Effect of high pressure on the structure and antibacterial activity of bovine lactoferrin treated in different media

Abstract

The effect of high-pressure treatment (400, 500 and 650 MPa) on the structure and activity of bovine lactoferrin in different iron-saturation forms has been studied by several techniques. The structural changes produced in lactoferrin by high-pressure were analysed by differential scanning calorimetry and fluorescence spectroscopy, and the immunoreactivity by ELISA. The effect of high-pressure was also studied on some biological properties of lactoferrin, such as iron binding capacity, retention of the bound iron, and antibacterial activity against Escherichia coli O157:H7. Results obtained indicate that treatment at 400 MPa does not substantially modify the conformation of lactoferrin, meanwhile treatments at 500 and 650 MPa greatly affect some of its properties. With respect to the antibacterial activity, the apo and native forms of lactoferrin maintain that activity against Esch. coli only after 400 MPa treatment.

The Multifaceted Roles of Bovine Lactoferrin: Molecular Structure, Isolation Methods, Analytical Characteristics, and Biological Properties

“…Thus, the composition of the secondary structure of bLF may vary with regard to the applied method of heat treatment. The temperature of denaturation and enthalpy change of denaturation of holo-LF is much higher than that of apo-LF, which suggests greater thermal resistance of iron-saturated forms of protein. , Application of high hydrostatic pressure as and alternative to heat treatment also confirmed much evident conformation stability of iron-saturated LF at extreme conditions compared to metal unsaturated LF …”

“…19,73 Application of high hydrostatic pressure as and alternative to heat treatment also confirmed much evident conformation stability of iron-saturated LF at extreme conditions compared to metal unsaturated LF. 74 Interestingly, relatively low temperatures are also capable of modifying protein biological functions. It was observed that LF storage of at 20 °C for 6 months significantly influenced the protein immunomodulatory function.…”

Effect of high hydrostatic pressure processing on the structure, functionality, and nutritional properties of food proteins: A review

“…Mazri et al (2012) observed that the denaturation rate of LFb under HHP treatment (450-700 MPa/20 • C/0-40 min) was the lowest in phosphate-buffered saline (PBS), followed by bovine milk and whey. However, Franco et al (2013) reported that HHP at 500 MPa (20 • C/15 min) caused a greater loss of LFb in milk than in PBS and whey. They also found out that the antimicrobial activity of LFb in its apo and native forms was maintained well in PBS after HHP treatment at 400 MPa but was completely lost after 500 MPa treatment (Franco et al, 2013).…”

“…(2013) reported that HHP at 500 MPa (20°C/15 min) caused a greater loss of LFb in milk than in PBS and whey. They also found out that the antimicrobial activity of LFb in its apo and native forms was maintained well in PBS after HHP treatment at 400 MPa but was completely lost after 500 MPa treatment (Franco et al., 2013).…”

Lactoferrin: properties and application. A review

“…In addition, pressure influences the lactoferrin structure and activity, its antimicrobial properties and ability to bind and hold iron. Under the action of 400 MPa, the lactoferrin structure does not change significantly, but treatment under 500 MPa and higher strongly affects LF properties, reduces its antimicrobial action [21]. For these reasons, the combined treatment of chicken breasts was used in the study.…”