Antioxidative capacity and binding affinity of the complex of green tea catechin and beta-lactoglobulin glycated by the Maillard reaction

Food Chemistry

Volumn 232, Issue , 2017, Pages 744-752

  Perusko, Marija ^a   Al Hanish, Ayah ^b   Mihailovic, Jelena ^b   Minic, Simeon ^b   Trifunovic, Sara ^b   Prodic, Ivana ^b   Cirkovic Velickovic, Tanja ^b,c,d  

^a Innovation Center   (Serbia)

^b UNIVERSITY OF BELGRADE   (Serbia)

^c GHENT UNIVERSITY   (Belgium)

^d and Centre for Advanced Process Technology for Urban Resource Recovery   (South Korea)

Author keywords

Beta lactoglobulin; Epigallocatechin 3 gallate; Glycation; Maillard reaction; Protein polyphenol interactions; Tea

Indexed keywords

BINDING ENERGY; CHEMICAL REACTIONS; FLAVONOIDS; GLYCOSYLATION; ORGANIC COMPOUNDS; OXYGEN; PHENOLS; PROTEINS;

BETA-LACTOGLOBULIN; EPIGALLOCATECHIN-3-GALLATE; GLYCATION; MAILLARD REACTION; PROTEIN-POLYPHENOL INTERACTIONS;

BINS;

BETA LACTOGLOBULIN; CATECHIN; SUPEROXIDE; ANTIOXIDANT; LACTOGLOBULIN; POLYPHENOL; TEA;

ANTIOXIDANT ACTIVITY; ARTICLE; BINDING AFFINITY; CIRCULAR DICHROISM; COMPLEX FORMATION; CONFORMATIONAL TRANSITION; GLYCATION; INFRARED SPECTROSCOPY; TEA; ANIMAL; BOVINE; FEMALE; MILK;

ANIMALS; ANTIOXIDANTS; CATECHIN; CATTLE; FEMALE; LACTOGLOBULINS; MAILLARD REACTION; MILK; POLYPHENOLS; TEA;

EID: 85017657241     PISSN: 03088146     EISSN: 18737072     Source Type: Journal    
DOI: 10.1016/j.foodchem.2017.04.074     Document Type: Article

References (40)

1. Al-Hanish, A., Stanic-Vucinic, D., Mihailovic, J., Prodic, I., Minic, S., Stojadinovic, M., et al. Noncovalent interactions of bovine α-lactalbumin with green tea polyphenol, epigalocatechin-3-gallate. Food Hydrocolloids 61 (2016), 241–250.
2. Butt, M.S., Sultan, M.T., Green tea: Nature's defense against malignancies. Critical Reviews in Food Science and Nutrition 49:5 (2009), 463–473.
3. Chaudhuri, S., Chakraborty, S., Sengupta, P.K., Probing the interactions of hemoglobin with antioxidant flavonoids via fluorescence spectroscopy and molecular modeling studies. Biophysical Chemistry 154:1 (2011), 26–34.
4. Chevalier, F., Chobert, J.M., Genot, C., Haertle, T., Scavenging of free radicals, antimicrobial, and cytotoxic activities of the Maillard reaction products of β-lactoglobulin glycated with several sugars. Journal of Agricultural and Food Chemistry 49 (2001), 5031–5038.
5. Chobert, J.M., Gaudin, J.C., Dalgalarrondo, M., Haertle, T., Impact of Maillard type glycation on properties of beta-lactoglobulin. Biotechnology Advances 24:6 (2006), 629–632.
6. Dong, A., Huang, P., Caughey, W.S., Protein secondary structures in water from second-derivative amide I infrared spectra. Biochemistry 29:13 (1990), 3303–3308.
7. Faridbod, F., Ganjali, M.R., Larijani, B., Riahi, S., Saboury, A.A., Hosseini, M., et al. Interaction study of pioglitazone with albumin by fluorescence spectroscopy and molecular docking. Spectrochimica Acta A Molecular and Biomolecular Spectroscopy 78:1 (2011), 96–101.
8. Fenaille, F., Morgan, F., Parisod, V., Tabet, J.C., Guy, P.A., Solid-state glycation of β-lactoglobulin by lactose and galactose: Localization of the modified amino acids using mass spectrometric techniques. Journal of Mass Spectrometry 39 (2004), 16–28.
9. Goormaghtigh, E., Cabiaux, V., Ruysschaert, J.M., Secondary structure and dosage of soluble and membrane proteins by attenuated total reflection Fourier-transform infrared spectroscopy on hydrated films. European Journal of Biochemistry 193:2 (1990), 409–420.
10. Hasni, I., Bourassa, P., Hamdani, S., Samson, G., Carpentier, R., Tajmir-Riahi, H.A., Interaction of milk alpha- and beta-caseins with tea polyphenols. Food Chemistry 126:2 (2011), 630–639.
11. Jia, J., Gao, X., Hao, M., Tang, L., Comparison of binding interaction between β-lactoglobulin and three common polyphenols using multi-spectroscopy and modeling methods. Food Chemistry 228 (2017), 143–151.
12. Johansson, J.S., Binding of the volatile anesthetic chloroform to albumin demonstrated using tryptophan fluorescence quenching. Journal of Biological Chemistry 272:29 (1997), 17961–17965.
13. Kanakis, C.D., Hasni, I., Bourassa, P., Tarantilis, P.A., Polissiou, M.G., Tajmir-Riahi, H.A., Milk beta-lactoglobulin complexes with tea polyphenols. Food Chemistry 127:3 (2011), 1046–1055.
14. Keppler, J.K., Martin, D., Garamus, V.M., Schwarz, K., Differences in binding behavior of (−)-epigallocatechin gallate to beta-lactoglobulin heterodimers (AB) compared to homodimers (A) and (B). Journal of Molecular Recognition 28:11 (2015), 656–666.
15. Keppler, J.K., Sonnichsen, F.D., Lorenzen, P.C., Schwarz, K., Differences in heat stability and ligand binding among beta-lactoglobulin genetic variants A, B and C using (1)H NMR and fluorescence quenching. Biochimica Biophysica Acta 1844:6 (2014), 1083–1093.
16. Keppler, J.K., Stuhldreier, M.C., Temps, F., Schwarz, K., Influence of mathematical models and correction factors on binding results of polyphenols and retinol with β-lactoglobulin measured with fluorescence quenching. Food Biophysics 9:2 (2014), 158–168.
17. Lakowicz, J.R., Gryczynski, I., Gryczynski, Z., Dattelbaum, J.D., Anisotropy-based sensing with reference fluorophores. Analytical Biochemistry 267:2 (1999), 397–405.
18. Lestringant, P., Guri, A., Gulseren, I., Relkin, P., Corredig, M., Effect of processing on physicochemical characteristics and bioefficacy of beta-lactoglobulin-epigallocatechin-3-gallate complexes. Journal of Agricultural and Food Chemistry 62:33 (2014), 8357–8364.
19. Li, B., Du, W., Jin, J., Du, Q., Preservation of (−)-epigallocatechin-3-gallate antioxidant properties loaded in heat treated beta-lactoglobulin nanoparticles. Journal of Agricultural and Food Chemistry 60:13 (2012), 3477–3484.
20. Liang, L., Subirade, M., Study of the acid and thermal stability of β-lactoglobulin–ligand complexes using fluorescence quenching. Food Chemistry 132:4 (2012), 2023–2029.
21. Liang, L., Tajmir-Riahi, H.A., Subirade, M., Interaction of beta-lactoglobulin with resveratrol and its biological implications. Biomacromolecules 9:1 (2008), 50–56.
22. Liu, H.C., Chen, W.L., Mao, S.J.T., Antioxidant nature of bovine milk beta-lactoglobulin. Journal of Dairy Science 90:2 (2007), 547–555.
23. Ma, J., Yin, Y.M., Liu, H.L., Xie, M.X., Interactions of flavonoids with biomacromolecules. Current Organic Chemistry 15:15 (2011), 2627–2640.
24. Nishikimi, M., Rao, N.A., Yagi, K., The occurrence of superoxide anion in the reaction of reduced phenazine methosulfate and molecular oxygen. Biochemical and Biophysical Research Communications 46 (1972), 849–854.
25. Ognjenovic, J., Stojadinovic, M., Milcic, M., Apostolovic, D., Vesic, J., Stambolic, I., et al. Interactions of epigallo-catechin 3-gallate and ovalbumin, the major allergen of egg white. Food Chemistry 164 (2014), 36–43.
26. Ozdal, T., Capanoglu, E., Altay, F., A review on protein–phenolic interactions and associated changes. Food Research International 51:2 (2013), 954–970.
27. Perusko, M., Al-Hanish, A., Cirkovic Velickovic, T., Stanic-Vucinic, D., Macromolecular crowding conditions enhance glycation and oxidation of whey proteins in ultrasound-induced Maillard reaction. Food Chemistry 177 (2015), 248–257.
28. Sakulnarmrat, K., Srzednicki, G., Konczak, I., Composition and inhibitory activities towards digestive enzymes of polyphenolic-rich fractions of Davidson's plum and quandong. Lwt-Food Science and Technology 57:1 (2014), 366–375.
29. Seo, J.A., Hedoux, A., Guinet, Y., Paccou, L., Affouard, F., Lerbret, A., et al. Thermal denaturation of beta-lactoglobulin and stabilization mechanism by trehalose analyzed from Raman spectroscopy investigations. Journal of Physical Chemistry B 114:19 (2010), 6675–6684.
30. Shpigelman, A., Cohen, Y., Livney, Y.D., Thermally-induced beta-lactoglobulin-EGCG nanovehicles: Loading, stability, sensory and digestive-release study. Food Hydrocolloids 29:1 (2012), 57–67.
31. Shpigelman, A., Israeli, G., Livney, Y.D., Thermally-induced protein-polyphenol co-assemblies: Beta lactoglobulin-based nanocomplexes as protective nanovehicles for EGCG. Food Hydrocolloids 24:8 (2010), 735–743.
32. Soares, S., Mateus, N., Freitas, V., Interaction of different polyphenols with bovine serum albumin (BSA) and human salivary alpha-amylase (HSA) by fluorescence quenching. Journal of Agricultural and Food Chemistry 55:16 (2007), 6726–6735.
33. Stanic-Vucinic, D., Prodic, I., Apostolovic, D., Nikolic, M., Cirkovic Velickovic, T., Structure and antioxidant activity of beta-lactoglobulin-glycoconjugates obtained by high-intensity-ultrasound-induced Maillard reaction in aqueous model systems under neutral conditions. Food Chemistry 138:1 (2013), 590–599.
34. Stojadinovic, M., Burazer, L., Ercili-Cura, D., Sancho, A., Buchert, J., Cirkovic Velickovic, T., et al. One-step method for isolation and purification of native β-lactoglobulin from bovine whey. Journal of the Science of Food and Agriculture 92:7 (2012), 1432–1440.
35. Stojadinovic, M., Radosavljevic, J., Ognjenovic, J., Vesic, J., Prodic, I., Stanic-Vucinic, D., et al. Binding affinity between dietary polyphenols and beta-lactoglobulin negatively correlates with the protein susceptibility to digestion and total antioxidant activity of complexes formed. Food Chemistry 136:3–4 (2013), 1263–1271.
36. Vesic, J., Stambolic, I., Apostolovic, D., Milcic, M., Stanic-Vucinic, D., Cirkovic Velickovic, T., Complexes of green tea polyphenol, epigalocatechin-3-gallate, and 2S albumins of peanut. Food Chemistry 185 (2015), 309–317.
37. Wu, X., Dey, R., Wu, H.U.I., Liu, Z., He, Q., Zeng, X., Studies on the interaction of -epigallocatechin-3-gallate from green tea with bovine β-lactoglobulin by spectroscopic methods and docking. International Journal of Dairy Technology 66:1 (2013), 7–13.
38. Xiao, J.B., Kai, G.Y., Yang, F., Liu, C.X., Xu, X.C., Yamamoto, K., Molecular structure-affinity relationship of natural polyphenols for bovine gamma-globulin. Molecular Nutrition & Food Research 55 (2011), S86–S92.
39. Yang, C.S., Wang, X., Lu, G., Picinich, S.C., Cancer prevention by tea: Animal studies, molecular mechanisms and human relevance. Nature Reviews Cancer 9:6 (2009), 429–439.
40. Zorilla, R., Liang, L., Remondetto, G., Subirade, M., Interaction of epigallocatechin-3-gallate with β-lactoglobulin: Molecular characterization and biological implication. Dairy Science & Technology 91:5 (2011), 629–644.