Efficient delivery of quercetin after binding to beta-lactoglobulin followed by formation soft-condensed core-shell nanostructures

Food Chemistry

Volumn 233, Issue , 2017, Pages 282-289

  Mirpoor, Seyedeh Fatemeh ^a   Hosseini, Seyed Mohammad Hashem ^a   Nekoei, Abdo Reza ^b  

^a SHIRAZ UNIVERSITY   (Iran)

^b SHIRAZ UNIVERSITY OF TECHNOLOGY   (Iran)

Author keywords

Complex coacervation; Controlled release; Core shell; Nanoencapsulation; Nanoparticle; Quercetin; Soft condensation

Indexed keywords

BINS; HIGH RESOLUTION TRANSMISSION ELECTRON MICROSCOPY; NANOPARTICLES; NANOSTRUCTURES; PHENOLS; SHELLS (STRUCTURES); TRANSMISSION ELECTRON MICROSCOPY;

COMPLEX COACERVATION; CONTROLLED RELEASE; CORE SHELL; NANO-ENCAPSULATION; QUERCETIN;

FLAVONOIDS;

ALGINIC ACID; BETA LACTOGLOBULIN; BIOPOLYMER; NANOMATERIAL; QUERCETIN; LACTOGLOBULIN;

ARTICLE; CONTROLLED STUDY; ENCAPSULATION; FLUORESCENCE; FLUOROMETRY; HEAT TREATMENT; PARTICLE SIZE; PH; PROTEIN BINDING; STOICHIOMETRY; STOMACH JUICE; SUSTAINED DRUG RELEASE; TRANSMISSION ELECTRON MICROSCOPY;

HYDROGEN-ION CONCENTRATION; LACTOGLOBULINS; MICROSCOPY, ELECTRON, TRANSMISSION; NANOSTRUCTURES; QUERCETIN;

EID: 85018803332     PISSN: 03088146     EISSN: 18737072     Source Type: Journal    
DOI: 10.1016/j.foodchem.2017.04.126     Document Type: Article

References (37)

1. Aberkane, L., Jasniewski, J., Gaiani, C., Hussain, R., Scher, J., Sanchez, C., Structuration mechanism of β-lactoglobulin – Acacia gum assemblies in presence of quercetin. Food Hydrocolloids 29 (2012), 9–20.
2. Aceituno-Medina, M., Mendoza, S., Rodríguez, B.A., Lagaron, J.M., López-Rubio, A., Improved antioxidant capacity of quercetin and ferulic acid during in-vitro digestion through encapsulation within food-grade electrospun fibers. Journal of Functional Foods 12 (2015), 332–341.
3. Arroyo-Maya, I.J., McClements, D.J., Biopolymer nanoparticles as potential delivery systems for anthocyanins: Fabrication and properties. Food Research International 69 (2015), 1–8.
4. Chen, L., Subirade, M., Alginate–whey protein granular microspheres as oral delivery vehicles for bioactive compounds. Biomaterials 27:26 (2006), 4646–4654.
5. Cogan, U., Kopelman, M., Mokady, S., Shinitzky, M., Binding affinities of retinol and related compounds to retinol binding proteins. European Journal of Biochemistry 65:1 (1976), 71–78.
6. D'Andrea, G., Quercetin: A flavonol with multifaceted therapeutic applications?. Fitoterapia 106 (2015), 256–271.
7. Dufour, E., Genot, C., Haertlé, T., β-Lactoglobulin binding properties during its folding changes studied by fluorescence spectroscopy. Biochimica et Biophysica Acta (BBA)-Protein Structure and Molecular Enzymology 1205:1 (1994), 105–112.
8. Giampieri, F., Alvarez-Suarez, J.M., Battino, M., Strawberry and human health: Effects beyond antioxidant activity. Journal of Agricultural and Food Chemistry 62:18 (2014), 3867–3876.
9. Gilley, A.D., Arca, H.C., Nichols, B.L.B., Mosquera-Giraldo, L.I., Taylor, L.S., Edgar, K.J., Neilson, A.P., Novel cellulose-based amorphous solid dispersions enhance quercetin solution concentrations in vitro. Carbohydrate Polymers 157 (2017), 86–93.
10. Gutierrez, J.C., Prater, M.R., Holladay, S.D., Quercetin supplementation reduces maternal hyperglycemia in a type 2 diabetes mellitus mouse model. Annual Research & Review in Biology 4:1 (2014), 306–311.
11. Ha, H.K., Kim, J.W., Lee, M.R., Lee, W.J., Formation and characterization of quercetin-loaded chitosan oligosaccharide/β-lactoglobulin nanoparticle. Food Research International 52 (2013), 82–90.
12. Hosseini, S.M.H., Emam-Djomeh, Z., Razavi, S.H., Moosavi-Movahedi, A.A., Saboury, A.A., Mohammadifar, M.A.,. Van der Meeren, P., Complex coacervation of β-lactoglobulin- κ-Carrageenan aqueous mixtures as affected by polysaccharide sonication. Food Chemistry 141 (2013), 215–222.
13. Hosseini, S.M.H., Emam-Djomeh, Z., Sabatino, P., Van der Meeren, P., Nanocomplexes arising from protein-polysaccharide electrostatic interaction as a promising carrier for nutraceutical compounds. Food Hydrocolloids 50 (2015), 16–26.
14. Ilyasoglu, H., El, S.N., Nanoencapsulation of EPA/DHA with sodium caseinate–gum Arabic complex and its usage in the enrichment of fruit juice. LWT-Food Science and Technology 56:2 (2014), 461–468.
15. Kitson, T.M., Spectrophotometric and kinetic studies on the binding of the bioflavonoid quercetin to bovine serum albumin. Bioscience, Biotechnology, and Biochemistry 68:10 (2004), 2165–2170.
16. Kontopidis, G., Holt, C., Sawyer, L., Invited review: β-lactoglobulin: Binding properties, structure, and function. Journal of Dairy Science 87:4 (2004), 785–796.
17. Kumari, A., Yadav, S.K., Pakade, Y.B., Singh, B., Yadav, S.C., Development of biodegradable nanoparticles for delivery of quercetin. Colloids and Surfaces B: Biointerfaces 80:2 (2010), 184–192.
18. Lakowicz, J.R., Freshwater, G., Weber, G., Nanosecond segmental mobilities of tryptophan residues in proteins observed by lifetime-resolved fluorescence anisotropies. Biophysical Journal, 32(1), 1980, 591.
19. Liang, L., Tajmir-Riahi, H.A., Subirade, M., Interaction of β-lactoglobulin with resveratrol and its biological implications. Biomacromolecules 9:1 (2007), 50–56.
20. Liu, W., Guo, R., Interaction between flavonoid, quercetin and surfactant aggregates with different charges. Journal of Colloid and Interface Science 302 (2006), 625–632.
21. Mátyus, L., Szöllősi, J., Jenei, A., Steady-state fluorescence quenching applications for studying protein structure and dynamics. Journal of Photochemistry and Photobiology B: Biology 83:3 (2006), 223–236.
22. Mohan Reddy, I., Kella, N.K.D., Kinsella, J.E., Structural and conformational basis of the resistance of β-lactoglobulin to peptic and chymotryptic digestion. Journal of Agricultural and Food Chemistry 36 (1988), 737–747.
23. Nori, M.P., Favaro-Trindade, C.S., de Alencar, S.M., Thomazini, M., de Camargo Balieiro, J.C., Castillo, C.J.C., Microencapsulation of propolis extract by complex coacervation. LWT-Food Science and Technology 44 (2011), 429–435.
24. Perez, A.A., Sponton, O.E., Andermatten, R.B., Amelia, C., Rubiolo, A.C., Santiago, L.G., Biopolymer nanoparticles designed for polyunsaturated fatty acid vehiculization: Protein–polysaccharide ratio study. Food Chemistry 188 (2015), 543–550.
25. Riihimäki, L.H., Vainio, M.J., Heikura, J.M., Valkonen, K.H., Virtanen, V.T., Vuorela, P.M., Binding of phenolic compounds and their derivatives to bovine and reindeer β-lactoglobulin. Journal of Agricultural and Food Chemistry 56:17 (2008), 7721–7729.
26. Ross, J.A., Kasum, C.M., Dietary flavonoids: Bioavailability, metabolic effects, and safety. Annual Review of Nutrition 22:1 (2002), 19–34.
27. Sahihi, M., Heidari-Koholi, Z., Bordbar, A.K., The interaction of polyphenol flavonoids with β-lactoglobulin: Molecular docking and molecular dynamics simulation studies. Journal of Macromolecular Science, Part B 51:12 (2012), 2311–2323.
28. Sanchez, C., Mekhloufi, G., Schmitt, C., Renard, D., Robert, P., Lehr, C.M., Hardy, J., Self-assembly of β-lactoglobulin and acacia gum in aqueous solvent: Structure and phase-ordering kinetics. Langmuir 18:26 (2002), 10323–10333.
29. Souza, M.P., Vaz, A.F.M., Correia, M.T.S., Cerqueira, M.A., Vicente, A.A., Carneiro-da-Cunha, M.G., Quercetin-loaded lecithin/chitosan nanoparticles for functional food applications. Food and Bioprocess Technology 7 (2013), 1149–1159.
30. Staszewski, M.V., Jagus, R.J., & Pilosof, A.M.R. (2011). Characterization of whey protein-polyphenol interactions by dynamic light scattering. presented in part at 11th International Congress on Engineering and Food, Athens, Greece, May.
31. Vasbinder, A.J., De Kruif, C.G., Casein–whey protein interactions in heated milk: The influence of pH. International Dairy Journal 13 (2003), 669–677.
32. 3 binding site of milk β-lactoglobulin. Proteins: Structure, Function, and Bioinformatics 71:3 (2008), 1197–1210.
33. Wang, W., Sun, C., Mao, L., Ma, P., Liu, F., Yang, J., Gao, Y., The biological activities, chemical stability, metabolism and delivery systems of quercetin: A review. Trends in Food Science & Technology 56 (2016), 21–38.
34. Zhang, L., Qi, Z., Huang, Q., Zeng, K., Sun, X., Li, J., Liu, Y.N., Imprinted-like biopolymeric micelles as efficient nanovehicles for curcumin delivery. Colloids and Surfaces B: Biointerfaces 123 (2014), 15–22.
35. Zhang, Y., Yang, Y., Tang, K., Hu, X., Zou, G., Physicochemical characterization and antioxidant activity of quercetin-loaded chitosan nanoparticles. Journal of Applied Polymer Science 107 (2008), 891–897.
36. Zhou, H., Sun, X., Zhang, L., Zhang, P., Li, J., Liu, Y.N., Fabrication of biopolymeric complex coacervation core micelles for efficient tea polyphenol delivery via a green process. Langmuir 28:41 (2012), 14553–14561.
37. Zimet, P., Livney, Y.D., Beta-lactoglobulin and its nanocomplexes with pectin as vehicles for ω-3 polyunsaturated fatty acids. Food Hydrocolloids 23:4 (2009), 1120–1126.