Changes of secondary structure and surface tension of whey protein isolate dispersions upon ph and temperature

Czech Journal of Food Sciences

Volumn 32, Issue 1, 2014, Pages 82-89

  TOMCZYŃSKA MLEKO, Marta ^a   KAMYSZ, Elzbieta ^b   SIKORSKA, Emilia ^b   PUCHALSKI, Czesław ^c   MLEKO, Stanisław ^a   OZIMEK, Lech ^d   KOWALUK, Grzegorz ^e   GUSTAW, Waldemar ^a   WESOŁOWSKA TROJANOWSKA, Marta ^a  

^a UNIVERSITY OF LIFE SCIENCES IN LUBLIN   (Poland)

^b UNIVERSITY OF GDA SK   (Poland)

^c UNIVERSITY OF RZESZÓW   (Poland)

^d UNIVERSITY OF ALBERTA   (Canada)

^e JÓZEF PI SUDSKI UNIVERSITY OF PHYSICAL EDUCATION IN WARSAW   (Poland)

Author keywords

Circular dichroism; Globular protein; Protein concentration

Indexed keywords

DAIRIES; DISPERSIONS; EXPONENTIAL FUNCTIONS; SURFACE TENSION;

NEGATIVE EXPONENTS; PROTEIN CONCENTRATIONS; PROTEIN SOLUTION; SECONDARY STRUCTURE OF PROTEINS; SECONDARY STRUCTURES; UNORDERED STRUCTURE; WHEY PROTEIN ISOLATE; WHEY PROTEINS;

PROTEINS;

EID: 84906562911     PISSN: 12121800     EISSN: 18059317     Source Type: Journal    
DOI: 10.17221/326/2012-CJFS     Document Type: Article

References (28)

1. Chen W.L., Hwang M.T., Liau C.Y., Ho J.C., Hong K.C., Mao S.J.T. (2005): β-Lactoglobulin is a thermal marker in processed milk as studied by electrophoresis and circular dichroic spectra. Journal of Dairy Science, 88: 1618-1630.
2. Chrysina E.D., Brew K., Acharya K.R. (2000): Crystal structure of apo- and holo-bovine α-lactalbumin at 2.2-A resolution reveal an effect of calcium on inter-lobe interactions. Journal of Biological Chemistry, 275: 37021-37029.
3. Cifra P. (2004): Differences and limits in estimates of persistence length for semi-flexible macromolecules. Polymer, 45: 5995-6002.
4. Creamer L.K., Parry D.A.D., Malcolm G.N. (1983): Secondary structure of bovine β-lactoglobulin. Archives of Biochemistry and Biophysics, 227: 98-105.
5. Curry S., Mandelkow H., Brick P., Franks N. (1998): Crystal structure of human serum albumin complexed with fatty acid reveals an asymmetric distribution of binding sites. Nature Structural Biology, 5: 827-835.
6. Davis J.P., Foegeding E.A., Hansen F.K. (2004): Electrostatic effects on the yield stress of whey protein isolate foams. Colloids and Surfaces B: Biointerfaces, 34: 13-23.
7. Fernández E., Artiguez M.L., de MaraÑon I.M., Villate M., Blanco F.J., Arboleya J.C. (2012): Effect of pulsed-light processing on the surface and foaming properties of β-lactoglobulin. Food Hydrocolloids, 27: 154-160.
8. Foegeding E.A., Kuhn P.R., Hardin C.C. (1992): Specific divalent cation-induced changes during gelation of β-lactoglobulin. Journal of Agricultural and Food Chemistry, 40: 2092-2097.
9. Foegeding E.A., Luck P.J., Davis J.P. (2006): Factors determining the physical properties of protein foams. Food Hydrocolloids, 20: 284-292.
10. Garcia-Hernández E., Hernández-Arana A., Zubillaga R.A., Rojo-Dominíguez A. (1998): Spectroscopic and thermodynamic evidence for a complex denaturation mechanism of bovine β-lactoglobulin A. Biochemistry & Molecular Biology International, 45: 761-768.
11. González-Tello P., Camacho F., Guadix E.M., Luzón G., González P.A. (2009): Density, viscosity and surface tension of whey protein concentrate solutions. Journal of Food Process Engineering, 32: 235-247.
12. Hamada D., Segawa S., Goto Y. (1996): Non-native α-helical intermediate in the refolding of β-lactoglobulin, a predominantly β-sheet protein. Nature Structural & Molecular Biology, 3: 868-873.
13. Kontopidis G., Holt C., Sawyer L. (2004): Invited review: β-lactoglobulin: Binding properties, structure, and function. Journal of Dairy Science, 87: 785-796.
14. Kratochvíl A., Hrnčíř E. (2002): Correlation between the cerebrospinal fluid surface tension value and 1. Concentration of total proteins 2. Number of cell elements. General Physiology and Biophysics, 21: 47-53.
15. Kuwata K., Hoshino M., Forge V., Era S., Batt C.A., Goto Y. (1999): Solution structure and dynamics of bovine β-lactoglobulin A. Protein Science, 8: 2541-2545.
16. López M.L. Bengoechea C., De La Fuente J., Ruiz M., Guerrero A. (2010): Influence of the presence of monoglyceride on the interfacial properties of wheat gluten. Journal of the Science of Food and Agriculture, 90: 1688-1694.
17. Mercade-Prieto R., Paterson W.R., Wilson D.I. (2007): The pH threshold in the dissolution of β-lactoglobulin gels and aggregates in alkali. Biomacromolecules, 8: 1162-1170.
18. Monahan F.J., German J.B., Kinsellat J.E. (1995) Effect of pH and temperature on protein unfolding and thiol/disulfide interchange reactions during heat-induced gelation of whey proteins. Journal of Agricultural and Food Chemistry, 43: 46-52.
19. Moro A., Baez G.D., Busti P.A., Ballerini G.A., Delo-renzi N.J. (2011): Effects of heat-treated β-lactoglobulin and its aggregates on foaming properties. Food Hydrocolloids, 25: 1009-1015.
20. Navarra G., Giacomazza D., Leone M., Librizzi F., Militello V., San Biagio P.L. (2009): Thermal aggregation and ion-induced cold-gelation of bovine serum albumin. European Biophysics Journal, 38: 437-446.
21. Nylander T., Hamraoui A., Paulsson M. (1999): Interfacial properties of whey proteins at air/water and oil/water interfaces studied by dynamic drop tensiometry, ellipsometry and spreading kinetics. International Journal of Food Science and Technology, 34: 573-585.
22. Qi P.X., Onwulata Ch.I. (2011): Physical properties, molecular structures, and protein quality of texturized whey protein isolate: Effect of extrusion temperature. Journal of Agricultural and Food Chemistry, 59: 4668-4675.
23. Rattray W., Jelen P. (1998): Thermal stability of skim milk/whey protein solution blends. Food Research International, 30: 327-334.
24. Sreerama N., Woody R.W. (2000): Estimation of protein secondary structure from circular dichroism spectra: Comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set. Analytical Biochemistry, 287: 252-260.
25. Wada R., Fujita Y., Kitabatake N. (2006): Effects of heating on neutral and acid pH on the structure of β-lactoglobulin A revealed by differential scanning calorimetry and circular dichroism spectroscopy. Biochimica et Biophysica Acta, 1760: 841-847.
26. Wilde P.J., Clark D.C. (1996): Foam formation and stability. In: Hall G.M. (ed.): Methods of Testing Protein Functionality. Blackie Academic & Professional, London: 110-148.
27. Woody R.W. (1996): Theory of circular dichroism in proteins. In: Fasman G.D. (ed.): Circular Dichroism and the Conformational Analysis of Biomolecules. Plenum Press, New York.
28. Xiong Y.L. (1992) Influence of pH and ionic environment on thermal aggregation of whey proteins. Journal of Agricultural and Food Chemistry, 40: 380-384