Abstract
Ovotransferrin (OVT) is a multi-functional protein showing over 50% homology with Bovine lactoferrin (BLF) and human lactoferrin (HLF), which have the potential to be a substitute for lactoferrin (LF) due to the limited production of LF. To explore the substitutability of OVT, the molecular properties and thermal stability of OVT, BLF and HLF were characterized because these properties will affect the processing quality and biological activities of protein products when exposed to different processing conditions (e.g., temperature, pH, ion strength). The results showed that although obviously different isoelectric point (5.31, 9.12 and 8.75 for OVT, BLF and HLF, respectively), particle size distribution and hydrophobicity were found, they exhibited good dispersity because of high potential value. They showed an endothermic peak at 80.64 °C, 65.71 °C and 90.01 °C, respectively, and the denaturation temperature varied at different pH and ionic strength. OVT and BLF were more susceptible to heating at pH 5.0 as reflected by the decline of denaturation temperature (21.78 °C shift for OVT and 5.81 °C shift for BLF), while HLF could remain stable. Compared with BLF, OVT showed higher secondary structure stability at pH 7.0 and 9.0 with heating. For example, the α-helix content of OVT changed from 20.35% to 15.4% at pH 7.0 after heating, while that of BLF changed from 20.05% to 6.65%. The increase on fluorescence intensity and redshifts on the maximum wavelength after heating indicated the changes of tertiary structure of them. The turbidity measurements showed that the thermal aggregation degree of OVT was lower than BLF and HLF at pH 7.0 (30.98%, 59.53% and 35.66%, respectively) and pH 9.0 (4.83%, 12.80% and 39.87%, respectively). This work demonstrated the similar molecular properties and comparable thermal stability of OVT to BLF and HLF, which can offer a useful reference for the substitute of LF by OVT.