[en] The aim of this work was to examine foaming and interfacial behavior of three milk protein mixtures, bovine α-lactalbumin-β-casein (M1), camel α-lactalbumin-β-casein (M2) and β-lactoglobulin-β-casein (M3), alone and in binary mixtures, at the air/water interface in order to better understand the foaming properties of bovine and camel milks. Different mixture ratios (100:0; 75:25; 50:50; 25:75; 0:100) were used during foaming tests and interfacial protein interactions were studied with a pendant drop tensiometer. Experimental results evidenced that the greatest foam was obtained with a higher β-casein amount in all camel and bovine mixtures. Good correlation was observed with the adsorption and the interfacial rheological properties of camel and bovine protein mixtures. The proteins adsorbed layers are mainly affected by the presence of β-casein molecules, which are probably the most abundant protein at interface and the most efficient in reducing the interfacial properties. In contrast of, the globular proteins, α-lactalbumin and β-lactoglobulin that are involved in the protein layer composition, but could not compact well at the interface to ensure foams creation and stabilization because of their rigid molecular structure.
Disciplines :
Food science
Author, co-author :
Lajnaf, Roua; Alimentary Analysis Unit, National Engineering School of Sfax, BPW 3038, Sfax, Tunisia, Montpellier University, UMR IATE, Place E. Bataillon, 34095 Montpellier Cedex 5, France.
Picart-Palmade, Laetitia; Montpellier University, UMR IATE, Place E. Bataillon, 34095 Montpellier Cedex 5, France.
Attia, Hamadi; Alimentary Analysis Unit, National Engineering School of Sfax, BPW 3038, Sfax, Tunisia.
Marchesseau, Sylvie; Montpellier University, UMR IATE, Place E. Bataillon, 34095 Montpellier Cedex 5, France.
Ayadi, Mohamed ; Alimentary Analysis Unit, National Engineering School of Sfax, BPW 3038, Sfax, Tunisia. Electronic address: ayadimedali@yahoo.fr.
Language :
English
Title :
Foaming and adsorption behavior of bovine and camel proteins mixed layers at the air/water interface.
[1] El-Agamy, E.I., Abou-Shloue, Z., Abdel-Kader, Y.I., Gel electrophoresis of proteins physicochemical characterization and vitamin C content of milk of different species. Alexandria J. Agric. Res. 43 (1998), 57–70.
[2] Ereifej, K.I., Alu'datt, M.H., Alkhalidy, H.A., Alli, I., Rababah, T., Comparison and characterisation of fat and protein composition for camel milk from eight Jordanian locations. Food Chem. 127 (2011), 282–289.
[3] Kappeler, S.R., Farah, Z., Puhan, Z., 5′-Flanking regions of camel milk genes are highly similar to homologue regions of other species and can be divided into two distinct groups. J. Dairy Sci. 86 (2003), 498–508.
[4] Kappeler, S., Farah, Z., Puhan, Z., Sequence analysis of Camelus dromedarius milk caseins. J. Dairy Res. 65 (1998), 209–222.
[5] Barzegar, A., Yousefi, R., Sharifzadeh, A., Dalgalarrondo, M., Chobert, J.M., Ganjali, M.R., Norouzi, P., Ehsani, M.R., Niasari-Naslaji, A., Saboury, A.A., Haertlé, T., Moosavi-Movahedi, A.A., Chaperone activities of bovine and camel β-caseins: importance of their surface hydrophobicity in protection against alcohol dehydrogenase aggregation. Int. J. Biol. Macromol. 42 (2008), 392–399.
[6] Laleye, L.C., Jobe, B., Wasesa, A.A.H., Comparative study on heat stability and functionality of camel and bovine milk whey proteins. J. Dairy Sci. 91 (2008), 4527–4534.
[7] Merin, U., Bernstein, S., Yagil, R., Van Creveld, C., Lindner, P., Gollop, N., Short communication A comparative study of milk serum proteins in camel (Camelus dromedarius) and bovine colostrum. Livest. Prod. Sci. 67 (2001), 297–301.
[8] Omar, A., Harbourne, N., Oruna-Concha, M.J., Quantification of major camel milk proteins by capillary electrophoresis. Int. Dairy J., 2016, 1–5.
[9] El-Hatmi, H., Girardet, J.M., Gaillard, J.L., Yahyaoui, M.H., Attia, H., Characterisation of whey proteins of camel (Camelus dromedarius) milk and colostrum. Small Rumin. Res. 70 (2007), 267–271.
[10] Beg, O.U., von Bahr-Lindström, H., Zaidi, Z.H., Jörnvall, H., The primary structure of alpha-lactalbumin from camel milk. Eur. J. Biochem. 147 (1985), 233–239.
[11] Atri, M.S., Saboury, A.A., Yousefi, R., Chobert, J., Haertle, T., Moosavi-Movahedi, A.A., Comparative study on heat stability of camel and bovine apo and holo α-lactalbumin. J. Dairy Res. 77 (2010), 43–49.
[12] Dickinson, E., Hydrocolloids at interfaces and the influence on the properties of dispersed systems. Food Hydrocoll. 17 (2003), 25–39.
[13] Borcherding, K., Lorenzen, P.C., Hoffmann, W., Schrader, K., Effect of foaming temperature and varying time/temperature-conditions of pre-heating on the foaming properties of skimmed milk. Int. Dairy J. 18 (2008), 349–358.
[14] Marinova, K.G., Basheva, E.S., Nenova, B., Temelska, M., Mirarefi, A.Y., Campbell, B., Ivanov, I.B., Physico-chemical factors controlling the foamability and foam stability of milk proteins: sodium caseinate and whey protein concentrates. Food Hydrocoll. 23 (2009), 1864–1876.
[15] Seta, L., Baldino, N., Gabriele, D., Lupi, F.R., De Cindio, B., Rheology and adsorption behaviour of β-casein and β-lactoglobulin mixed layers at the sunflower oil/water interface. Colloids Surf. A Physicochem. Eng. Asp. 441 (2014), 669–677.
[17] Dickinson, E., Milk protein interfacial layers and the relationship to emulsion stability and rheology. Colloids Surf. B Biointerfaces 20 (2001), 197–210.
[18] Brooker, B.E., Anderson, M., Andrews, A.T., The development of structure in whipped cream. Food Struct., 5, 1986, 12.
[19] Wüstneck, R., Krägel, J., Miller, R., Fainerman, V.B., Wilde, P.J., Sarker, D.K., Clark, D.C., Dynamic surface tension and adsorption properties of β-casein and β-lactoglobulin. Food Hydrocoll. 10 (1996), 395–405.
[20] Kappeler, S.R., Ackermann, M., Farah, Z., Puhan, Z., Sequence analysis of camel (Camelus dromedarius) lactoferrin. Int. Dairy J. 9 (1999), 481–486.
[21] Salami, M., Yousefi, R., Reza, M., Hadi, S., Chobert, J., Akbar, A., Sadat, M., Niasari-Naslaji, A., Ahmad, F., Haertle, T., Moosavi-Movahedi, A.A., Enzymatic digestion and antioxidant activity of the native and molten globule states of camel α-lactalbumin: possible significance for use in infant formula. Int. Dairy J. 19 (2009), 518–523.
[22] Felfoul, I., Lopez, C., Gaucheron, F., Attia, H., Ayadi, M.A., A laboratory investigation of cow and camel whey proteins deposition under different heat treatments. Food Bioprod. Process. 96 (2015), 256–263.
[23] Huppertz, T., Hennebel, J.B., Considine, T., Shakeel-Ur-Rehman, Kelly, A.L., Fox, P.F., A method for the large-scale isolation of β-casein. Food Chem. 99 (2006), 45–50.
[24] Laemmli, U.K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970), 680–685.
[25] Bobe, G., Beitz, D.C., Freeman, a. E., Lindberg, G.L., Separation and quantification of bovine milk proteins by reversed-phase high-performance liquid chromatography. J. Agric. Food Chem. 46 (1998), 458–463.
[26] Martinez, M.J., Carrera Sánchez, C., Rodríguez Patino, J.M., Pilosof, A.M.R., Interactions between β-lactoglobulin and casein glycomacropeptide on foaming. Colloids Surf. B Biointerfaces 89 (2012), 234–241.
[27] Ibanoglu, E., Ibanoglu, Ş., Foaming behaviour of EDTA-treated α-lactalbumin. Food Chem. 66 (1999), 477–481.
[28] Zhang, Z., Dalgleish, D.G., Goff, H.D., Effect of pH and ionic strength on competitive protein adsorption to air/water interfaces in aqueous foams made with mixed milk proteins. Colloids Surf. B Biointerfaces 34 (2004), 113–121.
[29] Slack, A.W., Amundson, C.H., Hill, C.G., Foaming and emulsifying characteristics of fractionated whey protein. J. Food Process. Preserv. 10 (1986), 81–88.
[30] Cases, E., Rampini, C., Cayot, P., Interfacial properties of acidified skim milk. J.Colloid Interface Sci. 282 (2005), 133–141.
[31] Salmen, S.H., Abu-Tarboush, H.M., Al-Saleh, A.A., Metwalli, A.A., Amino acids content and electrophoretic profile of camel milk casein from different camel breeds in Saudi Arabia. Saudi J. Biol. Sci. 19 (2012), 177–183.
[32] Salami, M., Moosavi-Movahedi, A.A., Moosavi-Movahedi, F., Ehsani, M.R., Yousefi, R., Farhadi, M., Niasari-Naslaji, A., Saboury, A.A., Chobert, J.-M., Haertlé, T., Biological activity of camel milk casein following enzymatic digestion. J. Dairy Res. 78 (2011), 471–478.
[33] Dickinson, E., Proteins at interfaces and in emulsions Stability, rheology and interactions. J. Chem. Soc. Faraday Trans. 94 (1998), 1657–1669.
[34] Robson, E.W., Dalgleish, D.G., Interfacial composition of sodium caseinate emulsions. J. Food Sci. 52 (1987), 1694–1698.
[35] Anderson, M., Brooker, B.E., Dickinson, E., Stainsby, G., Dairy foams. Adv. Food Emuls. Foam., 1988, 221–255.
[36] Dickinson, E., Horne, D.S., Phipps, J.S., Richardson, R.M., A neutron reflectivity study of the adsorption of beta-casein at fluid interfaces. Langmuir 9 (1993), 242–248.
[37] Mellema, M., Isenbart, J.G., Effect of acidification and heating on the rheological properties of oil-water interfaces with adsorbed milk proteins. J. Dairy Sci. 87 (2004), 2769–2778.
