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Caseinomacropeptide behaviour in a whey protein fractionation process based on α-lactalbumin precipitation

Published online by Cambridge University Press:  17 March 2011

Ayoa Fernández ,
Violeta Menéndez ,
Francisco A Riera  and
Ricardo Álvarez
Ayoa Fernández
Affiliation:
Department of Chemical Engineering and Environmental Technology, University of Oviedo, Julián Clavería 8, 33006 Oviedo, Spain
Violeta Menéndez
Affiliation:
Department of Chemical Engineering and Environmental Technology, University of Oviedo, Julián Clavería 8, 33006 Oviedo, Spain
Francisco A Riera*
Affiliation:
Department of Chemical Engineering and Environmental Technology, University of Oviedo, Julián Clavería 8, 33006 Oviedo, Spain
Ricardo Álvarez
Affiliation:
Department of Chemical Engineering and Environmental Technology, University of Oviedo, Julián Clavería 8, 33006 Oviedo, Spain
*
*For correspondence; e-mail: far@uniovi.es
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Abstract

This work studied the behaviour of caseinomacropeptide (CMP) in a whey protein fractionation process based on the selective precipitation of α-lactalbumin (α-la) in an acid medium. Three different acids (hydrochloric, citric and lactic) and different operating conditions (protein concentration, temperature and pH) were considered to perform the precipitation step. Under the optimised precipitation conditions obtained for α-la (pH 4, 55°C, initial α-la concentration around 12 g/l) CMP presents quite similar behaviour to that observed for β-lactoglobulin (β-lg), namely remaining in the supernatant fraction. However, at a lower pH value (3·5) the amount of precipitated CMP increases up to 72% when citric acid is added. This behaviour could be due to the fact that CMP is close to its isoelectric point, which allows a supernatant fraction enriched in β-lg that is almost free from the rest of proteins in sweet whey.

Keywords

Caseinomacropeptidewhey protein fractionationselective whey protein precipitation
Type
Research Article
Information
Journal of Dairy Research , Volume 78 , Issue 2 , May 2011 , pp. 196 - 202
Copyright
Copyright © Proprietors of Journal of Dairy Research 2011

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Footnotes

Dedicated to the memory of Professor José M. Concellón

References

Arnoldus, WP, Vermeer, P & Norde, W 2000 The thermal stability of immunoglobulin: unfolding and aggregation of a multi-domain protein. Biophysical Journal 78 394–404Google Scholar
Bramaud, C, Aimar, P & Daufin, G 1997a Optimization of a whey protein fractionation process based on the selective precipitation of α-lactalbumin. Lait 77 411–423CrossRefGoogle Scholar
Bramaud, C, Aimar, P & Daufin, G 1997b Whey protein fractionation: isoelectric precipitation of α-Lactalbumin under gentle heat treatment. Biotechnology and Bioengineering 56(4) 391–3973.0.CO;2-J>CrossRefGoogle ScholarPubMed
Brody, EP 2000 Biological activities of bovine glycomacropeptide. British Journal of Nutrition 84(Suppl.1 S) 39–46CrossRefGoogle ScholarPubMed
Casal, E, Corzo, N, Moreno, FJ & Olano, A 2005 Glycation of caseinmacropeptide. Food Chemistry 92(1) 33–36CrossRefGoogle Scholar
Chatterton, DEW, Smithers, G, Roupas, P & Brodkorb, A 2006 Bioactivity of β-lactoglobulin and α-lactalbumin – Technological implications for processing. International Dairy Journal 16 1229–1240CrossRefGoogle Scholar
Coolbear, KP, Elgar, DF & Ayers, JS 1996 Profiling of genetic variants of bovine κ-casein macropeptide by electrophoretic and chromatographic techniques. International Dairy Journal 6(11) 1055–1068CrossRefGoogle Scholar
Coolbear, KP, Elgar, DF, Coolbear, T & Ayers, JS 1996 Comparative study of methods for the isolation and purification of bovine κ-casein and its hydrolysis by chymosin. Journal of Dairy Research 63 61–71CrossRefGoogle ScholarPubMed
Elgar, DF, Norris, CS, Ayers, JS, Pritchard, M, Otter, DE & Palmano, KP 2000 Simultaneous separation and quantitation of the major bovine whey proteins including proteose peptone and caseinomacropeptide by reversed-phase high-performance liquid chromatography on polystyrene-divinylbenzene. Journal of Chromatography A 878 183–196CrossRefGoogle ScholarPubMed
ExPaSy Molecular Biology Server: http://www.expasy.org, June 2010Google Scholar
Farrell, HM Jr, Jimenez-Flores, R, Bleck, GT, Brown, EM, Butler, JE, Creamer, LK, Hicks, CL, Hollar, CM, Ng-Kwai-Hang, KF & Swaisgood, HE 2004 Nomenclature of the Proteins of Cows’ Milk-Sixth Revision. Journal of Dairy Science 87(6) 1641–1674CrossRefGoogle ScholarPubMed
Gezán-Guiziou, G, Daufin, G, Timmer, M, Allersma, D & Van der Horst, C 1999 Process steps for the preparation of purified fraction of α-lactalbumin and β-lactoglobulin from whey protein concentrates. Journal of Dairy Research 66 225–236CrossRefGoogle Scholar
Gumpen, S, Hegg, PO & Martens, M 1979 Thermal stabilisation of fatty acid serum albumin complexes studied by differencial scanning calorimetry. Biochimica et Biophysica Acta 574 189–198CrossRefGoogle Scholar
Konrad, G & Kleinschmidt, T 2008 A new method for isolation of native α-Lactalbumin from sweet whey. International Dairy Journal 18 47–54CrossRefGoogle Scholar
Korhonen, H 2009 Milk derived bioactive peptides: From science to applications. Journal of Functional Foods 1(2) 177–187CrossRefGoogle Scholar
Kreuß, M, Krause, I & Kulozik, U 2008 Separation of a glycosylated and non-glycosylated fraction of caseinomacropeptide using different anion-exchange stationary phases. Journal of Chromatography A 1208(1–2)126–132CrossRefGoogle ScholarPubMed
Kreuß, M, Krause, I & Kulozik, U 2009 Influence of glycosylation on foaming properties of bovine caseinomacropeptide. International Dairy Journal 19 715–720CrossRefGoogle Scholar
Léonil, L, Mollé, D, Fauquant, J, Maubois, RJ, Pearce, RJ & Bouhallab, S 1997 Characterization by ionization mass spectrometry of lactosyl-lactoglobulin conjugates formed during heat treatment of milk and whey and identification of one lactose-binding site. Journal of Dairy Science 80 2270–2281CrossRefGoogle ScholarPubMed
Lieske, B, Konrad, G & Kleinschmidt, TH 2004 Isolation of caseinomacropeptide from rennet whey by a multistage ultrafiltration process. III. Influence of pH in the first ultrafiltration-step on the chemical properties of isolated caseinomacropeptide. Milchwissenschaft 59(7–8) 408–410Google Scholar
López-Fandiño, R & Ramos, M 1992 Bovine caseinomacropeptide I. Physicochemical characteristics and biological activity. Revista Española de Ciencia y Tecnología de Alimentos 32 575–588Google Scholar
Lucena, ME, Álvarez, S, Menéndez, C, Riera, FA & Álvarez, R 2006 Beta-lactoglobulin removal from whey protein concentrates: Production of milk derivatives as a base for infant formulas. Separation and Purification Technology 52(2) 310–316CrossRefGoogle Scholar
Lucena, ME, Álvarez, S, Menéndez, C, Riera, FA & Álvarez, R 2007 Alpha-lactalbumin precipitation from commercial whey protein concentrates. Separation and Purification Technology 52(3) 446–453Google Scholar
Madureira, AR, Tavares, T, Gomes, AMP, Pintado, ME & Malcata, FX 2010 Invited review: Physiological properties of bioactive peptides obtained from whey proteins. Journal of Dairy Science 93(2) 437–455CrossRefGoogle ScholarPubMed
Martín-Diana, AB, Fraga, MJ & Fontecha, J 2002 Isolation and characterisation of caseinmacropeptide from bovine, ovine and caprine cheese whey. European Food Research and Technology 214(4) 282–286CrossRefGoogle Scholar
Mollé, D & Léonil, J 1995 Heterogeneity of the bovine κ-casein caseinomacropeptide resolved by liquid chromatography on-line with electrospray ionization mass spectrometry. Journal of Chromatography A 708(2) 223–230CrossRefGoogle ScholarPubMed
Mollé, D & Léonil, J 2005 Quantitative determination of bovine κ-casein macropeptide in dairy products by liquid chromatography/electrospray coupled to mass spectrometry (LC-ESI/MS) and liquid chromatography/electrospray coupled to tandem mass spectrometry (LC-ESI/MS/MS). International Dairy Journal 15(5) 419–428CrossRefGoogle Scholar
Nakano, T & Ozimek, L 2000 Purification of glycomacropeptide from dialyzed and non-dialyzed sweet whey by anion-exchange chromatography at different pH-values. Biotechnology Letters 22(13) 1081–1086CrossRefGoogle Scholar
Pearce, RJ 1983 Thermal separation of β-Lactoglobulin and α-Lactalbumin in bovine cheddar cheese whey. Australian Journal of Dairy Technology 38 144–149Google Scholar
Permyakov, EA & Berliner, LJ 2000 α-Lactalbumin: structure and function. FEBS Letters 473 269–274CrossRefGoogle ScholarPubMed
Resmini, P, Pellegrino, L, Andreini, R & Prati, F 1989 Determinazione delle sieroproteine solubili del latte per HPLC in fase inverse. Scienza e Tecnica Lattiero-Casearia 40 7–23Google Scholar
Saito, T, Yamaji, A & Itoh, T 1991 A new isolation method of caseinoglycopeptide from sweet cheese whey. Journal of Dairy Science 74 2831–2837CrossRefGoogle Scholar
Smithers, GW 2008 Whey and whey proteins – From ‘gutter-to-gold’. International Dairy Journal 18 695–704CrossRefGoogle Scholar
Thomä, C, Krause, I & Kulozik, U 2006 Precipitation behaviour of caseinomacropeptide and their simultaneous determination with whey proteins by RP-HPLC. International Dairy Journal 16(4) 285–293CrossRefGoogle Scholar
Thomä-Worringer, C, Sorensen, J & López-Fandiño, R 2006 Health effects and technological features of caseinomacropeptide. International Dairy Journal 16 1324–1333CrossRefGoogle Scholar
Tolkach, A & Kulozik, U 2005 Fractionation of whey proteins and caseinomacropeptide by means of enzymatic crosslinking and membrane separation techniques. Journal of Food Engineering 67(1–2) 13–20CrossRefGoogle Scholar