Increasing the emulsifying capacity of whey proteins at acidic pH values through covalent modification with allyl isothiocyanate

Colloids and Surfaces A: Physicochemical and Engineering Aspects

Volumn 522, Issue , 2017, Pages 514-524

  Keppler, Julia K ^a   Schwarz, Karin ^a  

^a UNIVERSITY OF KIEL   (Germany)

Author keywords

Allyl isothiocyanate; Beta Lactoglobulin; Covalent Modification; Creaming; Emulsion; Whey protein isolate

Indexed keywords

EMULSIONS; PH; PROTEINS;

ALLYL ISOTHIOCYANATE; BETA-LACTOGLOBULIN; COVALENT MODIFICATIONS; CREAMING; WHEY PROTEIN ISOLATE;

EMULSIFICATION;

ALLYL ISOTHIOCYANATE; AMIDE; OIL; RAPESEED OIL; WHEY PROTEIN;

ARTICLE; CHEMICAL MODIFICATION; CLINICAL ASSESSMENT; CONCENTRATION PROCESS; DISULFIDE BOND; ELECTROPHILICITY; EMULSION; HYDROPHOBICITY; NONHUMAN; PH; PHYSICAL CHEMISTRY; PRIORITY JOURNAL; PROTEIN STABILITY; ZETA POTENTIAL;

EID: 85016509968     PISSN: 09277757     EISSN: 18734359     Source Type: Journal    
DOI: 10.1016/j.colsurfa.2017.03.033     Document Type: Article

References (49)

1. [1] Dickinson, E., Milk protein interfacial layers and the relationship to emulsion stability and rheology. Colloids Surf. B Biointerfaces 20:3 (2001), 197–210.
2. [2] Gulzar, M., Lechevalier, V., Bouhallab, S., Croguennec, T., The physicochemical parameters during dry heating strongly influence the gelling properties of whey proteins. J. Food Eng. 112:4 (2012), 296–303.
3. [3] Das, K., Kinsella, J.E., pH dependent emulsifying properties of beta-lactoglobulin. J. Dispers. Sci. Technol. 10:1 (1989), 77–102.
4. [4] Kim, D.A., Cornec, M., Narsimhan, G., Effect of thermal treatment on interfacial properties of b-lactoglobulin. J. Colloid Interface Sci. 285:1 (2005), 100–109.
5. [5] McClements, D.J., Protein-stabilized emulsions. Curr. Opin. Colloid Interface Sci. 9:5 (2004), 305–313.
6. [6] Kim, H.-J., Decker, E.A., McClements, D.J., Impact of protein surface denaturation on droplet flocculation in hexadecane oil-in-water emulsions stabilized by beta-lactoglobulin. J. Agric. Food Chem. 50:24 (2002), 7131–7137.
7. [7] Mantovani, R.A., Cavallieri, Fazani, Angelo Luiz, Netto, F.M., Cunha, R.L., Stability and in vitro digestibility of emulsions containing lecithin and whey proteins. Food Funct. 4:9 (2013), 1322–1331.
8. [8] Masson, G., Jost, R., A study of oil-in-water emulsions stabilized by whey proteins. Colloid Polym. Sci. 264:7 (1986), 631–638.
9. [9] Dickinson, E., Matsumura, Y., Time-dependent polymerization of beta-lactoglobulin through disulphide bonds at the oil-water interface in emulsions. Int. J. Biol. Macromol. 13:1 (1991), 26–30.
10. [10] Tcholakova, S., Denkov, N.D., Ivanov, I.B., Campbell, B., Coalescence stability of emulsions containing globular milk proteins. Adv. Colloid Interface Sci. 123–126 (2006), 259–293.
11. [11] Kim, H.J., Decker, E.A., McClements, D.J., Comparison of droplet flocculation in hexadecane oil-in-water emulsions stabilized by beta-lactoglobulin at pH 3 and 7. Langmuir 20:14 (2004), 5753–5758.
12. [12] Matsumura, Y., Mitsui, S., Dickinson, E., Mori, T., Competitive adsorption of α-lactalbumin in the molten globule state. Food Hydrocoll. 8:6 (1994), 555–566.
13. [13] Shimizu, M., Kamiya, T., Yamauchi, K., The adsorption of whey proteins on the surface of emulsfied fat. Agric. Biol. Chem. 45:11 (1981), 2491–2496.
14. [14] Graham, D., Phillips, M., Proteins at liquid interfaces. J. Colloid Interface Sci. 70:3 (1979), 427–439.
15. [15] Das, K.P., Kinsella, J.E., Droplet size and coalescence stability of whey protein stabilized milkfat peanut oil emulsions. J. Food Sci. 58:2 (1993), 439–444.
16. [16] Halpin, M.I., Richardson, T., Selected functionality changes of beta-lactoglobulin upon esterification of side-chain carboxyl groups. J. Dairy Sci. 68:12 (1985), 3189–3198.
17. [17] Sitohy, M., Chobert, J.M., Haertlé, T., Improvement of solubility and of emulsifying properties of milk proteins at acid pHs by esterification. Die Nahrung 45:2 (2001), 87–93.
18. [18] Dickinson, E., James, J.D., Rheology and flocculation of high-pressure-treated β-lactoglobulin-stabilized emulsions: comparison with thermal treatment. J. Agric. Food Chem. 46:7 (1998), 2565–2571.
19. [19] Moro, A., Báez, G.D., Ballerini, G.A., Busti, P.A., Delorenzi, N.J., Emulsifying and foaming properties of β-lactoglobulin modified by heat treatment. Food Res. Int. 51:1 (2013), 1–7.
20. [20] Raikos, V., Effect of heat treatment on milk protein functionality at emulsion interfaces. A review. Food Hydrocoll. 24:4 (2010), 259–265.
21. [21] Rade-Kukic, K., Schmitt, C., Rawel, H.M., Formation of conjugates between [beta]-lactoglobulin and allyl isothiocyanate: effect on protein heat aggregation, foaming and emulsifying properties: food colloids 2010: on the road from interfaces to consumers. Food Hydrocoll. 25:4 (2011), 694–706.
22. [22] Keppler, J.K., Koudelka, T., Palani, K., Stuhldreier, M.C., Temps, F., Tholey, A., Schwarz, K., Characterization of the covalent binding of allyl isothiocyanate to β-lactoglobulin by fluorescence quenching, equilibrium measurement, and mass spectrometry. J. Biomol. Struct. Dyn. 32:7 (2014), 1103–1117.
23. [23] Keppler, J.K., Koudelka, T., Palani, K., Tholey, A., Schwarz, K., Interaction of β-lactoglobulin with small hydrophobic ligands—influence of covalent AITC modification on β-LG tryptic cleavage. Food Biophys. 9:4 (2014), 349–358.
24. [24] Keppler, J.K., Martin, D., Garamus, V.M., Berton-Carabin, C., Nipoti, E., Coenye, T., Schwarz, K., Functionality of whey proteins covalently modified by allyl isothiocyanate. Part 1 physicochemical and antibacterial properties of native and modified whey proteins at pH 2 to 7. Food Hydrocoll. 65 (2017), 130–143.
25. [25] Clawin-Rädecker, I., Kiesner, C., Schlimme, E., Analyse der säurelöslichen Gehalte von α-Lactalbumin, β-Lactoglobulin, Serumalbumin und der Immunglobulinfraktion in pasteurisierter Milch. Kieler Milchwirtschaftliche Forschungsberichte 52 (2000), 323–334.
26. [26] Keppler, J.K., Sönnichsen, F.D., Lorenzen, P.-C., Schwarz, K., Differences in heat stability and ligand binding among β-lactoglobulin genetic variants A, B and C using (1)H NMR and fluorescence quenching. Biochim. Biophys. Acta 1844:6 (2014), 1083–1093.
27. [27] Serfert, Y., Lamprecht, C., Tan, C.-P., Keppler, J.K., Appel, E., Rossier-Miranda, F.J., Schroen, K., Boom, R.M., Gorb, S., Selhuber-Unkel, C., Drusch, S., Schwarz, K., Characterisation and use of β-lactoglobulin fibrils for microencapsulation of lipophilic ingredients and oxidative stability thereof. J. Food Eng. 143:0 (2014), 53–61.
28. [28] Wilde, S.C., Keppler, J.K., Palani, K., Schwarz, K., beta-Lactoglobulin as nanotransporter—part I: binding of organosulfur compounds. Food Chem. 197:28 (2016), 1015–1021.
29. [29] Li, Y., Teng, Z., Chen, P., Song, Y., Luo, Y., Wang, Q., Enhancement of aqueous stability of allyl isothiocyanate using nanoemulsions prepared by an emulsion inversion point method. J. Colloid Interface Sci. 438 (2015), 130–137.
30. [30] Liu, T.-T., Yang, T.-S., Stability and antimicrobial activity of allyl isothiocyanate during long-term storage in an oil-in-water emulsion. J. Food Sci. 75:5 (2010), C445–C451.
31. [31] Ragona, L., Pusterla, F., Zetta, L., Monaco, H.L., Molinari, H., Identification of a conserved hydrophobic cluster in partially folded bovine β-lactoglobulin at pH 2. Fold. Des. 2:5 (1997), 281–290.
32. [32] Kuwata, K., Era, S., Hoshino, M., Forge, V., Goto, Y., Batt, C.A., Solution structure and dynamics of bovine β-lactoglobulin A. Protein Sci. 8:11 (1999), 2541–2545.
33. [33] Dickinson, E., Rolfe, S.E., Dalgleish, D.G., Surface shear viscometry as a probe of protein-protein interactions in mixed milk protein films adsorbed at the oil-water interface. Int. J. Biol. Macromol. 12:3 (1990), 189–194.
34. [34] Tcholakova, S., Denkov, N.D., Sidzhakova, D., Ivanov, I.B., Campbell, B., Effects of electrolyte concentration and pH on the coalescence stability of beta-lactoglobulin emulsions: experiment and interpretation. Langmuir 21:11 (2005), 4842–4855.
35. [35] Kato, A., Nakai, S., Hydrophobicity determined by a fluorescence probe method and its correlation with surface properties of proteins. Biochim. Biophys. Acta (BBA) Protein Struct. 624:1 (1980), 13–20.
36. [36] Fogolari, F., Ragona, L., Zetta, L., Romagnoli, S., De Kruif, K.G., Molinari, H., Monomeric bovine β-lactoglobulin adopts a β-barrel fold at pH 2. FEBS Lett. 436:2 (1998), 149–154.
37. [37] Engelhardt, K., Lexis, M., Gochev, G., Konnerth, C., Miller, R., Willenbacher, N., Peukert, W., Braunschweig, B., pH effects on the molecular structure of β-lactoglobulin modified air–water interfaces and its impact on foam rheology. Langmuir 29:37 (2013), 11646–11655.
38. [38] Ali, A., Mekhloufi, G., Huang, N., Agnely, F., β-Lactoglobulin stabilized nanemulsions—formulation and process factors affecting droplet size and nanoemulsion stability. Int. J. Pharm. 500:1–2 (2016), 291–304.
39. [39] Noureddini, H., Teoh, B.C., Davis Clements, L., Viscosities of vegetable oils and fatty acids. J. Am. Oil Chem. Soc. 69:12 (1992), 1189–1191.
40. [40] Cheetangdee, N., Oki, M., Fukada, K., The coalescence stability of protein-stabilized emulsions estimated by analytical photo-centrifugation. J. Oleo Sci. 60:8 (2011), 419–427.
41. [41] Rangsansarid, J., Fukada, K., Factors affecting the stability of O/W emulsion in BSA solution: stabilization by electrically neutral protein at high ionic strength. J. Colloid Interface Sci. 316:2 (2007), 779–786.
42. [42] Sun, C., Gunasekaran, S., Effects of protein concentration and oil-phase volume fraction on the stability and rheology of menhaden oil-in-water emulsions stabilized by whey protein isolate with xanthan gum. Food Hydrocoll. 23:1 (2009), 165–174.
43. [43] Dickinson, E., Flocculation of protein-stabilized oil-in-water emulsions. Colloids Surf. B Biointerfaces 81:1 (2010), 130–140.
44. [44] Delahaije, R.J., Wierenga, P.A., van Nieuwenhuijzen, N.H., Giuseppin, M.L., Gruppen, H., Protein concentration and protein-exposed hydrophobicity as dominant parameters determining the flocculation of protein-stabilized oil-in-water emulsions. Langmuir 29:37 (2013), 11567–11574.
45. [45] Badolato, G.G., Aguilar, F., Schuchmann, H.P., Sobisch, T., Lerche, D., Evaluation of long term stability of model emulsions by multisample analytical centrifugation. Auernhammer, G.K., Butt, H.-J., Vollmer, D., (eds.) Surface and Interfacial Forces—From Fundamentals to Applications, 2008, Springer Berlin Heidelberg, Berlin, Heidelberg, 66–73.
46. [46] Sobisch, T., Lerche, D., Thickener performance traced by multisample analytical centrifugation, Frontiers in formulation science (Formula V—2007)., November 2007, Potsdam, Germany Selected Papers from the 5th International Conference on Formulation Technology, 331, 2008, 114–118 1–2.
47. [47] Robins, M.M., Emulsions—creaming phenomena. Curr. Opin. Colloid Interface Sci. 5:5–6 (2000), 265–272.
48. [48] Ali, M., Homann, T., Khalil, M., Kruse, H.-P., Rawel, H., Milk whey protein modification by coffee-specific phenolics: effect on structural and functional properties. J. Agric. Food Chem. 61:28 (2013), 6911–6920.
49. [49] ISO/TR 13097:2013 (E), Guidelines for the characterization of dispersion stability.