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ABSTRACT: Background/objectives
Lactoferrin (Lf) is an iron-binding glycoprotein with multiple bioactivities, including promotion of cell proliferation and differentiation, immunomodulation, and antimicrobial activity. Lf, a basic glycoprotein, can bind to α-lactalbumin (α-Lac), an acidic whey protein. The current study aimed to evaluate whether Lf forms protein complexes with α-Lac and proteins/peptides from whey protein hydrolysate (WPH) and nonfat bovine milk powder (MP) and whether forming protein complexes influences resistance to gastrointestinal digestion and affects the bioactivities of Lf in human intestinal epithelial cells (HIECs and differentiated Caco-2 cells).Methods
Lf was blended with α-Lac, WPH, or MP. Assays were conducted to evaluate the bioactivities of proteins (
SUBMITTER: Jiang R
PROVIDER: S-EPMC11644007 | biostudies-literature | 2024 Nov
REPOSITORIES: biostudies-literature