Thermal behavior of bovine lactoferrin in water and its relation to bacterial interaction and antibacterial activity.

Heat-induced enthalpy changes in different forms of bovine lactoferrin in water were examined by differential scanning calorimetry. Two thermal transitions with varying enthalpies were observed, depending on the iron-binding status of the protein. Iron-saturated lactoferrin was more resistant to heat-induced changes than was the apolactoferrin. Native lactoferrin had two transitional peaks, and pasteurization affected only the low temperature transition. Iron-saturated lactoferrin revealed a single transitional peak that was resistant to pasteurization. However, both protein forms were completely denatured by UHT. The effect of pasteurization and UHT on the protein interaction capacity with bacteria was examined in a 125I-labeled lactoferrin binding-inhibition assay. The ability of native and iron-saturated lactoferrins to bind various bacterial species was unaffected by pasteurization. However, UHT treatment decreased this interaction capacity. Native lactoferrins, both unheated and pasteurized, showed similar antibacterial properties and moderately inhibited Escherichia coli. However, this inhibitory capacity was lost after UHT treatment. Finally, iron-saturated lactoferrin did not inhibit bacterial growth; neither pasteurization nor UHT could change this property. Thus, UHT seems to affect structural as well as certain biological properties of both native and iron-saturated bovine lactoferrins, and pasteurization seems to be a treatment of choice for products containing this protein.