Collagen peptides are a potential treatment for osteoporosis due to their antiosteoporosis activity. In this study, we prepared immobilized protease with eggshell membrane as carrier, and then hydrolyzed collagen to obtain collagen peptide. The antiosteoporosis of collagen peptides was confirmed by hBMSC osteogenic differentiation and bone mineralization improvement results. Surprisingly, antiosteoporosis of collagen peptides was related to the molecular weight of collagen peptides. This was derived from the osteoblast marker gene expressions, and mineral elements in P1 treatment were higher than those in P3 treatment. Consequently, these results confirmed that antiosteoporosis of low molecular weight collagen peptides is higher than that of higher molecular weight collagen peptides. Furthermore, the antiosteoporosis activity of P1 was due to its peptide sequences with known antiosteoporosis activity in P1. PRACTICAL APPLICATION: Using eggshell membrane as carrier to prepare immobilized protease was meaningful for solving the problem of resource waste. In addition, the results showed that collagen peptides possessed antiosteoporosis, and the effect of low molecular weight collagen peptides was better. This study provides a theoretical basis for developing high antiosteoporosis collagen peptides able to treat osteoporosis.
Keywords: antiosteoporosis; collagen peptides; egg membrane; immobilized enzyme; zebrafsh larvae.
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