@article{Ren2026, 
author = {Jiandong Ren and Jianping Wu},
title = {Preparation and characterization of phosphopeptides derived from egg yolk granules},
year = {2026},
journal = {Journal of Food Bioactives},
volume = {33},
pages = {73-84},
keywords = {Granules, Phosvitin, Phosphopeptides, Hydrolysis, Peptide sequence},
url = {https://www.sciopen.com/article/10.26599/JFB.2026.95033441},
doi = {10.26599/JFB.2026.95033441},
abstract = {Phosphorylated peptides derived from egg yolk phosvitin (PPP) have been reported with various physiological functions such as mineral absorption promoting, antioxidant, antimicrobial and anti-inflammatory activities. However, the animal/clinical study and commercial application of PPP was hampered by the difficulties in phosvitin purification and peptide fragmentation. This study introduced a new approach to prepare phosphopeptides from egg yolk granules to avoid difficulties obtaining purified phosvitin. The egg yolk granules were first dephosphorylated by 0.2 N NaOH for 0.5 h and then hydrolyzed by eight enzymes, respectively. Pancreatin produced the highest degree of hydrolysis of 24.2% with a protein recovery of 41.8% and nitrogen to phosphorus atomic ratio of 19.1, which is comparable to commercial casein phosphopeptides. In the pancreatin hydrolysate 15 peptide sequences were characterized from three phosvitin domains: AKTSSSSSSASSTATSSSSSSASSPN (PV 9-34), DEEENDQV (PV 40-47) and SGHLEDDSSSSSSSSVLSKIWG (PV 190-211). In addition, 54 peptides were characterized from lipovitellins, and 26 of them were phosphorylated. This experiment suggests that it is feasible to produce phosphopeptides from granules instead of purified phosvitin.}
}