In the present work, fermented microalgae (Pavlova lutheri) preparation is product of yeast fermentation by Hansenula polymorpha. And purified and characterized a alkaline phosphatase (ALP) activity peptide from fermented microalgae. After its separation from the fermented microalgae by several purification steps, the peptide responsible for the ALP activity was isolated and its sequence was identified as Glu-Pro-Gln-Trp-Phe-Leu  (908.9 Da). Our results indicate that a non-toxic peptide can increase activity of ALP as phenotypic markers for early-stage osteoblastic differentiation. Furthermore, the results showed positive effects of peptide on alkaline phosphatase and bone morphogenic protein-2 (BMP-2) as important factors for bone formation, remodeling and mineralization. To elucidate the mechanisms by which the peptide acted, we examined its effects on TPA-induced MAPKs/NF-?B activation and determined that the peptide treatment significantly reduced p-p38 (p-ERK) kinase/NF-?B (p65) in MG-63 cells. The present study may provide new insights in the osteoblastic differentiation of purified peptide and possibility for its application in bone health supplement.

Peptide from microalgae, Pavlova Lutheri (Haptophyceae) increases ALP activity through MAPK and NF-kB activation and induces human osteoblastic differentiation

243rd National Meeting (2012)

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.