Influence of heat on miscibility of Quillaja saponins in mixtures with a co-surfactant

Food Research International

Volumn 88, Issue , 2016, Pages 16-23

  Reichert, Corina L ^a   Salminen, Hanna ^a   Leuenberger, Bruno H ^b   Weiss, Jochen ^a  

^a UNIVERSITY OF HOHENHEIM   (Germany)

^b DSM NUTRITIONAL PRODUCTS LTD   (Switzerland)

Author keywords

Heating; Lecithin; Miscibility; Protein; Quillaja saponin; Surface hydrophobicity

Indexed keywords

ASSOCIATION REACTIONS; BINS; FLOCCULATION; HEAT TREATMENT; HEATING; HYDROPHOBICITY; LECITHIN; MIXTURES; OILSEEDS; PROTEINS; SODIUM; SOLUBILITY; SURFACE ACTIVE AGENTS; THERMAL PROCESSING (FOODS);

BINARY SURFACTANT SYSTEMS; CONCENTRATION RATIO; ELECTROSTATIC REPULSIVE FORCES; HYDROPHOBIC INTERACTIONS; MISCIBILITY BEHAVIOR; MIXED SURFACTANT SYSTEMS; QUILLAJA SAPONIN; SURFACE HYDROPHOBICITY;

METABOLITES;

EID: 84963960020     PISSN: 09639969     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.foodres.2016.03.034     Document Type: Article

References (36)

1. 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.
2. Alizadeh-Pasdar, N., Li-Chan, E.C.Y., Application of PRODAN fluorescent probe to measure surface hydrophobicity of proteins interacting with κ-carrageenan. Food Hydrocolloids 15 (2001), 285–294.
3. Batista, A.P., Portugal, C.A.M., Sousa, I., Crespo, J.G., Raymundo, A., Accessing gelling ability of vegetable proteins using rheological and fluorescence techniques. International Journal of Biological Macromolecules 36 (2005), 135–143.
4. Brune, M., Hallberg, L., Skaanberg, A.B., Determination of iron-binding phenolic groups in foods. Journal of Food Science 56 (1991), 128–131.
5. FAO-WHO, Safety evaluation of certain food additives. Chemical and technical assessment — Quillaja extract type 1 and type 2. Joint FAO–WHO Expert Committee report on food additives (65th: 17). 2005, International Programme on Chemical Safety World Health Organization, Geneva, Switzerland.
6. Fukuda, K., Utsumi, H., Shoji, J., Hamada, A., Saponins can cause the agglutination of phospholipid vesicles. Biochimica et Biophysica Acta (BBA) - Biomembranes 820 (1985), 199–206.
7. Grizzuti, K., Perlmann, G.E., Binding of magnesium and calcium ions to the phosphoglycoprotein phosvitin. Biochemistry 12 (1973), 4399–4403.
8. Grizzuti, K., Perlmann, G.E., Further studies on the binding of divalent cations to the phosphoglycoprotein phosvitin. Biochemistry 14 (1975), 2171–2175.
9. Horne, D.S., Casein interactions: Casting light on the black boxes, the structure in dairy products. International Dairy Journal 8 (1998), 171–177.
10. Huopalahti, R., López-Fandiño, R., Anton, M., Schade, R., Bioactive egg compounds. 2007, Springer, Berlin.
11. Jakobek, J., Interactions of polyphenols with carbohydrates, lipids and proteins. Food Chemistry 175 (2015), 556–567.
12. Jiang, B., Mine, Y., Phosphopeptides derived from hen egg yolk phosvitin: Effect of molecular size on the calcium-binding properties. Bioscience, Biotechnology, and Biochemistry 65 (2001), 1187–1190.
13. Kessler, A., Menéndez-Aguirre, O., Hinrichs, J., Stubenrauch, C., Weiss, J., Properties of an αs-casein-rich casein fraction: Influence of dialysis on surface properties, miscibility, and micelle formation. Journal of Dairy Science 96 (2013), 5575–5590.
14. Kezwon, A., Wojciechowski, K., Interaction of Quillaja bark saponins with food-relevant proteins. Advances in Colloid and Interface Science 209 (2014), 185–195.
15. Li-Chan, E.C.Y., Hydrophobicity in food protein systems. Hui, Y.H., Francis, F.J., (eds.) Encyclopedia of food science and technology, 2nd ed., 2000, Wiley, New York.
16. Ma, Z., Boye, J.I., Simpson, B.K., Prasher, S.O., Monpetit, D., Malcolmson, L., Thermal processing effects on the functional properties and microstructure of lentil, chickpea, and pea flours. Food Research International 44 (2011), 2534–2544.
17. Maier, C., Conrad, J., Carle, R., Weiss, J., Schweiggert, R.M., Phenolic constituents in commercial aqueous Quillaja (Quillaja saponaria Molina) wood extracts. Journal of Agricultural and Food Chemistry 63 (2015), 1756–1762.
18. McClements, D.J., Food emulsions principles, practices, and techniques. 2nd ed., 2005, CRC Press, Boca Raton, Florida, USA.
19. McFarlane, N.L., Wagner, N.J., Kaler, E.W., Lynch, M.L., Poly(ethylene oxide) (PEO) and poly(vinyl pyrolidone) (PVP) induce different changes in the colloid stability of nanoparticles. Langmuir 26 (2010), 13823–13830.
20. Mession, J.L., Sok, N., Assifaoui, A., Saurel, R., Thermal denaturation of pea globulins (Pisum sativum L.) — Molecular interactions leading to heat-induced protein aggregation. Journal of Agricultural and Food Chemistry 61 (2013), 1196–1204.
21. Morton, P.A.J., Murray, B.S., Acid beverage floc: Protein–saponin interactions and an unstable emulsion model. Colloids and Surfaces B: Biointerfaces 21 (2001), 101–106.
22. 1H NMR spectra for saponins from Quillaja saponaria Molina. Analytica Chimica Acta 446 (2001), 199–209.
23. O'Kane, F., Molecular characterization and heat-induced gelation of pea vicilin and legumin. (Phd thesis), 2004, Wageningen University.
24. Ozdal, T., Capanoglu, E., Altay, F., A review on protein–phenolic interactions and associated changes. Food Research International 51 (2013), 954–970.
25. Palacios, A.C., Sarnthein-Graf, C., La Mesa, C., Equilibrium between phases in water–protein–surfactant systems. Colloids and Surfaces A: Physicochemical and Engineering Aspects 228 (2003), 25–35.
26. Pomeranz, Y., Functional properties of food components. 2nd ed., 1991, Academic Press, San Diego, California.
27. Post, A.E., Arnold, B., Weiss, J., Hinrichs, J., Effect of temperature and pH on the solubility of caseins: Environmental influences on the dissociation of αS- and β-casein. Journal of Dairy Science 95 (2012), 1603–1616.
28. Potter, S.M., Jimenez-Flores, R., Pollack, J., Lone, T.A., Berber-Jimenez, M.D., Protein–saponin interaction and its influence on blood lipids. Journal of Agricultural and Food Chemistry 41 (1993), 1287–1291.
29. Qi, P.X., Wickham, E.D., Farrell, H.M. Jr., Thermal and alkaline denaturation of bovine β-casein. Protein Journal 23 (2004), 389–402.
30. Reichert, C.L., Salminen, H., Leuenberger, B.H., Hinrichs, J., Weiss, J., Miscibility of Quillaja saponins with other co-surfactants under different pH values. Journal of Food Science 80 (2015), E2495–E2503.
31. Skurtys, O., Aguilera, J.M., Formation of O/W macroemulsions with a circular microfluidic device using saponin and potato starch. Food Hydrocolloids 23 (2009), 1810–1817.
32. Sun, X.D., Arntfield, S.D., Gelation properties of salt-extracted pea protein isolate induced by heat treatment: Effect of heating and cooling rate. Food Chemistry 124 (2011), 1011–1016.
33. Tanaka, M., Fang-I, L., Ishizaki, S., Taguchi, T., Interaction of saponins with salt-soluble proteins from walleye pollack meat. Fisheries Science 61 (1995), 373–374.
34. Wojciechowski, K., Kezwon, A., Lewandowska, J., Marcinkowski, K., Effect of β-casein on surface activity of Quillaja bark saponin at fluid/fluid interfaces. Food Hydrocolloids 34 (2014), 208–216.
35. Yang, Y., Leser, M.E., Sher, A.A., McClements, D.J., Formation and stability of emulsions using a natural small molecule surfactant: Quillaja saponin (Q-Naturale®). Food Hydrocolloids 30 (2013), 589–596.
36. Young, E.G., Phinney, J.I., On the fractionation of the proteins of egg yolk. The Journal of Biological Chemistry 193 (1951), 73–80.