Reducing the allergenic capacity of β-lactoglobulin by covalent conjugation with dietary polyphenols

Food Chemistry

Volumn 256, Issue , 2018, Pages 427-434

  Wu, Xuli ^a   Lu, Yuqin ^a   Xu, Haoxie ^a   Lin, Dongxu ^a   He, Zhendan ^a   Wu, Haiqiang ^a   Liu, Lizhong ^a   Wang, Zimei ^a  

^a Shenzhen University   (China)

Author keywords

Allergenicity; Antioxidant activity; Conjugation; Polyphenol; lactoglobulin

Indexed keywords

ALLERGENS; ANTIOXIDANTS; CIRCULAR DICHROISM SPECTROSCOPY; DICHROISM; ELECTROPHORESIS; FLUORESCENCE SPECTROSCOPY; PROTEINS;

ALLERGENICITY; ANTI-OXIDANT ACTIVITIES; CONJUGATION; LACTOGLOBULIN; POLYPHENOLS;

FOURIER TRANSFORM INFRARED SPECTROSCOPY;

ASCORBIC ACID; BETA LACTOGLOBULIN; CHLOROGENIC ACID; DIMER; EPIGALLOCATECHIN GALLATE; HISTIDINE; IMMUNOGLOBULIN E; METHIONINE; MONOMER; PROLINE; RETINOL; THIOL GROUP; TROLOX C; TRYPTOPHAN; TYROSINE; ALLERGEN; CATECHIN; LACTOGLOBULIN; POLYPHENOL;

ABTS RADICAL SCAVENGING ASSAY; ALLERGENICITY; ALPHA HELIX; AMINO ACID SEQUENCE; ANTIOXIDANT ACTIVITY; ARTICLE; BETA SHEET; BETA TURN; BINDING AFFINITY; CHILD; CIRCULAR DICHROISM; CLINICAL ARTICLE; COMPARATIVE EFFECTIVENESS; CONJUGATE; CONTROLLED STUDY; COVALENT BOND; DIFFERENTIAL SCANNING CALORIMETRY; DPPH RADICAL SCAVENGING ASSAY; DRUG CONJUGATION; DRUG EFFICACY; ENZYME LINKED IMMUNOSORBENT ASSAY; FLUORESCENCE SPECTROSCOPY; FOOD ALLERGY; HUMAN; IN VITRO STUDY; INFRARED SPECTROSCOPY; MATRIX ASSISTED LASER DESORPTION IONIZATION TIME OF FLIGHT MASS SPECTROMETRY; MOLECULAR WEIGHT; NONHUMAN; POLYACRYLAMIDE GEL ELECTROPHORESIS; PROTEIN ANALYSIS; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE; PROTEIN TERTIARY STRUCTURE; QUANTITATIVE ANALYSIS; STRUCTURE ANALYSIS; THERMOSTABILITY; WESTERN BLOTTING; ANALOGS AND DERIVATIVES; ANIMAL; BOVINE; CHEMISTRY; IMMUNOLOGY; SPECTROFLUOROMETRY;

ALLERGENS; ANIMALS; CATECHIN; CATTLE; CHLOROGENIC ACID; CIRCULAR DICHROISM; ELECTROPHORESIS, POLYACRYLAMIDE GEL; LACTOGLOBULINS; POLYPHENOLS; SPECTROMETRY, FLUORESCENCE;

EID: 85043311674     PISSN: 03088146     EISSN: 18737072     Source Type: Journal    
DOI: 10.1016/j.foodchem.2018.02.158     Document Type: Article

References (48)

1. Abd El-Maksoud, A.A., Abd El-Ghany, I.H., El-Beltagi, H.S., Anankanbil, S., Banerjee, C., Petersen, S.V., Guo, Z., Adding functionality to milk-based protein: Preparation, and physico-chemical characterization of β-lactoglobulin-phenolic conjugates. Food Chemistry 241 (2018), 281–289.
2. Ali, M., Homann, T., Khalil, M., Kruse, H., Rawel, H., Milk whey protein modification by coffee-specific phenolics: Effect on structural and functional properties. Journal of Agricultural and Food Chemistry 61 (2013), 6911–6920.
3. Besler, M., Steinhart, H., Paschke, A., Stability of food allergens and allergenicity of processed foods. Journal of Chromatography B: Biomedical Sciences and Applications 756 (2001), 207–228.
4. Cao, Y., Xiong, Y.L., Chlorogenic acid-mediated gel formation of oxidatively stressed myofibrillar protein. Food Chemistry 180 (2015), 235–243.
5. Chen, Y., Tu, Z., Wang, H., Zhang, L., Sha, X., Pang, J., Yang, P., Liu, G., Yang, W., Glycation of β-lactoglobulin under dynamic high pressure microfluidization treatment: Effects on IgE-binding capacity and conformation. Food Research International 89 (2016), 882–888.
6. Chung, S., Champagne, E.T., Reducing the allergenic capacity of peanut extracts and liquid peanut butter by phenolic compounds. Food Chemistry 115 (2009), 1345–1349.
7. Flower, D.R., The lipocalin protein family: Structure and function. Biochemical Journal 318:Pt 1 (1996), 1–14.
8. Gholami, S., Bordbar, A., Exploring binding properties of naringenin with bovine β-lactoglobulin: A fluorescence, molecular docking and molecular dynamics simulation study. Biophysical Chemistry 187–188 (2014), 33–42.
9. Gong, Y., Hou, Z., Gao, Y., Xue, Y., Liu, X., Liu, G., Optimization of extraction parameters of bioactive components from defatted marigold (Tagetes erecta L.) residue using response surface methodology. Food and Bioproducts Processing 90 (2012), 9–16.
10. Guo, Y., Harris, P., Kaur, A., Pastrana, L., Jauregi, P., Characterisation of β-lactoglobulin nanoparticles and their binding to caffeine. Food Hydrocolloids 71 (2017), 85–93.
11. Hattori, M., Okada, Y., Takahashi, K., Functional changes in β-Lactoglobulin upon conjugation with carboxymethyl cyclodextrin. Journal of Agricultural and Food Chemistry 48 (2000), 3789–3794.
12. Heino, S., Michael, B.D., Resolution-enhanced Fourier transform infrared spectroscopy of enzymes. Methods in Enzymology 130 (1896), 290–311.
13. Huang, X., Tu, Z., Xiao, H., Wang, H., Zhang, L., Hu, Y., Niu, P., Characteristics and antioxidant activities of ovalbumin glycated with different saccharides under heat moisture treatment. Food Research International 48 (2012), 866–872.
14. 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.
15. Kanakis, C.D., Hasni, I., Bourassa, P., Tarantilis, P.A., Polissiou, M.G., Tajmir-Riahi, H., Milk β-lactoglobulin complexes with tea polyphenols. Food Chemistry 127 (2011), 1046–1055.
16. Kilmartin, P.A., Hsu, C.F., Characterisation of polyphenols in green, oolong, and black teas, and in coffee, using cyclic voltammetry. Food Chemistry 82 (2003), 501–512.
17. Kleber, N., Krause, I., Illgner, S., Hinrichs, J.R., The antigenic response of β-lactoglobulin is modulated by thermally induced aggregation. European Food Research and Technology 219 (2004), 105–110.
18. Kobayashi, K., Hirano, A., Ohta, A., Yoshida, T., Takahashi, K., Hattori, M., Reduced immunogenicity of β-lactoglobulin by conjugation with carboxymethyl dextran differing in molecular weight. Journal of Agricultural and Food Chemistry 49 (2001), 823–831.
19. Kontopidis, G., Holt, C., Sawyer, L., Invited review: Beta-lactoglobulin: Binding properties, structure, and function. Journal of Dairy Science 87 (2004), 785–796.
20. Kroll, J., Rawel, H.M., Rohn, S., Reactions of plant phenolics with food proteins and enzymes under special consideration of covalent bonds. Foodence and Technology Research 9 (2003), 205–218.
21. Li, X., Yuan, S., He, S., Gao, J., Chen, H., Identification and characterization of the antigenic site (epitope) on bovine β-lactoglobulin: Common residues in linear and conformational epitopes. Journal of the Science of Food and Agriculture 95 (2015), 2916–2923.
22. Liu, F., Ma, C., Gao, Y., McClements, D.J., Food-grade covalent complexes and their application as nutraceutical delivery systems: A review. Comprehensive Reviews in Food Science and Food Safety 16 (2017), 76–95.
23. Liu, F., Ma, C., McClements, D.J., Gao, Y., A comparative study of covalent and non-covalent interactions between zein and polyphenols in ethanol-water solution. Food Hydrocolloids 63 (2017), 625–634.
24. Liu, F., Sun, C., Yang, W., Yuan, F., Gao, Y., Structural characterization and functional evaluation of lactoferrin-polyphenol conjugates formed by free-radical graft. Royal Society of Chemistry Advances 5:20 (2015), 15641–15651.
25. Meng, X., Bai, Y., Gao, J., Li, X., Chen, H., Effects of high hydrostatic pressure on the structure and potential allergenicity of the major allergen bovine β-lactoglobulin. Food Chemistry 219 (2017), 290–296.
26. Ognjenović, J., Stojadinović, M., Milčić, M., Apostolović, D., Vesić, J., Stambolić, I., Velickovic, T.C., Interactions of epigallo-catechin 3-gallate and ovalbumin, the major allergen of egg white. Food Chemistry 164 (2014), 36–43.
27. Ozdal, T., Capanoglu, E., Altay, F., A review on protein–phenolic interactions and associated changes. Food Research International 51 (2013), 954–970.
28. Perez, M.D., Calvo, M., Interaction of beta-lactoglobulin with retinol and fatty acids and its role as a possible biological function for this protein: A review. Journal of Dairy Science 78 (1995), 978–988.
29. Prigent, S.V., Voragen, A.G., Visser, A.J., van Koningsveld, G.A., Gruppen, H., Covalent interactions between proteins and oxidation products of caffeoylquinic acid (chlorogenic acid). Journal of the Science of Food and Agriculture 873 (2007), 2502–2510.
30. Rawel, H.M., Rohn, S., Kruse, H.P., Kroll, J., Structural changes induced in bovine serum albumin by covalent attachment of chlorogenic acid. Food Chemistry 78 (2002), 443–455.
31. Rohn, S., Possibilities and limitations in the analysis of covalent interactions between phenolic compounds and proteins. Food Research International 65 (2014), 13–19.
32. Sélo, I., Clément, G., Bernard, H., Chatel, J., Créminon, C., Peltre, G., Wal, J., Allergy to bovine b-lactoglobulin: Specificity of human IgE to tryptic peptides. Clinical and Experimental Allergy: Journal of the British Society for Allergy and Clinical Immunology 29 (1999), 1055–1063.
33. Shek, L.P.C., Bardina, L., Castro, R., Sampson, H.A., Beyer, K., Humoral and cellular responses to cow milk proteins in patients with milk-induced IgE-mediated and non-IgE-mediated disorders. Allergy 60 (2005), 912–919.
34. Singh, B.N., Shankar, S., Srivastava, R.K., Green tea catechin, epigallocatechin-3-gallate (EGCG): Mechanisms, perspectives and clinical applications. Biochemical Pharmacology 82 (2011), 1807–1821.
35. Tajik, N., Tajik, M., Mack, I., Enck, P., The potential effects of chlorogenic acid, the main phenolic components in coffee, on health: A comprehensive review of the literature. European Journal of Nutrition 56 (2017), 2215–2244.
36. Uk, L., Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970), 680–685.
37. Verhoeckx, K.C.M., Vissers, Y.M., Baumert, J.L., Faludi, R., Feys, M., Flanagan, S., Kimber, I., Food processing and allergenicity. Food and Chemical Toxicology 80 (2015), 223–240.
38. Wu, X., Dey, R., Wu, H., 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 (2013), 7–13.
39. Wu, X., Liu, M., Xia, L., Wu, H., Liu, Z., Xu, X., Conjugation of functional oligosaccharides reduced in vitro allergenicity of β-lactoglobulin. Food and Agricultural Immunology 24 (2013), 379–391.
40. Wu, X., Wu, H., Liu, M., Liu, Z., Xu, H., Lai, F., Analysis of binding interaction between (−)-epigallocatechin (EGC) and β-lactoglobulin by multi-spectroscopic method. Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy 82 (2011), 164–168.
41. Yang, W., Tu, Z., Wang, H., Zhang, L., Xu, S., Niu, C., Kaltashov, I., Mechanism of reduction in IgG and IgE binding of β-lactoglobulin induced by ultrasound pretreatment combined with dry-state glycation: A study using conventional spectrometry and high-resolution mass spectrometry. Journal of Agriculture and Food Chemistry 65 (2017), 8018–8027.
42. Yin, C., Yang, L., Zhao, H., Li, C., Improvement of antioxidant activity of egg white protein by phosphorylation and conjugation of epigallocatechin gallate. Food Research International 64 (2014), 855–863.
43. You, J., Luo, Y., Wu, J., Conjugation of ovotransferrin with catechin shows improved antioxidant activity. Journal of Agricultural and Food Chemistry 62 (2014), 2581–2587.
44. Zhang, M., Zheng, J., Ge, K., Zhang, H., Fang, B., Jiang, L., Ren, F.Z., Glycation of alpha-lactalbumin with different size saccharides: Effect on protein structure and antigenicity. International Dairy Journal 34 (2014), 220–228.
45. Zhong, J., Cai, X., Liu, C., Liu, W., Xu, Y., Luo, S., Purification and conformational changes of bovine PEGylated β-lactoglobulin related to antigenicity. Food Chemistry 199 (2016), 387–392.
46. Zhong, J., Tu, Y., Liu, W., Luo, S., Liu, C., Comparative study on the effects of nystose and fructofuranosyl nystose in the glycation reaction on the antigenicity and conformation of β-lactoglobulin. Food Chemistry 188 (2015), 658–663.
47. Zhong, J., Tu, Y., Liu, W., Xu, Y., Liu, C., Dun, R., Antigenicity and conformational changes of β-lactoglobulin by dynamic high pressure microfluidization combining with glycation treatment. Journal of Dairy Science 97 (2014), 4695–4702.
48. Zhong, J., Xu, Y., Liu, W., Liu, C., Luo, S., Tu, Z., Antigenicity and functional properties of β-lactoglobulin conjugated with fructo-oligosaccharides in relation to conformational changes. Journal of Dairy Science 96 (2013), 2808–2815.