Thermal stability and in vitro biological fate of lactoferrin-polysaccharide complexes.

Lactoferrin (LF) is a thermally sensitive iron-binding globular glycoprotein. Heat treatment can induce its denaturation and aggregation and thus affect its functional activity. In this study, carrageenan (CG), xanthan gum (XG) and locust bean gum (LBG), allowed to apply in infant food, were used to form protein-polysaccharide complexes to improve the thermal stability of LF. Meanwhile, in vitro simulated infant digestion and absorption properties of LF were also estimated. The results showed that the complexes formed by CG and XG with LF (LF-CG and LF-XG) could significantly inhibit the loss of α-helix structure of LF against heating. LF-CG and LF-LBG could protect LF from digestion in simulated infant gastric fluid and slow down the degradation of LF under the simulated intestinal conditions. Besides, LF, LF-CG and LF-XG showed no adverse effects on the growth of Caco-2 cells in the LF concentration range of 10-300 µg/mL, and LF-XG exhibited better beneficial to improve the cell uptake of the digestive product than the other protein-polysaccharides at the LF concentration of 100 µg/mL. This study may provide a reference for the enhancement of thermal processing stability of LF and development infant food ingredient with high nutrients absorption efficiency in the gastrointestinal environment in the future.

Digestive properties and peptide profiles exhibited significant differences between skim camel milk and bovine milk powder after static in vitro simulated infant gastrointestinal digestion.

This study aims to analyze the differences in digestion properties and peptide profiles between the skim camel and bovine milk powder after static in vitro simulated infant gastrointestinal digestion. The hydrolysis degree of camel milk proteins exceeded by 13.18% that of bovine milk. The concentration and release rate of free amino groups in the camel milk digesta was higher than that of bovine milk powder, which was likely due to the higher ß-/αs-casein ratio and larger casein micelle size in camel milk. Camel milk powder presented higher ß-CN coverage and comparatively shorter bioactive peptides compared to bovine milk powder. The anti-inflammatory peptide KVLPVPQ displayed the highest abundance in camel milk powder. Outcomes of this study showed that camel milk proteins possessed superior digestibility and unique peptides, which outlined the potential nutritional implications of camel milk for infants.