@article{SONG2026, 
author = {Sijia SONG and Yingying LIN and Yuning ZHANG and Huiyuan GUO},
title = {In Vitro Digestion Characteristics of Partially Dephosphorylated Bovine β-Casein},
year = {2026},
journal = {Food Science},
volume = {47},
number = {2},
pages = {40-47},
keywords = {dephosphorylated β-casein, in vitro digestion, particle size, peptide profile, bioactive peptides},
url = {https://www.sciopen.com/article/10.7506/spkx1002-6630-20250710-084},
doi = {10.7506/spkx1002-6630-20250710-084},
abstract = {The in vitro simulated gastrointestinal digestion characteristics and peptide profile of partially dephosphorylated β-casein (PDP-BCN), prepared enzymatically, were determined via dynamic light scattering (DLS), confocal laser scanning microscopy (CLSM), and liquid chromatography-tandem mass spectrometry (LC-MS/MS). The results demonstrated that the flocculated structures and particle size formed by PDP-BCN in simulated infant gastric fluid were significantly smaller than those of native β-casein (β-CN), making it more easily digested into smaller particles. Moreover, during simulated infant gastrointestinal digestion, PDP-BCN degradation generated 880 peptide fragments, far exceeding the 533 peptides produced by native β-CN. This difference in peptide fragments was particularly notable at the N-terminal region of the protein. Additionally, PDP-BCN degradation yielded 8 unique bioactive peptides and 137 peptides with potential bioactivity, exceeding both the number and functional diversity of peptides derived from native β-CN. Therefore, PDP-BCN exhibited significant advantages over native β-CN in terms of digestibility. This study provides a theoretical basis for the future application of PDP-BCN as a novel protein ingredient in infant formula.}
}