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Abstract:

The aim of this work was to evaluate the effect of the presence of casein glycomacropeptide (CMP) on the in vitro digestibility and potential allergenicity of β-lactoglobulin (β-lg)-CMP mixtures. The digestion products were analyzed by RP-HPLC and RP-HPLC-ESI-MS/MS. The potential allergenicity of the digestion products was studied by human IgE binding by inhibition ELISA with serum samples from children with clinical allergic symptoms to β-lg. No differences were observed by HPLC in the mixtures hydrolysates due to CMP-β-lg interactions. RP-HPLC-ESI-MS/MS results showed different peptides occurring in the mixtures hydrolysates. Additionally, it was observed a significant reduction of β-lg IgE binding in the presence of CMP. The disappearance of epitopes in the digested mixtures could explain the lower IgE binding observed in these systems compared to β-lg. It can be concluded that the presence of CMP in products containing β-lg may modify the digestion products that may reduce the potential allergenicity of β-lg. © 2015 Elsevier Ltd. All rights reserved.

Registro:

Documento: Artículo
Título:Reduced β-lactoglobulin IgE binding upon in vitro digestion as a result of the interaction of the protein with casein glycomacropeptide
Autor:Martinez, M.J.; Martos, G.; Molina, E.; Pilosof, A.M.R.
Filiación:Departamento de Industrias, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Avenida Intendente Güiraldes s/n, Buenos Aires, Argentina
Instituto de Investigación en Ciencias de Alimentación (CIAL), CSIC-UAM, C/ Nicolás Cabrera 9, Madrid, 28049, Spain
European Commission, Joint Research Centre, Institute for Reference Materials and Measurements, Retieseweg 111, Geel, B-2440, Belgium
Palabras clave:Allergenicity; Digestion; Interactions; Allergens; Beam plasma interactions; Casein; Sludge digestion; Allergenicity; Allergic symptoms; Beta-lactoglobulin; Casein glycomacropeptide; Digestion products; IgE bindings; In-vitro digestions; Serum samples; Mixtures; beta lactoglobulin; casein; casein glycomacropeptide; glycoprotein; immunoglobulin E; unclassified drug; allergen; casein; caseinomacropeptide; epitope; immunoglobulin E; lactoglobulin; peptide fragment; allergenicity; Article; complex formation; differential scanning calorimetry; digestion; freeze drying; high performance liquid chromatography; human; immunogenicity; immunoreactivity; in vitro study; light scattering; nonhuman; particle size; protein binding; protein expression; protein function; protein protein interaction; stomach juice; tandem mass spectrometry; child; digestion; electrospray mass spectrometry; enzyme linked immunosorbent assay; immunology; metabolism; milk allergy; Allergens; Caseins; Child; Chromatography, High Pressure Liquid; Digestion; Enzyme-Linked Immunosorbent Assay; Epitopes; Humans; Immunoglobulin E; Lactoglobulins; Milk Hypersensitivity; Peptide Fragments; Spectrometry, Mass, Electrospray Ionization; Tandem Mass Spectrometry
Año:2016
Volumen:192
Página de inicio:943
Página de fin:949
DOI: http://dx.doi.org/10.1016/j.foodchem.2015.07.097
Título revista:Food Chemistry
Título revista abreviado:Food Chem.
ISSN:03088146
CODEN:FOCHD
CAS:beta lactoglobulin, 9045-23-2; casein, 9000-71-9; immunoglobulin E, 37341-29-0; Allergens; caseinomacropeptide; Caseins; Epitopes; Immunoglobulin E; Lactoglobulins; Peptide Fragments
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03088146_v192_n_p943_Martinez

Referencias:

  • Adams, S.L., Barnett, D., Walsh, B.J., Pearce, R.J., Hill, D.J., Howden, M.E.H., Human IgE-binding synthetic peptides of bovine β-lactoglobulin and α-lactalbumin. in vitro cross-reactivity of the allergens (1991) Immunology and Cell Biology, 69, pp. 191-197
  • Bossios, A., Theodoropoulou, M., Mondoulet, L., Rigby, N.M., Papadopoulos, N.G., Bernard, H., Effect of simulated gastro-duodenal digestion on the allergenic reactivity of beta-lactoglobulin (2011) Clinical and Translational Allergy, 1 (6), pp. 1-11
  • Brody, E.P., Biological activities of bovine glycomacropeptide (2000) British Journal of Nutrition, 84 (1), pp. S39-S46
  • Corzo-Martínez, M., Soria, A.C., Belloque, J., Villamiel, M., Moreno, F.J., Effect of glycation on the gastrointestinal digestibility and immunoreactivity of bovine [beta]-lactoglobulin (2010) International Dairy Journal, 20 (11), pp. 742-752
  • Chatterton, D.E.W., Rasmussen, J.T., Heegaard, C.W., Sørensen, E.S., Petersen, T.E., In vitro digestion of novel milk protein ingredients for use in infant formulas: Research on biological functions (2004) Trends in Food Science & Technology, 15, pp. 373-383
  • El-Salam, M.H.A., El-Shibiny, S., Buchheim, W., Characteristics and potential uses of the casein macropeptide (1996) International Dairy Journal, 6 (4), pp. 327-341
  • Foegeding, E.A., Davis, J.P., Doucet, D., McGuffey, M.K., Advances in modifying and understanding whey protein functionality (2002) Trends in Food Science & Technology, 13 (5), pp. 151-159
  • Hambling, S.G., Mc Alpine, A.S., Sawyer, L., β-Lactoglobulin (1992) Advanced Dairy chemistry-1: Proteins, pp. 141-190. , P.F. Fox (Ed.), London: Elsevier Applied Science
  • Harnsilawat, T., Pongsawatmanit, R., McClements, D.J., Characterization of β-lactoglobulin-sodium alginate interactions in aqueous solutions: A calorimetry, light scattering, electrophoretic mobility and solubility study (2006) Food Hydrocolloids, 20, pp. 577-585
  • Hattori, M., Miyakawa, S., Ohama, Y., Kawamura, H., Yoshida, T., To-o, K., Reduced immunogenicity of β-lactoglobulin by conjugation with acidic oligosaccharides (2004) Journal of Agricultural and Food Chemistry, 52 (14), pp. 4546-4553
  • Hattori, M., Numamoto, K.-I., Kobayashi, K., Takahashi, K., Fnctional canges in β-lactoglobulin by conjugation with cationic saccharides (2000) Journal of Agricultural and Food Chemistry, 48 (6), pp. 2050-2056
  • Heinzmann, A., Blattmann, S., Spuergin, P., Forster, J., Deichmann, K.A., The recognition pattern of sequential B cell epitopes of beta-lactoglobulin does not vary with the clinical manifestations of cow's milk allergy (1999) International Archives of Allergy and Immunology, 120, pp. 280-286
  • Järvinen, K.-M., Chatchatee, P., Bardina, L., Beyer, K., Sampson, H.A., IgE and IgG binding epitopes on α-lactalbumin and β-lactoglobulin in cow's milk allergy (2001) International Archives of Allergy and Immunology, 126, pp. 111-118
  • Jiménez-Saiz, R., Belloque, J., Molina, E., López-Fandiño, R., Human immunoglobulin e (IgE) binding to heated and glycated ovalbumin and ovomucoid before and after in vitro digestion (2011) Journal of Agricultural and Food Chemistry, 59 (18), pp. 10044-10051
  • Jiménez-Saiz, R., López-Expósito, I., Molina, E., López-Fandiño, R., IgE-binding and in-vitro gastrointestinal digestibility of egg allergens in the presence of polysaccharides (2013) Food Hydrocolloids, 30 (2), pp. 597-605
  • Jiménez-Saiz, R., Martos, G., Carrillo, W., López-Fandiño, R., Molina, E., Susceptibility of lysozyme to in-vitro digestion and immunoreactivity of its digests (2011) Food Chemistry, 127 (4), pp. 1719-1726
  • Jiménez-Saiz, R., Pizones Ruiz-Henestrosa, V.M., López-Fandiño, R., Molina, E., In vitro digestibility and allergenicity of emulsified hen egg (2012) Food Research International, 48, pp. 404-409
  • Kobayashi, K., Hirano, A., Ohta, A., Yoshida, T., Takahashi, K., Hattori, M., Reduced immunogenicity of β-lactoglobulin by conjugation with carboxymethyl dextran differing in molecular weight (2001) Journal of Agricultural and Food Chemistry, 49 (2), pp. 823-831
  • Kreuß, M., Strixner, T., Kulozik, U., The effect of glycosylation on the interfacial properties of bovine caseinomacropeptide (2009) Food Hydrocolloids, 23 (7), pp. 1818-1826
  • Mandalari, G., Adel-Patient, K., Barkholt, V., Baro, C., Bennett, L., Bublin, M., In vitro digestibility of β-casein and β-lactoglobulin under simulated human gastric and duodenal conditions: A multi-laboratory evaluation (2009) Regulatory Toxicology and Pharmacology, 55 (3), pp. 372-381
  • Martinez, M.J., Carrera Sánchez, C., Rodríguez Patino, J.M., Pilosof, A.M.R., Interactions in the aqueous phase and adsorption at the air-water interface of caseinoglycomacropeptide (GMP) and β-lactoglobulin mixed systems (2009) Colloids and Surfaces B: Biointerfaces, 68, pp. 39-47
  • Martinez, M.J., Carrera Sánchez, C., Rodríguez Patino, J.M., Pilosof, A.M.R., Interactions between β-lactoglobulin and casein glycomacropeptide on foaming (2012) Colloids and Surfaces B: Biointerfaces, 89, pp. 234-241
  • Martinez, M.J., Farías, M.E., Pilosof, A.M.R., The dynamics of heat gelation of casein glycomacropeptide-β-lactoglobulin mixtures as affected by interactions in the aqueous phase (2010) International Dairy Journal, 20, pp. 580-588
  • Martos, G., Contreras, P., Molina, E., López-Fandiño, R., Egg white ovalbumin digestion mimicking physiological conditions (2010) Journal of Agricultural and Food Chemistry, 58, pp. 5640-5648
  • Martos, G., López-Fandiño, R., Molina, E., Immunoreactivity of hen egg allergens: Influence on in vitro gastrointestinal digestion of the presence of other egg white proteins and of egg yolk (2013) Food Chemistry, 136 (2), pp. 775-781
  • Minkiewicz, P., Slangen, C., Lagerwerf, F., Haverkamp, J., Rollema, H., Visser, S., Reversed-phase high-performance liquid chromatographic separation of bovine κ-casein macropeptide and characterization of isolated fractions (1996) Journal of Chromatography A, 743, pp. 123-135
  • Molina, E., Chicón, R., Belloque, J., López-Fandiño, R., Alegia a proteínas lácteas (2009) Funcionalidad e Componentes Lácteos, pp. 197-221. , J. Fontecha, I. Recio, & A.M.R. Pilosof (Eds.), Valencia, España: Universidad Miguel Hernández
  • Mollé, D., Leonil, J., 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 (LS-ESI/MS/MS) (2005) International Dairy Journal, 15, pp. 419-428
  • Mouécoucou, J., Frémont, S., Villaume, C., Sanchez, C., Méjean, L., Polysaccharides reduce in vitro IgG/IgE-binding of β-lactoglobulin after hydrolysis (2007) Food Chemistry, 104 (3), pp. 1242-1249
  • Mouécoucou, J., Villaume, C., Sanchez, C., Méjean, L., β-Lactoglobulin/polysaccharide interactions during in vitro gastric and pancreatic hydrolysis assessed in dialysis bags of different molecular weight cut-offs (2004) Biochimica et Biophysica Acta (BBA) - General Subjects, 1670 (2), pp. 105-112
  • Sélo, I., Clément, G., Bernard, H., Chatel, J.-M., Créminon, C., Peltre, G., Allergy to bovine β-lactoglobulin: Specificity of human IgE to tryptic peptides (1999) Clinical & Experimental Allergy, 29, pp. 1055-1063
  • Teuber, S.S., Hypothesis: The protein body effect and other aspects of food matrix effects (2002) Annals of the New York Academy of Science, 964, pp. 111-116
  • Thomä-Worringer, C., Sørensen, J., López Fandiño, R., Health effects and technological features of caseinomacropeptide (2006) International Dairy Journal, 16, pp. 1324-1333
  • Thomä, C., Krause, I., Kulozik, U., Precipitation behaviour of caseinomacropeptides and their simultaneous determination with whey proteins by RP-HPLC (2006) International Dairy Journal, 16, pp. 285-293
  • Villas-Boas, M.B., Vieira, K.P., Trevizan, G., De Lima Zollner, R., Netto, F.M., The effect of transglutaminase-induced polymerization in the presence of cysteine on β-lactoglobulin antigenicity (2010) International Dairy Journal, 20 (6), pp. 386-392

Citas:

---------- APA ----------
Martinez, M.J., Martos, G., Molina, E. & Pilosof, A.M.R. (2016) . Reduced β-lactoglobulin IgE binding upon in vitro digestion as a result of the interaction of the protein with casein glycomacropeptide. Food Chemistry, 192, 943-949.
http://dx.doi.org/10.1016/j.foodchem.2015.07.097
---------- CHICAGO ----------
Martinez, M.J., Martos, G., Molina, E., Pilosof, A.M.R. "Reduced β-lactoglobulin IgE binding upon in vitro digestion as a result of the interaction of the protein with casein glycomacropeptide" . Food Chemistry 192 (2016) : 943-949.
http://dx.doi.org/10.1016/j.foodchem.2015.07.097
---------- MLA ----------
Martinez, M.J., Martos, G., Molina, E., Pilosof, A.M.R. "Reduced β-lactoglobulin IgE binding upon in vitro digestion as a result of the interaction of the protein with casein glycomacropeptide" . Food Chemistry, vol. 192, 2016, pp. 943-949.
http://dx.doi.org/10.1016/j.foodchem.2015.07.097
---------- VANCOUVER ----------
Martinez, M.J., Martos, G., Molina, E., Pilosof, A.M.R. Reduced β-lactoglobulin IgE binding upon in vitro digestion as a result of the interaction of the protein with casein glycomacropeptide. Food Chem. 2016;192:943-949.
http://dx.doi.org/10.1016/j.foodchem.2015.07.097