Effects of Collagen Peptides Derived from Perch Scale Hydrolysates on the Physiological Activity of Osteoblasts

A plethora of studies have demonstrated the bioactive properties of collagen peptides, including the promotion of wound healing and bone health. Research has demonstrated that these effects are attributable to their elevated biocompatibility and signaling capabilities. The present study investigated the effects of collagen peptides produced by enzymatic hydrolysis of perch scales on the induction of extracellular matrix formation and osteogenesis. The findings demonstrated that a combination of pre-heating and enzymatic hydrolysis resulted in the optimal peptide yield, with 94.9% of the peptides exhibiting a molecular weight below 1200 Daltons and containing elevated levels of hydroxyproline. The addition of perch scale collagen peptides to fibroblasts 890510-01F ATIT has been demonstrated to effectively induce the production of type I procollagen and fibronectin, a protein associated with the osteoblast phenotype and osteoblast differentiation. It is also worthy of note that experiments conducted using MC3T3-E1 osteoblasts indicate that collagen peptides significantly increased alkaline phosphatase activity by a factor of 1.46. This study demonstrates that collagen peptides derived from perch scales are enriched in bioactive peptides containing C-terminal tyrosine residues, including DYPRNHY and DPYNRHY. These findings provide a scientific basis for the future development of perch scale-derived collagen peptides as dietary supplements or functional food ingredients for promoting bone health.