Conformational changes of β-lactoglobulin induced by shear, heat, and pH-Effects on antigenicity

Journal of Dairy Science

Volumn 98, Issue 7, 2015, Pages 4255-4265

  Rahaman, Toheder ^a   Vasiljevic, Todor ^a   Ramchandran, Lata ^a  

^a VICTORIA UNIVERSITY   (Australia)

Author keywords

Antigenicity; Conformation; Heat; PH; Shear

Indexed keywords

LACTOGLOBULIN; THIOL DERIVATIVE;

AGAR GEL ELECTROPHORESIS; CHEMICAL PHENOMENA; CHEMISTRY; ENZYME LINKED IMMUNOSORBENT ASSAY; HEAT; IMMUNOLOGY; INFRARED SPECTROSCOPY; PH; PROTEIN CONFORMATION; SHEAR STRENGTH;

ELECTROPHORESIS, AGAR GEL; ENZYME-LINKED IMMUNOSORBENT ASSAY; HOT TEMPERATURE; HYDROGEN-ION CONCENTRATION; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; LACTOGLOBULINS; PROTEIN CONFORMATION; SHEAR STRENGTH; SPECTROSCOPY, FOURIER TRANSFORM INFRARED; SULFHYDRYL COMPOUNDS;

EID: 84931571972     PISSN: 00220302     EISSN: 15253198     Source Type: Journal    
DOI: 10.3168/jds.2014-9010     Document Type: Article

References (39)

1. Alizadeh-Pasdar N., Li-Chan E.C. Comparison of protein surface hydrophobicity measured at various pH values using three different fluorescent probes. J. Agric. Food Chem. 2000, 48:328-334.
2. Bekard I.B., Asimakis P., Bertolini J., Dunstan D.E. The effects of shear flow on protein structure and function. Biopolymers 2011, 95:733-745.
3. Bhattacharjee C., Saha S., Biswas A., Kundu M., Ghosh L., Das K.P. Structural changes of β-lactoglobulin during thermal unfolding and refolding-An FT-IR and circular dichroism study. Protein J. 2005, 24:27-35.
4. Bossios A., Theodoropoulou M., Mondoulet L., Rigby N.M., Papadopoulos N.G., Bernard H., Adel-Patient K., Wal J.-M., Mills C.E.N., Papageorgiou P. Effect of simulated gastro-duodenal digestion on the allergenic reactivity of beta-lactoglobulin. Clin. Transl. Allergy 2011, 1:6.
5. Bu G., Luo Y., Zheng Z., Zheng H. Effect of heat treatment on the antigenicity of bovine α-lactalbumin and β-lactoglobulin in whey protein isolate. Food Agric. Immunol. 2009, 20:195-206.
6. Casal H.L., Köhler U., Mantsch H.H. Structural and conformational changes of β-lactoglobulin B: An infrared spectroscopic study of the effect of pH and temperature. Biochim. Biophys. Acta 1988, 957:11-20.
7. Clement G., Boquet D., Frobert Y., Bernard H., Negroni L., Chatel J.-M., Adel-Patient K., Créminon C., Wal J.-M., Grassi J. Epitopic characterization of native bovine β-lactoglobulin. J. Immunol. Methods 2002, 266:67-78.
8. Davis P.J., Williams S.C. Protein modification by thermal processing. Allergy 1998, 53(Suppl.):102-105.
9. de la Fuente M.A., Singh H., Hemar Y. Recent advances in the characterisation of heat-induced aggregates and intermediates of whey proteins. Trends Food Sci. Technol. 2002, 13:262-274.
10. Dissanayake M., Ramchandran L., Vasiljevic T. Denaturation of whey proteins as a function of temperature, pH and protein concentration. Int. Dairy J. 2013, 31:93-99.
11. Dunstan D.E., Hamilton-Brown P., Asimakis P., Ducker W., Bertolini J. Shear-induced structure and mechanics of β-lactoglobulin amyloid fibrils. Soft Matter 2009, 5:5020-5028.
12. Dupont D., Croguennec T., Brodkorb A., Kouaouci R. Quantitation of proteins in milk and milk products. Advanced Dairy Chemistry-Proteins: Basic Aspects 2013, 87-134. Springer Science+Business Media, New York, NY, Volume 1A. 4th. P.L.H. McSweeney, P.F. Fox (Eds.).
13. Ena J.M., Van Beresteijn E.C.H., Robben A.J.P., Schmidt D.G. Whey protein antigenicity reduction by fungal proteinases and a pepsin/pancreatin combination. J. Food Sci. 1995, 60:104-110.
14. Fritsche R. Role for technology in dairy allergy. Aust. J. Dairy Technol. 2003, 58:89-91.
15. Grar H., Kaddouri H., Gourine H., Negaoui H., Kheroua O., Saïdi D. Microwave irradiation under different pH conditions induced a decrease in β-lactoglobulin antigenicity. Eur. Food Res. Technol. 2009, 229:779-783.
16. Heyman M. Evaluation of the impact of food technology on the allergenicity of cow's milk proteins. Proc. Nutr. Soc. 1999, 58:587-592.
17. Kella N.K., Kinsella J.E. Enhanced thermodynamic stability of beta-lactoglobulin at low pH. A possible mechanism. Biochem. J. 1988, 255:113-118.
18. Kleber N., Krause I., Illgner S., Hinrichs J. The antigenic response of β-lactoglobulin is modulated by thermally induced aggregation. Eur. Food Res. Technol. 2004, 219:105-110.
19. Lee J.-W., Kim J.-H., Yook H.-S., Kang K.-O., Lee S.-Y., Hwang H.-J., Byun M.-W. Effects of gamma radiation on the allergenic and antigenic properties of milk proteins. J. Food Prot. 2001, 64:272-276.
20. Lefèvre T., Subirade M. Molecular differences in the formation and structure of fine-stranded and particulate β-lactoglobulin gels. Biopolymers 2000, 54:578-586.
21. Lehrer S.B., Horner W.E., Reese G. Why are some proteins allergenic? Implications for biotechnology. Crit. Rev. Food Sci. Nutr. 1996, 36:553-564.
22. Liyanaarachchi W.S., Ramchandran L., Vasiljevic T. Controlling heat induced aggregation of whey proteins by casein inclusion in concentrated protein dispersions. Int. Dairy J. 2015, 44:21-30.
23. Monahan F.J., German J.B., Kinsella J.E. Effect of pH and temperature on protein unfolding and thiol/disulfide interchange reactions during heat-induced gelation of whey proteins. J. Agric. Food Chem. 1995, 43:46-52.
24. Mudgal P., Daubert C.R., Foegeding E.A. Kinetic study of β-lactoglobulin thermal aggregation at low pH. J. Food Eng. 2011, 106:159-165.
25. Niemi M., Jylhä S., Laukkanen M.-L., Söderlund H., Mäkinen-Kiljunen S., Kallio J.M., Hakulinen N., Haahtela T., Takkinen K., Rouvinen J. Molecular interactions between a recombinant IgE antibody and the β-lactoglobulin allergen. Structure 2007, 15:1413-1421.
26. SAS/STAT Software. Changes and enhancements through release 6.11 1996, SAS Institute, SAS Institute Inc, Cary, NC.
27. Sava N., Van der Plancken I., Claeys W., Hendrickx M. The kinetics of heat-induced structural changes of β-lactoglobulin. J. Dairy Sci. 2005, 88:1646-1653.
28. Sélo I., Clément G., Bernard H., Chatel J.M., Créminon C., Peltre G., Wal J.M Allergy to bovine β-lactoglobulin: Specificity of human IgE to tryptic peptides. Clin. Exp. Allergy 1999, 29:1055-1063.
29. Sélo I., Créminon C., Grassi J., Couraud J.-Y. Anti-allergen antibodies can be neutralized by antibodies obtained against a peptide complementary to the allergen: Towards a new peptide therapy for allergy. Immunol. Lett. 2002, 80:133-138.
30. Sélo I., Négroni L., Créminon C., Yvon M., Peltre G., Wal J.M. Allergy to bovine β-lactoglobulin: Specificity of human IgE using cyanogen bromide-derived peptides. Int. Arch. Allergy Immunol. 1998, 117:20-28.
31. Shimizu M., Saito M., Yamauchi K. Emulsifying and structural properties of β-lactoglobulin at different pHs. Agric. Biol. Chem. 1985, 49:189-194.
32. Stanic-Vucinic D., Stojadinovic M., Atanaskovic-Markovic M., Ognjenovic J., Grönlund H., van Hage M., Lantto R., Sancho A.I., Velickovic T.C. Structural changes and allergenic properties of β-lactoglobulin upon exposure to high-intensity ultrasound. Mol. Nutr. Food Res. 2012, 56:1894-1905.
33. Visschers R.W., de Jongh H.H.J. Disulphide bond formation in food protein aggregation and gelation. Biotechnol. Adv. 2005, 23:75-80.
34. Wada R., Fujita Y., Kitabatake N. Effects of heating at neutral and acid pH on the structure of β-lactoglobulin A revealed by differential scanning calorimetry and circular dichroism spectroscopy. Biochim. Biophys. Acta 2006, 1760:841-847.
35. Wal J.M. Structure and function of milk allergens. Allergy 2001, 56(Suppl. 67):35-38.
36. Wróblewska B., Troszyńska A. Enzymatic hydrolysis of cow's whey milk proteins in the aspect of their utilization for the production of hypoallergenic formulas. Pol. J. Food Nutr. Sci. 2005, 14:349-357.
37. Yim S., Shamlou P. The engineering effects of fluids flow on freely suspended biological macro-materials and macromolecules. Influence of Stress on Cell Growth and Product Formation 2000, 83-122. Springer Science+Business Media, New York, NY.
38. Zhong J.Z., Liu W., Liu C.M., Wang Q.H., Li T., Tu Z.C., Luo S.J., Cai X.F., Xu Y. Aggregation and conformational changes of bovine β-lactoglobulin subjected to dynamic high-pressure microfluidization in relation to antigenicity. J. Dairy Sci. 2012, 95:4237-4245.
39. Zhong J., Liu C., Liu W., Cai X., Tu Z., Wan J. Effect of dynamic high-pressure microfluidization at different temperatures on the antigenic response of bovine β-lactoglobulin. Eur. Food Res. Technol. 2011, 233:95-102.