[en] The antioxidant and antibacterial activities of camel and bovine α-lactalbumin (α-La) in both calcium-loaded (holo) and calcium-depleted (apo) forms were investigated and compared. Antioxidant assay showed that camel and bovine α-La exhibited significant Ferric-reducing antioxidant power (FRAP), ferrous iron-chelating activity (FCA) and antiradical activities especially in their apo form. Camel apo α-La also exhibited attractive antibacterial activities against Gram-negative bacteria (Pseudomonas aeruginosa) and against fungal pathogens species (Penicillium bilaiae, Aspergillus tamari and Aspergillus sclerotiorum). Likewise, emulsifying properties (emulsification ability (EAI) and stability (ESI) indexes) and the surface characteristics (surface hydrophobicity, ζ-potential and interfacial tension) of the α-La were assessed. Maximum EAI were found at pH 7.0, with higher EAI values for the camel apo α-La (EAI ~19.5 m(2)/g). This behavior was explained by its relative high surface hydrophobicity and its greater efficiency to reduce the surface tension at the oil-water interface. Furthermore, emulsions were found to be more stable at pH 7.0 compared to pH 5.0 (ESI ~50%) due to the higher electrostatic repulsive forces between oil droplets at pH 7.0 in consistence with the ζ-potential results. This study concluded that the camel apo α-La has antibacterial, antioxidant, and emulsifying properties in agricultural and food industries.
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. Electronic address: roua_lajnaf@yahoo.fr.
Gharsallah, Houda; Alimentary Analysis Unit, National Engineering School of Sfax, BPW 3038 Sfax, Tunisia, Tunisian Olive Institute, University of Sfax, Tunisia.
Jridi, Mourad; National School of Engineering of Sfax (ENIS), University of Sfax, Laboratory of Enzyme Engineering and Microbiology, P.O. Box 1173, Sfax 3038, Tunisia, Higher Institute of Biotechnology of Beja, University of Jendouba, Beja, Tunisia.
Attia, Hamadi; Alimentary Analysis Unit, National Engineering School of Sfax, BPW 3038 Sfax, Tunisia.
Ayadi, Mohamed ; Alimentary Analysis Unit, National Engineering School of Sfax, BPW 3038 Sfax, Tunisia.
Language :
English
Title :
Antioxidant and antibacterial activities, interfacial and emulsifying properties of the apo and holo forms of purified camel and bovine α-lactalbumin.
Publication date :
15 December 2020
Journal title :
International Journal of Biological Macromolecules
Khalesi, M., Salami, M., Moslehishad, M., Winterburn, J., Moosavi-Movahedi, A.A., Biomolecular content of camel milk: a traditional superfood towards future healthcare industry. Trends Food Sci. Technol. 62 (2017), 49–58.
El-Agamy, E.I., Nawar, M., Shamsia, S.M., Awad, S., Haenlein, G.F.W., Are camel milk proteins convenient to the nutrition of cow milk allergic children?. Small Rumin. Res. 82 (2009), 1–6.
Hailu, Y., Hansen, E.B., Seifu, E., Eshetu, M., Ipsen, R., Kappeler, S., Functional and technological properties of camel milk proteins: a review. J. Dairy Res. 83 (2016), 422–429.
Lajnaf, R., Zouari, A., Trigui, I., Attia, H., Ayadi, M.A., Effect of different heating temperatures on foaming properties of camel milk proteins: a comparison with bovine milk proteins. Int. Dairy J., 104, 2020.
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.
Swaisgood H.E., O. R. Fennema, (eds.), 3rd ed. Food Chem., 1996, Marcel Dekker, New York, NY, 841–878.
Uchida, Y., Shimatani, M., Mitsuhashi, T., Koutake, M., Process for Preparing a Fraction Having a High Content of α-Lactalbumin From Whey and Nutritional Compositions Containing Such Fractions, US Patent. vol. 5, 1996, 503–864 (Urbisinov).
Merin, U., Bernstein, S., Yagil, R., Van Creveld, C., Lindner, P., Gollop, N., communication, Short, A comparative study of milk serum proteins in camel (Camelus dromedarius) and bovine colostrum. Livestock Production Sci 67 (2001), 297–301.
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.
Omar, A., Harbourne, N., Oruna-Concha, M.J., Quantification of major camel milk proteins by capillary electrophoresis. Int. Dairy J. 58 (2016), 31–35.
Lajnaf, R., Picart-Palmade, L., Attia, H., Marchesseau, S., Ayadi, M.A., The effect of pH and heat treatments on the foaming properties of purified α-lactalbumin from camel milk. Colloids Surfaces B Biointerfaces 156 (2017), 55–61.
Hill, R.L., Brew, K., Lactose synthetase. Adv. Enzymol. Relat. Areas Mol. Biol. 43 (1975), 411–490.
Calderone, V., Giuffrida, M.G., Viterbo, D., Napolitano, L., Fortunato, D., Conti, A., Acharya, K.R., Amino acid sequence and crystal structure of buffalo α-lactalbumin. FEBS Lett. 394 (1996), 91–95.
Beg, O.U., Bahr-Lindström, H. von, Zaidi, Z.H., Jörnvall, H., The primary structure of alpha-lactalbumin from camel milk. Eur. J. Biochem. 147 (1985), 233–239.
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(1), 2010, 43.
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.
Lajnaf, R., Picart-Palmade, L., Attia, H., Marchesseau, S., Ayadi, M.A., Foaming and adsorption behavior of bovine and camel proteins mixed layers at the air/water interface. Colloids Surfaces B Biointerfaces. 151 (2016), 287–294.
Ellouze, M., Lajnaf, R., Zouari, A., Attia, H., Ayadi, M.A., Vial, C., Camel α-lactalbumin at the oil-water interface: effect of protein concentration and pH change on surface characteristics and emulsifying properties. Colloids Surfaces B Biointerfaces, 189, 2020.
Ellouze, M., Vial, C., Attia, H., Ayadi, M.A., Camel α-lactalbumin at the oil-water interface: effect of pH and heat treatment on the structure, surface characteristics and emulsifying properties. LWT-Food Sci. Technol., 116, 2019, 108550.
Felfoul, I., Jardin, J., Gaucheron, F., Attia, H., Ayadi, M.A., Proteomic profiling of camel and cow milk proteins under heat treatment. Food Chem. 216 (2017), 161–169.
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.
Lajnaf, R., Picart-Palmade, L., Cases, E., Attia, H., Marchesseau, S., Ayadi, M.A., The foaming properties of camel and bovine whey: the impact of pH and heat treatment. Food Chem. 240 (2018), 295–303.
Muller, A., Chaufer, B., Merin, U., Daufin, G., Purification of alpha-lactalbumin from a prepurified acid whey: ultrafiltration or precipitation. Lait 83 (2003), 439–451.
Muller, A., Chaufer, B., Merin, U., Daufin, G., Prepurification of alpha-lactalbumin with ultrafiltration ceramic membranes from acid casein whey: study of operating conditions. Lait 83 (2003), 111–129.
Yüksel, Z., Erdem, Y.K., Detection of the milk proteins by RP-HPLC. GIDA-Journal Food. 35 (2010), 5–11.
Svensson, M., Håkansson, A., Mossberg, A.K., Linse, S., Svanborg, C., Conversion of alpha-lactalbumin to a protein inducing apoptosis. Proc. Natl. Acad. Sci. U. S. A. 97 (2000), 4221–4226.
Lam, R.S.H., Nickerson, M.T., The effect of pH and temperature pre-treatments on the structure, surface characteristics and emulsifying properties of alpha-lactalbumin. Food Chem. 173 (2015), 163–170.
Bersuder, P., Hole, M., Smith, G., Antioxidants from a heated histidine-glucose model system. I: investigation of the antioxidant role of histidine and isolation of antioxidants by high-performance liquid chromatography. J. Am. Oil Chem. Soc. 75 (1998), 181–187.
Benzie, I.F.F., Strain, J.J., [2] Ferric reducing/antioxidant power assay: direct measure of total antioxidant activity of biological fluids and modified version for simultaneous measurement of total antioxidant power and ascorbic acid concentration. Methods Enzymol, 1999, Elsevier, 15–27.
Kumar, D., Chatli, M.K., Singh, R., Mehta, N., Kumar, P., Antioxidant and antimicrobial activity of camel milk casein hydrolysates and its fractions. Small Rumin. Res. 139 (2016), 20–25.
Boyer, R.F., J. McCleary, C., Superoxide ion as a primary reductant in ascorbate-mediated ferretin iron release. Free Radic. Biol. Med. 3 (1987), 389–395.
Al-Shamsi, K.A., Mudgil, P., Hassan, H.M., Maqsood, S., Camel milk protein hydrolysates with improved technofunctional properties and enhanced antioxidant potential in in vitro and in food model systems. J. Dairy Sci., 2017, 1–14.
Håkansson, A., Svensson, M., Mossberg, A., Sabharwal, H., Linse, S., Lazou, I., LoÈnnerdal, B., Svanborg, C., A folding variant of α-lactalbumin with bactericidal activity against Streptococcus pneumoniae. Mol. Microbiol. 35 (2000), 589–600.
Lajnaf, R., Trigui, I., Samet-Bali, O., Attia, H., Ayadi, M.A., Comparative study on emulsifying and physico-chemical properties of bovine and camel acid and sweet wheys. J. Food Eng., 109741, 2019.
Pearce, K.N., Kinsella, J.E., Emulsifying properties of proteins: evaluation of a turbidimetric technique. J. Agric. Food Chem. 26 (1978), 716–723.
Lam, R.S.H., Nickerson, M.T., The effect of pH and temperature pre-treatments on the physicochemical and emulsifying properties of whey protein isolate. LWT-Food Sci. Technol. 60 (2015), 427–434.
Kappeler, S.R., Heuberger, C., Farah, Z., Puhan, Z., Expression of the peptidoglycan recognition protein, PGRP, in the lactating mammary gland. J. Dairy Sci. 87 (2004), 2660–2668.
Elias, R.J., McClements, D.J., Decker, E.A., Antioxidant activity of cysteine, tryptophan, and methionine residues in continuous phase β-lactoglobulin in oil-in-water emulsions. J. Agric. Food Chem. 53 (2005), 10248–10253.
Arcan, I., Yemenicioğlu, A., Antioxidant activity of protein extracts from heat-treated or thermally processed chickpeas and white beans. Food Chem. 103 (2007), 301–312.
Alemán, A., Pérez-Santín, E., Bordenave-Juchereau, S., Arnaudin, I., Gómez-Guillén, M.C., Montero, P., Squid gelatin hydrolysates with antihypertensive, anticancer and antioxidant activity. FRIN 44 (2011), 1044–1051.
Corrochano, A.R., Sariçay, Y., Arranz, E., Kelly, P.M., Buckin, V., Giblin, L., Comparison of antioxidant activities of bovine whey proteins before and after simulated gastrointestinal digestion. J. Dairy Sci. 102 (2019), 54–67.
Tang, L., Zhang, Y., Qian, Z., Shen, X., The mechanism of Fe2+-initiated lipid peroxidation in liposomes: the dual function of ferrous ions, the roles of the pre-existing lipid peroxides and the lipid peroxyl radical. Biochem. J. 352 (2000), 27–36.
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.
Murakami, K., Berliner, L.J., A distinct zinc-binding site in the alpha-lactalbumins regulates calcium binding. Is there a physiological role for this control?. Biochemistry 22 (1983), 3370–3374.
Baumy, J.J., Brule, G., Binding of bivalent cations to α-lactalbumin and β-lactoglobulin: effect of pH and ionic strength. Lait 68 (1988), 33–48.
Sedaghati, M., Ezzatpanah, H., Mashhadi Akbar Boojar, M., Tajabadi Ebrahimi, M., β-Lactoglobulin and α-lactalbumin hydrolysates as sources of antibacterial peptides. J. Agric. Sci. Technol. 16 (2014), 1587–1600.
Svensson, M., Sabharwal, H., Håkansson, A., Mossberg, A.-K., Lipniunas, P., Leffler, H., Svanborg, C., Linse, S., Molecular characterization of α–lactalbumin folding variants that induce apoptosis in tumor cells. J. Biol. Chem. 274 (1999), 6388–6396.
Uversky, V.N., El-Fakharany, E.M., Abu-Serie, M.M., Almehdar, H.A., Redwan, E.M., Divergent anticancer activity of free and formulated camel milk α-lactalbumin. Cancer Investig. 35 (2017), 610–623.
Breydo, L., Almehdar, H.A., El-Fakharany, E.M., Redwan, E.M., Uversky, V.N., Not all AMLETs are made equal: complexes of cow and camel α-lactalbumin with oleic acid show different structure and stability. J. Biomol. Struct. Dyn. 36 (2018), 4405–4412.
Redington, J.M., Breydo, L., Almehdar, H.A., Redwan, E.M., Uversky, V.N., α-Lactalbumin: of camels and cows. Protein Pept. Lett. 23 (2016), 1072–1080.
McClements, D.J., Food Emulsions: Principles, Practices, and Techniques. 2004, CRC.
Momen, S., Salami, M., Emam-Djomeh, Z., Hosseini, E., Sheibani, N., Moosavi-Movahedi, A.A., Effect of dry heating on physico-chemical, functional properties and digestibility of camel whey protein. Int. Dairy J. 86 (2018), 9–20.
Dickinson, E., Matsumura, Y., Proteins at liquid interfaces: role of the molten globule state. Colloids Surfaces B Biointerfaces 3 (1994), 1–17.
Ibanoglu, E., Ibanoglu, Ş., Foaming behaviour of EDTA-treated α-lactalbumin. Food Chem. 66 (1999), 477–481.