Milk fat globule membrane glycoproteins: Valuable ingredients for lactic acid bacteria encapsulation?

The membrane (Milk Fat Globule Membrane – MFGM) surrounding the milk fat globule is becoming increasingly studied for its use in food applications due to proven nutritional and technological properties. This review focuses first on current researches which have been led on the MFGM structure and composition and also on laboratory and industrial purification and isolation methods developed in the last few years. The nutritional, health benefits and techno-functional properties of the MFGM are then discussed. Finally, new techno-functional opportunities of MFGM glycoproteins as a possible ingredient for Lactic Acid Bacteria (LAB) encapsulation are detailed. The ability of MFGM to form liposomes entrapping bioactive compounds has been already demonstrated. One drawback is that liposomes are too small to be used for bacteria encapsulation. For the first time, this review points out the numerous advantages to use MFGM glycoproteins as a protecting, encapsulating matrix for bacteria and especially for LAB.     

Physicochemical and techno-functional properties of acid-aided pH-shifted protein isolate from over-salted duck egg (Anas platyrhucus) albumen

Here, potential physicochemical and techno-functional properties of the albumen protein recovered from over-salted albumen by an effective acid-aided pH-shift process (POA) were tested in comparison with the fresh albumen (FA) and albumen protein recovered from fresh albumen by acid-aided pH-shift process (PFA). POA contained 66.73% protein and 11.30% sodium (dry basis). Surface hydrophobicities of PFA and POA were higher than FA (P < 0.05), whereas the reactive sulfhydryl content of FA was higher than PFA and POA (P < 0.05). PFA had the highest whiteness followed by POA and FA, respectively. Single endothermic peak in DSC thermogram was found at 86.86, 89.67 and 98.96 °C for FA, PFA and POA, respectively. Long-term salting impaired the solubility, viscosity, emulsifying activity and gelation but not for foaming of albumen protein isolate. FA can be softly gelled with continuously packed structure, whereas PFA and POA underwent agglutination to form white clot suspension with spongy network.