Effects of ultrasound treatment on physicochemical and emulsifying properties of whey proteins pre- and post-thermal aggregation

Food Hydrocolloids

Volumn 63, Issue , 2017, Pages 668-676

  Shen, Xue ^a   Fang, Tianqi ^a   Gao, Feng ^a   Guo, Mingruo ^a,b  

^a JILIN UNIVERSITY   (China)

^b UNIVERSITY OF VERMONT   (United States)

Author keywords

Emulsifying property; Physicochemical property; Thermal aggregation; Whey protein isolate

Indexed keywords

AGGLOMERATION; AGGREGATES; EMULSIFICATION; HYDROPHOBICITY; NANOCOMPOSITES; PARTICLE SIZE; PROTEINS; TURBIDITY; ZETA POTENTIAL;

EMULSIFYING PROPERTY; PHYSICOCHEMICAL PROPERTY; SOLUBLE AGGREGATES; SULPHYDRYL GROUPS; SURFACE HYDROPHOBICITY; THERMAL; THERMAL AGGREGATION; ULTRASOUND TREATMENTS; WHEY PROTEIN ISOLATE; WHEY PROTEINS;

ULTRASONICS;

EID: 84995937418     PISSN: 0268005X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.foodhyd.2016.10.003     Document Type: Article

References (78)

1. Akbari, A., Wu, J., Cruciferin nanoparticles: Preparation, characterization and their potential application in delivery of bioactive compounds. Food Hydrocolloids 54 (2016), 107–118.
2. Alizadeh-Pasdar, N., Li-Chan, E.C.Y., Comparison of protein surface hydrophobicity measured at various pH values using three different fluorescent probes. Journal of Agricultural and Food Chemistry 48 (2000), 328–334.
3. Alting, A.C., Hamer, R.J., De Kruif, C.G., Paques, M., Visschers, R.W., Number of thiol groups rather than the size of the aggregates determines the hardness of cold set whey protein gels. Food Hydrocolloids 17 (2003), 469–479.
4. Arzeni, C., Martinez, K., Zema, P., Arias, A., Perez, O.E., Pilosof, A.M.R., Comparative study of high intensity ultrasound effects on food proteins functionality. Journal of Food Engineering 108 (2012), 463–472.
5. Ashokkumar, M., The characterization of acoustic cavitation bubbles - An overview. Ultrasonics Sonochemistry 18 (2011), 864–872.
6. Ashokkumar, M., Lee, J., Kentish, S., Grieser, F., Bubbles in an acoustic field: An overview. Ultrasonics Sonochemistry 14 (2007), 470–475.
7. Awad, T.S., Moharram, H.A., Shaltout, O.E., Asker, D., Youssef, M.M., Applications of ultrasound in analysis, processing and quality control of food: A review. Food Research International 48 (2012), 410–427.
8. Boye, J.I., Alli, I., Thermal denaturation of mixtures of alpha-lactalbumin and β-lactoglobulin: A differential scanning calorimetric study. Food Research International 33 (2000), 673–682.
9. Chandrapala, J., Zisu, B., Palmer, M., Kentish, S., Ashokkumar, M., Effects of ultrasound on the thermal and structural characteristics of proteins in reconstituted whey protein concentrate. Ultrasonics Sonochemistry 18 (2011), 951–957.
10. Chen, L., Chen, J., Ren, J., Zhao, M., Effects of Ultrasound pretreatment on the enzymatic hydrolysis of soy protein isolates and on the emulsifying properties of hydrolysates. Journal of Agricultural and Food Chemistry 59 (2011), 2600–2609.
11. Ciawi, E., Rae, J., Ashokkumar, M., Grieser, F., Determination of temperatures within acoustically generated bubbles in aqueous solutions at different ultrasound frequencies. Journal of Physical Chemistry B 110 (2006), 13656–13660.
12. D'Amico, D.J., Silk, T.M., Wu, J.R., Guo, M.R., Inactivation of microorganisms in milk and apple cider treated with ultrasound. Journal of Food Protection 69 (2006), 556–563.
13. Destribats, M., Rouvet, M., Gehin-Delval, C., Schmitt, C., Binks, P., Emulsions stabilised by whey protein microgel particles: towards food-grade Pickering emulsions. Soft Matter 10 (2014), 6941–6954.
14. Dickinson, E., Colloids in food: Ingredients, structure, and stability. Annual Review of Food Science and Technology 6 (2015), 211–233.
15. Dissanayake, M., Liyanaarachchi, S., Vasiljevic, T., Functional properties of whey proteins microparticulated at low pH. Journal of Dairy Science 95 (2012), 1667–1679.
16. Dissanayake, M., Vasiljevic, T., Functional properties of whey proteins affected by heat treatment and hydrodynamic high-pressure shearing. Journal of Dairy Science 92 (2009), 1387–1397.
17. El-Salam, M.H.A., El-Shibiny, S., Salem, A., Factors affecting the functional properties of whey protein products: A review. Food Reviews International 25 (2009), 251–270.
18. Ellman, G.L., Tissue sulfhydryl groups. Archives of Biochemistry and Biophysics 82 (1959), 70–77.
19. Fitzsimons, S.A., Mulvihill, D.M., Morris, E.R., Denaturation and aggregation processes in thermal gelation of whey proteins resolved by differential scanning calorimetry. Food Hydrocolloids 21 (2007), 638–644.
20. Foegeding, E.A., Davis, J.P., Doucet, D., McGuffey, M.K., Advances in modifying and understanding whey protein functionality. Trends in Food Science & Technology 13 (2002), 151–159.
21. Gallego-Juarez, J.A., Rodriguez, G., Acosta, V., Riera, E., Power ultrasonic transducers with extensive radiators for industrial processing. Ultrasonics Sonochemistry 17 (2010), 953–964.
22. Gordon, L., Pilosof, A.M.R., Application of high-intensity ultrasounds to control the size of whey proteins particles. Food Biophysics 5 (2010), 203–210.
23. Gulseren, I., Guezey, D., Bruce, B.D., Weiss, J., Structural and functional changes in ultrasonicated bovine serum albumin solutions. Ultrasonics Sonochemistry 14 (2007), 173–183.
24. Guo, M.R., Wang, G.R., Whey protein polymerisation and its application: In environmentally safe adhesives: A review. Internationl Jornal of Dairy Techonology 69 (2016), 1–8.
25. Guyomarc'h, F., Famelart, M.-H., Henry, G., Gulzar, M., Leonil, J., Hamon, P., et al. Current ways to modify the structure of whey proteins for specific functionalities-a review. Dairy Science & Technology 95 (2015), 795–814.
26. Helgason, T., Gislason, J., McClements, D.J., Kristbergsson, K., Weiss, J., Influence of molecular character of chitosan on the adsorption of chitosan to oil droplet interfaces in an in vitro digestion model. Food Hydrocolloids 23 (2009), 2243–2253.
27. Hermoso, J., Martinez-Boza, F., Gallegos, C., Influence of viscosity modifier nature and concentration on the viscous flow behaviour of oil-based drilling fluids at high pressure. Applied Clay Science 87 (2014), 14–21.
28. Hiller, B., Lorenzen, P.C., Surface hydrophobicity of physicochemically and enzymatically treated milk proteins in relation to techno-functional properties. Journal of Agricultural and Food Chemistry 56 (2008), 461–468.
29. Hu, H., Li-Chan, E., C., Y., Wan, L., Tian, M., Pan, S., The effect of high intensity ultrasonic pre-treatment on the properties of soybean protein isolate gel induced by calcium sulfate. Food Hydrocolloids 32 (2013), 303–311.
30. Hussain, R., Gaiani, C., Jeandel, C., Ghanbaja, J., Scher, J., Combined effect of heat treatment and ionic strength on the functionality of whey proteins. Journal of Dairy Science 95 (2012), 6260–6273.
31. Hu, H., Wu, J., Li-Chan, E.C.Y., Zhu, L., Zhang, F., Xu, X., et al. Effects of ultrasound on structural and physical properties of soy protein isolate (SPI) dispersions. Food Hydrocolloids 30 (2013), 647–655.
32. Ibanoglu, E., Effect of hydrocolloids on the thermal denaturation of proteins. Food Chemistry 90 (2005), 621–626.
33. Jambrak, A.R., Lelas, V., Mason, T.J., Kresic, G., Badanjak, M., Physical properties of ultrasound treated soy proteins. Journal of Food Engineering 93 (2009), 386–393.
34. Jambrak, A.R., Mason, T.J., Lelas, V., Herceg, Z., Herceg, I.L., Effect of ultrasound treatment on solubility and foaming properties of whey protein suspensions. Journal of Food Engineering 86 (2008), 281–287.
35. Jambrak, A.R., Mason, T.J., Lelas, V., Kresic, G., Ultrasonic effect on physicochemical and functional properties of alpha-lactalbumin. Lwt-Food Science and Technology 43 (2010), 254–262.
36. Kato, A., Nakai, S., Hydrophobicity determined by a fluorescence probe method and its correlation with surface properties of proteins. Biochimica et Biophysica Acta 624 (1980), 13–20.
37. Kazmierski, M., Corredig, M., Characterization of soluble aggregates from whey protein isolate. Food Hydrocolloids 17 (2003), 685–692.
38. Kim, D.A., Cornec, M., Narsimhan, G., Effect of thermal treatment on interfacial properties of beta-lactoglobulin. Journal of Colloid and Interface Science 285 (2005), 100–109.
39. Krebs, M.R.H., Devlin, G.L., Donald, A.M., Protein particulates: Another generic form of protein aggregation?. Biophysical Journal 92 (2007), 1336–1342.
40. Lam, R.S.H., Nickerson, M.T., The effect of pH and temperature pre-treatments on the physicochemical and emulsifying properties of whey protein isolate. Lwt-Food Science and Technology 60 (2015), 427–434.
41. Lauterborn, W., Kurz, T., Geisler, R., Schanz, D., Lindau, O., Acoustic cavitation, bubble dynamics and sonoluminescence. Ultrasonics Sonochemistry 14 (2007), 484–491.
42. Liu, Q., Li, J., Kong, B.H., Li, P.J., Xia, X.F., Physicochemical and antioxidant properties of Maillard reaction products formed by heating whey protein isolate and reducing sugars. International Journal of Dairy Technology 67 (2014), 220–228.
43. Madadlou, A., Mousavi, M.E., Emam-djomeh, Z., Ehsani, M., Sheehan, D., Sonodisruption of re-assembled casein micelles at different pH values. Ultrasonics Sonochemistry 16 (2009), 644–648.
44. Madalena, D.A., Ramos, O.L., Pereira, R.N., Bourbon, A.I., Pinheiro, A.C., Malcata, F.X., et al. In vitro digestion and stability assessment of beta-lactoglobulin/riboflavin nanostructures. Food Hydrocolloids 58 (2016), 89–97.
45. Ma, H., Forssell, P., Partanen, R., Buchert, J., Boer, H., Charge modifications to improve the emulsifying properties of whey protein isolate. Journal of Agricultural and Food Chemistry 59 (2011), 13246–13253.
46. Mirmoghtadaie, L., Aliabadi, S.S., Hosseini, S.M., Recent approaches in physical modification of protein functionality. Food Chemistry 199 (2016), 619–627.
47. Mishra, S., Mann, B., Joshi, V.K., Functional improvement of whey protein concentrate on interaction with pectin. Food Hydrocolloids 15 (2001), 9–15.
48. Mitidieri, F.E., Wagner, J.R., Coalescence of o/w emulsions stabilized by whey and isolate soybean proteins. Influence of thermal denaturation, salt addition and competitive interfacial adsorption. Food Research International 35 (2002), 547–557.
49. Moro, A., Gatti, C., Delorenzi, N., Hydrophobicity of whey protein concentrates measured by fluorescence quenching and its relation with surface functional properties. Journal of Agricultural and Food Chemistry 49 (2001), 4784–4789.
50. Nicolai, T., Britten, M., Schmitt, C., β-Lactoglobulin and WPI aggregates: Formation, structure and applications. Food Hydrocolloids 25 (2011), 1945–1962.
51. Nicolai, T., Durand, D., Controlled food protein aggregation for new functionality. Current Opinion in Colloid & Interface Science 18 (2013), 249–256.
52. Nik, A.M., Tosh, S., Poysa, V., Woodrow, L., Corredig, M., Physicochemical characterization of soymilk after step-wise centrifugation. Food Research International 41 (2008), 286–294.
53. O'Sullivan, J., Arellano, M., Pichot, R., Norton, I., The effect of ultrasound treatment on the structural, physical and emulsifying properties of dairy proteins. Food Hydrocolloids 42 (2014), 386–396.
54. O'Sullivan, J., Beevers, J., Park, M., Greenwood, R., Norton, I., Comparative assessment of the effect of ultrasound treatment on protein functionality pre- and post-emulsification. Colloids and Surfaces a-Physicochemical and Engineering Aspects 484 (2015), 89–98.
55. Peram, M.R., Loveday, S.M., Ye, A.Q., Singh, H., In vitro gastric digestion of heat-induced aggregates of beta-lactoglobulin. Journal of Dairy Science 96 (2013), 63–74.
56. Ramos, O.L., Pereira, R.N., Rodrigues, R., Teixeira, J.A., Vicente, A.A., Xavier, et al. Physical effects upon whey protein aggregation for nanocoating production. Food Research International 66 (2014), 344–355.
57. Raoufi, N., Fang, Y.P., Kadkhodaee, R., O'Phillips, G., Najafi, M.N., Changes in turbidity, zeta potential and precipitation yield induced by persian gum-whey protein isolate interactions during acidification. Journal of Food Processing and Preservation, 2016, 1–8.
58. Raso, J., Manas, P., Pagan, R., Sala, F.J., Influence of different factors on the output power transferred into medium by ultrasound. Ultrasonics Sonochemistry 5 (1999), 157–162.
59. Ryan, K.N., Foegeding, E.A., Formation of soluble whey protein aggregates and their stability in beverages. Food Hydrocolloids 43 (2015), 265–274.
60. Ryan, K.N., Vardhanabhuti, B., Jaramillo, D.P., van Zanten, J.H., Coupland, J.N., Foegeding, E.A., Stability and mechanism of whey protein soluble aggregates thermally treated with salts. Food Hydrocolloids 27 (2012), 411–420.
61. Ryan, K.N., Zhong, Q., Foegeding, E.A., Use of whey protein soluble aggregates for thermal stabilityA hypothesis paper. Journal of Food Science 78 (2013), R1105–R1115.
62. Schmitt, C., Bovay, C., Rouvet, M., Shojaei-Rami, S., Kolodziejczyk, E., Whey protein soluble aggregates from heating with NaCl: Physicochemical, interfacial, and foaming properties. Langmuir 23 (2007), 4155–4166.
63. Segat, A., Misra, N.N., Fabbro, A., Buchini, F., Lippe, G., Cullen, P.J., et al. Effects of ozone processing on chemical, structural and functional properties of whey protein isolate. Food Research International 66 (2014), 365–372.
64. Singh, T.K., Oiseth, S.K., Lundin, L., Day, L., Influence of heat and shear induced protein aggregation on the in vitro digestion rate of whey proteins. Food & Function 5 (2014), 2686–2698.
65. Smithers, G.W., Whey-ing up the options - Yesterday, today and tomorrow. International Dairy Journal 48 (2015), 2–14.
66. Soria, A.C., Villamiel, M., Effect of ultrasound on the technological properties and bioactivity of food: A review. Trends in Food Science & Technology 21 (2010), 323–331.
67. de Souza, H.K.S., Bai, G., Goncalves, M.D.P., Bastos, M., Whey protein isolate-chitosan interactions: A calorimetric and spectroscopy study. Thermochimica Acta 495 (2009), 108–114.
68. Sun, Y., Chen, J., Zhang, S., Li, H., Lu, J., Liu, L., et al. Effect of power ultrasound pre-treatment on the physical and functional properties of reconstituted milk protein concentrate. Journal of Food Engineering 124 (2014), 11–18.
69. Taylor, M.J., Richardson, T., Antioxidant activity of skim milk: Effect of sonication. Journal of Dairy Science 63 (1980), 1938–1942.
70. Turian, R.M., Attal, J.F., Sung, D.J., Wedgewood, L.E., Properties and rheology of coal-water mixtures using different coals. Fuel 81 (2002), 2019–2033.
71. Unterhaslberger, G., Schmitt, C., Sanchez, C., Appolonia-Nouzille, C., Raemy, A., Heat denaturation and aggregation of beta-lacto globulin enriched WPI in the presence of arginine HCl, NaCl and guanidinium HCl at pH 4.0 and 7.0. Food Hydrocolloids 20 (2006), 1006–1019.
72. Vardhanabhuti, B., Foegeding, E.A., Rheological properties and characterization of polymerized whey protein isolates. Journal of Agricultural and Food Chemistry 47 (1999), 3649–3655.
73. Wagoner, T., Vardhanabhuti, B., Foegeding, E.A., Designing Whey protein-polysaccharide particles for colloidal stability. Annual Review of Food Science and Technology 7 (2016), 93–116.
74. Wang, W., Zhong, Q., Hu, Z., Nanoscale understanding of thermal aggregation of whey protein pretreated by transglutaminase. Journal of Agricultural and Food Chemistry 61 (2013), 435–446.
75. Webb, M.R., Naeem, H.A., Schmidt, K.A., Food protein functionality in a liquid system: A comparison of deamidated wheat protein with dairy and soy proteins. Journal of Food Science 67 (2002), 2896–2902.
76. Wijayanti, H.B., Bansal, N., Deeth, H.C., Stability of whey proteins during thermal processing: A review. Comprehensive Reviews in Food Science and Food Safety 13 (2014), 1235–1251.
77. Zhong, Q., Wang, W., Hu, Z., Ikeda, S., Sequential preheating and transglutaminase pretreatments improve stability of whey protein isolate at pH 7.0 during thermal sterilization. Food Hydrocolloids 31 (2013), 306–316.
78. Zisu, B., Bhaskaracharya, R., Kentish, S., Ashokkumar, M., Ultrasonic processing of dairy systems in large scale reactors. Ultrasonics Sonochemistry 17 (2010), 1075–1081.