Heat Stability of Bovine Lactoferrin at Acidic pH

Native, but not thermally denatured lactoferrin solubilizes iron in the presence of bicarbonate ions

“…However, the thermal treatment of Lf reduces some of its biological activities (Kussendrager 1994;Oria et al 1993;Paulsson et al 1993). The thermal denaturation of Lf has been well studied under many experimental conditions, including different pH values, buffers and concentrations of buffer salts (Abe et al 1991;Kawakami et al 1992). When Lf was heated near its isoelectric point (Table 3), the denaturation temperature (about 65°C) was consistent with that in the literature (Hu et al 2008).…”

Dietary administration of bovine lactoferrin influences the immune ability of the giant freshwater prawn Macrobrachium rosenbergii (de Man) and its resistance against Aeromonas hydrophila infection and nitrite stress

“…For a compound such as Lf to increase resistance against diseases, when administered as a feed additive, it must withstand the feed production conditions, pass unaltered through the digestive tract and be absorbed in a form capable of triggering protective responses in the prawn. Lf is resistant to high temperatures [37] and it is able to bind iron at pH levels as low as 2.2 [38]. It is also relatively resistant to proteolytic degradation [39], thus indicating that it could overcome the feed production conditions, the acid gastric fluids as well as proteolytic attack in the gut.…”

Effects of lactoferrin on non-specific immune responses of gilthead seabream (Sparus auratus L.)

“…Furthermore, Lf is resistant to high temperatures [54] and is also relatively resistant to proteolytic degradation [39], suggesting that it could survive feed production conditions, acid gastric fluids and the gut proteolytic attack [22].…”