Caseins; Lactoglobulins; Milk Proteins; Proteomics; Tandem Mass Spectrometry; Camel milk; Cow milk; Electrophoresis; Heat treatment; LC/MS; LC–MS/MS
Abstract :
[en] Cow and camel milk proteins before and after heat treatment at 80°C for 60min were identified using LC/MS and LC-MS/MS following monodimensional electrophoresis. The database used for the identification of camel and cow proteins was set from http://www.uniprot.org/. The obtained results showed that, after heating, camel milk at 80°C for 60min, camel α-lactalbumin (α-la) and peptidoglycan recognition protein (PGRP) were not detected while camel serum albumin (CSA) was significantly diminished. When heating cow milk at 80°C for 60min, α-lactalbumin (α-la) and β-lactoglobulin (β-lg) were not significantly detected. Moreover, 19 protein bands from SDS-PAGE were analyzed and a total of 45 different proteins were identified by LC-MS/MS. Casein fractions were kept intact under a heat treatment of 80°C during 60min of both camel and cow milks. Camel and bovine whey proteins were affected by a heat treatment of 80°C for 60min.
Disciplines :
Food science
Author, co-author :
Felfoul, Imène; Laboratoire Analyses, Valorisation et Sécurité des Aliments, Ecole Nationale d'Ingénieurs de Sfax, Université de Sfax, Route Soukra, Sfax 3038, Tunisia.
Jardin, Julien; INRA, UMR1253 STLO, 65 rue de Saint-Brieuc, F-35000 Rennes, France, Agrocampus Ouest, UMR 1253 STLO, 65 rue de Saint Brieuc, F-35000, France.
Gaucheron, Frédéric; INRA, UMR1253 STLO, 65 rue de Saint-Brieuc, F-35000 Rennes, France, Agrocampus Ouest, UMR 1253 STLO, 65 rue de Saint Brieuc, F-35000, France.
Attia, Hamadi; Laboratoire Analyses, Valorisation et Sécurité des Aliments, Ecole Nationale d'Ingénieurs de Sfax, Université de Sfax, Route Soukra, Sfax 3038, Tunisia.
Ayadi, Mohamed ; Laboratoire Analyses, Valorisation et Sécurité des Aliments, Ecole Nationale d'Ingénieurs de Sfax, Université de Sfax, Route Soukra, Sfax 3038, Tunisia. Electronic address: ayadimedali@yahoo.fr.
Language :
English
Title :
Proteomic profiling of camel and cow milk proteins under heat treatment.
Atri, M.S., Saboury, A.A., Yousefi, R., Dalgalarrondo, M., Chobert, J.M., Haertle, T., et al. Comparative study on heat stability of camel and bovine apo and holo α-lactalbumin. Journal of Dairy Research 77 (2010), 43–49.
Bradford, M.M., A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical Biochemistry 72 (1976), 248–254.
Corredig, M., Dalgleish, D.G., Effect of temperature and pH on the interactions of whey proteins with casein micelles in skim milk. Food Research International 29 (1999), 49–55.
de Jong, P., Impact and control of fouling in milk processing. Trends in Food Science & Technology 8 (1997), 401–405.
Donato, L., Guyomarc'H, F., Formation and properties of the whey protein/kappa-casein complexes in heated skim milk – A review. Lait 89 (2009), 3–29.
Dupont, D., Croguennec, T., Brodkorb, A., Kouaouci, R., Quantitation of proteins in milk and milk products. McSweeney, P.L.H., Fox, P.F., (eds.) Advanced dairy chemistry: Volume 1A: Proteins: Basic aspects, 4th ed., 2013, Springer, New York, 87–134.
El-Agamy, E.I., Effect of heat treatment on camel milk proteins with respect to antimicrobiol factors: A comparison with cow's and buffalo milk proteins. Food Chemistry 68 (2000), 227–232.
Farah, M., Is face recognition “special”? Evidence from neuropsychology. Behavioural Brain Research 76 (1996), 181–189.
Farah, Z., Effect of heat treatment on whey proteins of camel milk. Milchwissenschaft 41 (1986), 763–765.
Farivar, F., Moosavi-Movahedi, A.A., Salami, M., Bohlooli, M., Niasari-Naslaji, A., Heat-induced conformational unfolding of fatty acid-free and fatted camel serum albumin: A comparative study. Cell Biochemistry and Biophysics 67 (2013), 727–734.
Felfoul, I., Beaucher, E., Cauty, C., Attia, H., Gaucheron, F., Ayadi, M.A., Deposit generation during camel and cow milk heating: Microstructure and chemical composition. Food and Bioprocess Technology, 2016, 10.1007/s11947-016-1714-1.
Felfoul, I., Lopez, C., Gaucheron, F., Attia, H., Ayadi, M.A., Fouling behavior of camel and cow milks under different heat treatment. Food and Bioprocess Technology 8 (2015), 1771–1778.
Hinz, K., O'Connor, P., Huppertz, T., Ross, R.P., Kelly, A.L., Comparison of the principal proteins in bovine, caprine, buffalo, equine and camel milk. Journal of Dairy Research 79 (2012), 185–191.
Jovanović, S., Barać, M., Maćej, O., Whey proteins – Properties and possibility of application. Mljekarstvo 55 (2005), 215–233.
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. Journal of Dairy Science 86 (2003), 498–508.
Kim, D.A., Cornec, M., Narsimhan, G., Effect of thermal treatment on interfacial properties of β-lactoglobulin. Journal of Colloid and Interface Science 285 (2005), 100–109.
Laemmli, U.K., Cleavage of structural proteins during assembly of the head bacteriophage T4. Nature 277 (1970), 680–685.
Levieux, D., Levieux, A., El-Hatmi, H., Rigaudière, J.P., Immunochemical quantification of heat denaturation of camel (Camelus dromedarius) whey proteins. Journal of Dairy Research 73 (2006), 1–9.
Mal, G., Sena, D.S., Jain, V.K., Sahani, M.S., Therapeutic value of camel milk as a nutritional supplement for multiple drug resistant (MDR) tuberculosis patients. Israel Journal of Veterinary Medicine 61 (2006), 88–91.
Manzo, C., Nicolai, M.A., Pizzano, R., Thermal markers arising from changes in the protein component of milk. Food Control 51 (2015), 251–255.
Moro, A., Báez, G.D., Busti, P.A., Ballerini, G.A., Delorenzi, N.J., Effects of heat-treated β-lactoglobulin and its aggregates on foaming properties. Food Hydrocolloids 25 (2011), 1009–1015.
Pappa, E.C., Robertsona, J.A., Rigbya, N.M., Mellona, F., Kandarakisb, I., Mills, E.N.C., Application of proteomic techniques to protein and peptide profiling of Teléme cheese made from different types of milk. International Dairy Journal 18 (2008), 605–614.
Petit, J., Six, T., Moreau, A., Ronse, G., Delaplace, G., β-Lactoglobulin denaturation, aggregation and fouling in a plate heat exchanger: Pilot-scale experiments and dimensional analysis. Chemical Engineering Science 101 (2013), 432–450.
Roefs, S.P., De Kruif, K.G., A model for the denaturation and aggregation of β-lactoglobulin. European Journal of Biochemistry 226 (1994), 883–889.
Rüegg, M., Morr, U., Blanc, B., A calorimetric study of the thermal denaturation of whey proteins in simulated milk ultrafiltrate. Journal of Dairy Research 44 (1977), 509–520.
Shamsia, S.M., Nutritional and therapeutic properties of camel and human milk. International Journal of Genetics and Molecular Biology 1 (2009), 52–58.
Shevchenko, A., Wilm, M., Vorm, O., Mann, M., Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels. Analytical Chemistry 68 (1996), 850–858.
Singh, H., Heat-induced changes in casein, including interactions with whey proteins. Fox, P.F., (eds.) Heat induced changes in milk, 2nd ed., 1995, International Dairy Federation, Brussels, 86–104.
Zhang, L., Boeren, S., Smits, M., van Hooijdonk, T., Vervoort, J., Hettinga, K., Proteomic study on the stability of proteins in bovine, camel, and caprine milk sera after processing. Food Research International 82 (2016), 104–111.
