Molecular Structure of Lactoferrin Influences the Thermal Resistance of Lactococcal Phages
| Autor: | Hany Geagea, Gabriel E. Remondetto, Muriel Subirade, Sylvain Moineau, Ahmed Gomaa |
|---|---|
| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
Circular dichroism Whey protein Hot Temperature 030106 microbiology Virulence Protein Structure Secondary 03 medical and health sciences chemistry.chemical_compound Cheese Molecule Animals Thermal stability Bacteriophages biology Lactoferrin Chemistry General Chemistry Hydrogen-Ion Concentration biology.organism_classification Lactic acid Lactococcus lactis 030104 developmental biology Milk Whey Proteins Biochemistry Fermentation biology.protein General Agricultural and Biological Sciences Bacteria |
| Zdroj: | Journal of agricultural and food chemistry. 65(10) |
| ISSN: | 1520-5118 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|