Biological activities of commercial bovine lactoferrin sources

Lactoferrin (Lf) samples from several manufacturers were evaluated in vitro. The purity and protein form of each Lf were examined by SDS-PAGE, Western blot, and proteomics analysis. Assays were conducted to evaluate uptake of Lfs and iron from Lfs by enterocytes as well as Lf bioactivities, including effects on intestinal cell proliferation and differentiation, IL-18 secretion, TGF-beta 1 transcription, and growth of enteropathogenic Escherichia coli (EPEC). Composition of the Lfs varies; some only contain a major Lf band (similar to 80 kDa), and some also contain minor forms. All Lfs and iron from the Lfs were absorbed by Caco-2 cells, with various efficiencies. The bioactivities of the Lfs varied considerably, but there was no consistent trend. All Lfs promoted intestinal cell proliferation, secretion of IL-18, and transcription of TGF-beta 1. Some Lfs exhibited pro-differentiation effects on Caco-2 cells. Effects of pasteurization (62.5 degrees C for 30 min, 72 degrees C for 15 s, or 121 degrees C for 5 min) on integrity, uptake, and bioactivities were examined using Dicofarm, Tatua, and native bovine Lfs. Results show that pasteurization did not affect protein integrity, but variously affected uptake of Lf and its effects on intestinal proliferation, differentiation, and EPEC growth. To choose a Lf source for a clinical trial, assessment of bioactivities is recommended.

Automated summary

In this study, lactoferrin samples from various manufacturers were evaluated for purity, protein form, and bioactivities. Results showed that lactoferrins vary in composition and absorption efficiency, with different effects on intestinal cell proliferation, differentiation, and IL-18 secretion. Pasteurization had varying impacts on lactoferrin integrity, uptake, and bioactivities, indicating the importance of assessing bioactivities when choosing a lactoferrin source for clinical trials.