Correlation between bulk characteristics of aggregated β-lactoglobulin and its surface and foaming properties

Food Hydrocolloids

Volumn 61, Issue , 2016, Pages 318-328

  Dombrowski, Jannika ^a   Johler, Florian ^a   Warncke, Malou ^a   Kulozik, Ulrich ^a  

^a TECHNICAL UNIVERSITY OF MUNICH   (Germany)

Author keywords

Foaming properties; Heat induced denaturation; PH value; Surface activity; Lactoglobulin

Indexed keywords

AGGREGATES; HYDROPHOBICITY; PARTICLE SIZE; PROTEINS; SODIUM CHLORIDE; ZETA POTENTIAL;

BOVINE Β-LACTOGLOBULIN; FOAMING PROPERTIES; HEAT-INDUCED DENATURATION; LACTOGLOBULIN; MEDIAN PARTICLE DIAMETERS; PH VALUE; PROTEIN ADSORPTION; SURFACE ACTIVITIES; SURFACE HYDROPHOBICITY; Β-LACTOGLOBULIN;

SURFACE PROPERTIES;

EID: 84973480997     PISSN: 0268005X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.foodhyd.2016.05.027     Document Type: Article

References (64)

1. Bals A., Kulozik U. Effect of pre-heating on the foaming properties of whey protein isolate using a membrane foaming apparatus. International Dairy Journal 2003, 13:903-908.
2. Bals A., Kulozik U. The influence of the pore size, the foaming temperature and the viscosity of the continuous phase on the properties of foams produced by membrane foaming. Journal of Membrane Science 2003, 220:5-11.
3. Barnthip N., Vogler E.A. Protein adsorption kinetics from single- and binary-solution. Applied Surface Science 2012, 262:19-23.
4. Binks B.P. Particles as surfactants -similarities and differences. Current Opinion in Colloid & Interface Science 2002, 7:21-41.
5. Croguennec T., Bouhallab S., Mollé D., O'Kennedy B., Mehra R. Stable monomeric intermediate with exposed Cys-119 is formed during heat denaturation of β-lactoglobulin. Biochemical and Biophysical Research Communications 2003, 301(2):465-471.
6. Damodaran S. Protein stabilization of emulsions and foams. Journal of Food Science 2005, 70:R54-R66.
7. Dannenberg F., Kessler H.-G. Reaction kinetics of the denaturation of whey proteins in milk. Journal of Food Science 1988, 53(1):258-263.
8. Dickinson E. Food emulsions and foams: stabilization by particles. Current Opinion in Colloid & Interface Science 2010, 15:40-49.
9. Dickinson E. Microgels - an alternative colloidal ingredient for stabilization of food emulsions. Trends in Food Science & Technology 2015, 43:178-188.
10. Dombrowski J., Dechau J., Kulozik U. Multiscale approach to characterize bulk, surface and foaming behavior of casein micelles as a function of alkalinisation. Food Hydrocolloids 2016, 57:92-102.
11. Donato L., Schmitt C., Bovetto L., Rouvet M. Mechanism of formation of stable heat-induced β-lactoglobulin microgels. International Dairy Journal 2009, 19(5):295-306.
12. Engelhardt K., Lexis M., Gochev G., Konnerth C., Miller R., Willenbacher N., et al. pH effects on the molecular structure of β-lactoglobulin modified air-water interfaces and its impact on foam rheology. Langmuir 2013, 29:11646-11655.
13. Fainerman V.B., Miller R. Equlibrium and dynamic characteristics of protein adsorption layers at gas-liquid interfaces: theoretical and experimental data. Colloid Journal 2005, 67(4):393-404.
14. Feijter J.de, Benjamins J. Adsorption kinetics of proteins at the air-water interface. Food emulsions and foams 1987, 72-85. Woodhead Publishing Limited, Cambridge. E. Dickinson (Ed.).
15. de la Fuente M.A., Singh H., Hemar Y. Recent advances in the characterisation of heat-induced aggregates and intermediates of whey proteins. Trends in Food Science & Technology 2002, 13(8):262-274.
16. Gochev G., Retzlaff I., Aksenenko E.V., Fainerman V.B., Miller R. Adsorption isotherm and equation of state for β-lactoglobulin layers at the air/water interface. Colloids and Surfaces A: Physicochemical and Engineering Aspects 2013, 442:33-38.
17. Gochev G., Retzlaff I., Exerowa D., Miller R. Electrostatic stabilization of foam films from β-lactoglobulin solutions. Colloids and Surfaces A: Physicochemical and Engineering Aspects 2014, 460:272-279.
18. Graham D.E., Phillips M.C. Proteins at liquid interfaces, I. Kinetics of adsorption and surface denaturation. Journal of Colloid and Interface Science 1979, 70(3):403-414.
19. Horozov T.S. Foams and foam films stabilized by solid particles. Current Opinion in Colloid & Interface Science 2008, 13:134-140.
20. Kaptay G. On the equation of the maximum capillary pressure induced by solid particles to stabilize emulsions and foams and on the emulsion stability diagrams. Colloids and Surfaces A: Physicochemical and Engineering Aspects 2006, 282-283:387-401.
21. Karapantsios T.D., Kostoglou M. Investigation of the oscillating bubble technique for the determination of interfacial dilatational properties. Colloids and Surfaces A: Physicochemical Engineering 1999, 156:49-64.
22. Kato A., Nakai S. Hydrophobicity determined by a fluorescence probe method and its correlation with surface properties of proteins. Biochimica et Biophysica Acta 1980, 624(1):13-20.
23. Kim D.A., Cornec M., Narsimhan G. Effect of thermal treatment on interfacial properties of β-lactoglobulin. Journal of Colloid and Interface Science 2005, 285:100-109.
24. Kinsella J.E. Functional properties of proteins: possible relationships between structure and function in foams. Food Chemistry 1981, 7:273-288.
25. Lam S., Velikov K., Velev O. Pickering stabilization of foams and emulsions with particles of biological origin. Current Opinion in Colloid & Interface Science 2014, 19:490-500.
26. Lazidis A., Hancocks R.D., Spyropoulos F., Kreuß M., Berrocal R., Norton I.T. Whey protein fluid gels for the stabilization of foams. Food Hydrocolloids 2016, 53:209-217.
27. Lexis M., Willenbacher N. Relating foam and interfacial rheological properties of β-lactoglobulin solutions. Soft Matter 2014, 48(10):9626-9636.
28. Lucassen J. Dynamic properties of free liquid films and foams. Anionic surfactants - Physical chemistry of surfactant action 1981, 217-265. Marcel Dekker, New York. E.H. Lucassen-Reynders (Ed.).
29. Lucassen J., van den Tempel M. Dynamic measurements of dilatational properties of a liquid interface. Chemical Engineering Science 1972, 27:1283-1291.
30. MacRitchie F. Proteins at interfaces. Advances in Protein Chemistry 1978, 32:283-326.
31. MacRitchie F. Reversibility of protein adsorption. Proteins at liquid interfaces 1998, 7:149-177. Elsevier, Amsterdam.
32. Mahmoudi N., Gaillard C., Boué F., Axelos M.A.V., Riaublanc A. Self-similar assemblies of globular whey proteins at the air-water interface: effect of structure. Journal of Colloid and Interface Science 2010, 345:54-63.
33. Marinova K.G., Basheva E.S., Nenova B., Temelska M., Mirarefi A.Y., Campbell B., et al. Physico-chemical factors controlling the foamability and foam stability of milk proteins: sodium caseinate and whey protein concentrates. Food Hydrocolloids 2009, 23:1864-1876.
34. Miller R., Aksenenko E.V., Fainerman V.B., Pison U. Kinetics of adsorption of globular proteins at liquid/fluid interfaces. Colloids and Surfaces A: Physicochemical and Engineering Aspects 2001, 183-185:381-390.
35. Miller R., Fainerman V., Makievski A., Krägel J., Grigoriev D., Kazakov V., et al. Dynamics of protein and mixed protein surfactant adsorption layers at the water fluid interface. Advances in Colloid and Interface Science 2000, 86:39-82.
36. Moro A., Báez G.D., Busti P.A., Ballerini G.A., Delorenzi N.J. Effects of heat-treated β-lactoglobulin and its aggregates on foaming properties. Food Hydrocolloids 2011, 25:1009-1015.
37. Murray B.S., Ettelaie R. Foam stability: proteins and nanoparticles. Current Opinion in Colloid & Interface Science 2004, 9:314-320.
38. Narsimhan G., Uraizee F. Kinetics of adsorption of globular proteins at an air-water interface. Biotechnology Progress 1992, 8:187-196.
39. Nicolai T., Britten M., Schmitt C. β-lactoglobulin and WPI aggregates: formation, structure and applications. Food Hydrocolloids 2011, 25(8):1945-1962.
40. Oetjen K., Bilke-Krause C., Madani M., Willers T. Temperature effect on foamability, foam stability, and foam structure of milk. Colloids and Surfaces A: Physicochemical and Engineering Aspects 2014, 460(20):280-285.
41. Pérez O., Carrera Sánchez C., Pilosof A., Rodríguez Patino J. Dynamics of adsorption of hydroxypropyl methylcellulose at the air-water interface. Food Hydrocolloids 2008, 22:387-402.
42. Pessen H., Purcell J.M., Farrell H.M.J.R. Proton relaxation rates of water in dilute solutions of β-lactoglobulin. Determination of cross relaxation and correlation with structural changes by the use of two genetic variants of a self-associating globular protein. Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology 1985, 828(1):1-12.
43. Phillips L.G., Schulman W., Kinsella J.E. pH and heat treatment effects on foaming of whey protein isolate. Journal of Food Science 1990, 55:1116-1119.
44. Rullier B., Axelos M.A.V., Langevin D., Novales B. β-lactoglobulin aggregates in foam films: correlation between foam films and foaming properties. Journal of Colloid and Interface Science 2009, 336:750-755.
45. Rullier B., Axelos M.A.V., Langevin D., Novales B. β-lactoglobulin aggregates in foam films: effect of the concentration and size of the protein aggregates. Journal of Colloid and Interface Science 2010, 343:330-337.
46. Rullier B., Novales B., Axelos M.A.V. Effect of protein aggregates on foaming properties of β-lactoglobulin. Colloids and Surfaces A: Physicochemical and Engineering Aspects 2008, 330:96-102.
47. Saalfeld D., Gebhardt R., Kulozik U. Salting out experiments with β-lactoglobulin in "molten globule state" 2016, to be submitted.
48. Schmidt S., Liu T., Rütten S., Phan K.-H., Möller M., Richtering W. Influence of microgel architecture and oil polarity on stabilization of emulsions by stimuli-sensitive core-shell poly(N-isopropylacrylamide-co-methacrylic acid) microgels: mickering versus pickering behavior?. Langmuir 2011, 27:9801-9806.
49. Schmitt C., Bovay C., Rouvet M. Bulk self-aggregation drives foam stabilization properties of why protein microgels. Food Hydrocolloids 2014, 42:139-148.
50. Schmitt C., Bovay C., Rouvet M., Shojaei-Rami S., Kolodziejczyk Whey protein soluble aggregates from heating with NaCl: physicochemical, interfacial, and foaming properties. Langmuir 2007, 23:4155-4166.
51. Schokker E., Singh H., Creamer L. Heat-induced aggregation of β-lactoglobulin A and B with α-lactalbumin. International Dairy Journal 2000, 10(12):843-853.
52. Talansier E., Loisel C., Dellavalle D., Desrumaux A., Lechevalier V., Legrand J. Optimization of dry heat treatment of egg white in relation to foam and interfacial properties. LWT - Food Science and Technology 2009, 42:496-503.
53. Tolkach A., Kulozik U. Reaction kinetic pathway of reversible and irreversible thermal denaturation of β-Lactoglobulin. Lait 2007, 87(4-5):301-315.
54. Toro-Sierra J., Tolkach A., Kulozik U. Fractionation of α-lactalbumin and β-lactoglobulin from whey protein isolate using selective thermal aggregation, an optimized membrane separation procedure and resolubilization techniques at pilot plant scale. Food and Bioprocess Technology 2013, 6(4):1032-1043.
55. Tripp B., Magda J., Andrade J. Adsorption of globular proteins at the air/water interface as measured via dynamic surface tension: concentration dependence, mass-transfer considerations, and adsorption kinetics. Journal of Colloid and Interface Science 1995, 173(1):16-27.
56. Unterhaslberger G., Schmitt C., Shojaei-Rami S., Sanchez C. β-lactoglobulin aggregates from heating with charges cosolutes: formation, characterization and foaming. Food colloids: Self-assembly and material science 2007, 177-194. The Royal Society of Chemistry, Cambridge. M.E. Leser, E. Dickinson (Eds.).
57. Verheul M., Pedersen J.S., Roefs S.P.F.M., de Kruif K.G. Association behavior of native β-lactoglobulin. Biopolymers 1999, 49(1):11-20.
58. Verheul M., Roefs S., de Kruif K. Kinetics of heat-induced aggregation of β-lactoglobulin. Journal of Agricultural and Food Chemistry 1998, 46:896-903.
59. Ward A.F.H., Tordai L. Time-dependence of boundary tensions of solutions I. The role of diffusion in time-effects. The Journal of Chemical Physics 1946, 14(7):453-461.
60. Wierenga P.A., Meinders M.B.J., Egmond M.R., Voragen F.A.G.J., de Jongh H.H.J. Protein exposed hydrophobicity reduces the kinetic barrier for adsorption of ovalbumin to the air-water interface. Langmuir 2003, 19:8964-8970.
61. Wierenga P.A., Meinders M.B.J., Egmond M.R., Voragen A.G.J., de Jongh H.H.J. Quantitative description of the relation between protein net charge and protein adsorption to air-water interfaces. The Journal of Physical Chemistry B 2005, 109:16946-16952.
62. Wijnen M.E., Prins A. Disproportionation in aerosol whipped cream. Food macromolecules and colloids 1995, 309-311. The Royal Society of Chemistry, London. E. Dickinson, D. Lorient (Eds.).
63. de Wit J.N. Thermal behaviour of bovine β-lactoglobulin at temperatures up to 150 °C. a review. Trends in Food Science & Technology 2009, 20:27-34.
64. Zúñiga R.N., Tolkach A., Kulozik U., Aguilera J.M. Kinetics of formation and physicochemical characterization of thermally-induced β-lactoglobulin aggregates. Journal of Food Science 2010, 75(5):E261-E268.