Related Experiment Video
Updated: Mar 7, 2026

Bacteriophage Effectiveness for Biocontrol of Foodborne Pathogens Evaluated via High-Throughput Settings
Published on: August 19, 2021
Molecular Structure of Lactoferrin Influences the Thermal Resistance of Lactococcal Phages
Hany Geagea, Ahmed Gomaa1, Gabriel Remondetto2
1Department of Food Science and Nutrition, National Research Centre , Cairo, Egypt.
Abstract:
The protective effect of whey proteins on phages of lactic acid bacteria during heat treatment limits the recycling of whey proteins into cheese. To investigate this protective effect, we used lactoferrin (LF) as a whey protein model as a result of its unique physicochemical properties and its antiviral activity. First, the thermal inactivation of lactococcal thermoresistant virulent phage P1532 was measured in LF at 95 °C and under different pH values. Phage inactivation results revealed a strong protective effect of LF on P1532 phage at pH 5 but none at pH 7. The structural conformational changes of LF were then monitored by Fourier transform infrared and circular dichroism spectroscopies. Spectroscopic analysis showed that LF was unfolded after heating at pH 7, while it preserved its tertiary and secondary structures when heated at pH 5. There is a direct correlation between the thermal stability of LF and its ability to protect P1532 phage from heat treatment.
Related Concept Videos
DNA Bacteriophages
Viral Replication: Lysogenic Cycle
Lysogenic Cycle of Bacteriophages
Lytic Cycle of Bacteriophages
Diversity of Archaea III
Diversity of Archaea IV

