Food and Biotechnology of Wuhan Institute of Design and Science, Wuhan 430205, China;

关键词: Collagen peptide;    Phosphorylation;    Calcium binding capacity;    MC3T3-E1 cells;    Proliferation;    Mineralization;   

DOI  :  

来源: DOAJ

【 摘 要 】

In this study, porcine bone collagen peptide (CP) was phosphorylated with sodium tripoly phosphate (STP) in order to improve its calcium binding capacity and osteogenic activity. Firstly, the phosphorylation process were optimized by an orthogonal experiment. Then, the effects of CP, phosphorylated CP (PCP), CP-calcium chelate (CP-Ca) and PCP-Ca on proliferation, differentiation and mineralization of MC3T3-E1 cells were investigated. The results showed that all of the CP, PCP, CP-Ca and PCP-Ca could enhance the proliferation, differentiation and mineralization of MC3T3-E1 cells by increasing the mRNA expression levels of alkaline phosphatase (ALP), Runt-related transcription factor-2 (Runx2), osteocalcin (OCN), osteopontin (OPN) and collagen type I (Col I), as well as the protein expression levels of Runx2 and β-Catenin. Especially, PCP-Ca had the greatest and significant effect on mineralization of MC3T3-E1 cells (P < 0.05). These results suggested that phosphorylation is a promising method to improve the calcium binding capacity and osteogenic activity of collagen peptides.

【 授权许可】

Unknown