Identification of octopus peptide and its promotion of β-casein synthesis in a mouse mammary epithelial cell line.

Abstract

Octopus protein hydrolysate has been reported to increase milk yield and milk protein production. In this paper, the utilization and underlying mechanisms of bioactive peptide fractions from octopus protein hydrolysate on β-casein expression in mouse mammary epithelial cells (HC11) were investigated. Fraction OPH3-1 significantly stimulated cell proliferation and β-casein synthesis in HC11 cells, which was purified by ultra-filtration and gel-filtration chromatography. The MWs of the peptides from OPH3-1 ranged from 525-2,578Da and consisted of 7-26 amino acid residues. Most of the peptides demonstrated the typical characteristics of milk protein synthesis promotion, especially MGLAGPR, MGDVLNF, EAPLMHV, and TEAPLMHV. Additionally, the mRNA abundances of mTOR, S6K1, 4EBP1, JAK2, and STAT5 were significantly enhanced by OPH3-1, which was consistent with the increased β-casein expression. These results suggest that the OPH3-1 peptides can promote the proliferation of mammary epithelial cells and increase β-casein synthesis. PRACTICAL APPLICATIONS: Breastfeeding mothers are generally recommended to take octopus soup as a daily diet to promote lactation. The peptides fraction OPH3-1 from the enzymatic hydrolysate of Octopus vulgaris which was revealed to significantly stimulate mammary epithelial cell proliferation and β-casein synthesis was obtained. This study suggests that octopus peptides can be used as nutritional supplements to increase the quantity and quality of milk production.