Complexation of thermally-denatured soybean protein isolate with anthocyanins and its effect on the protein structure and in vitro digestibility

Food Research International

Volumn 106, Issue , 2018, Pages 619-625

  Zhang, Yan ^a   Chen, Si ^a   Qi, Baokun ^a,b   Sui, Xiaonan ^a,b   Jiang, Lianzhou ^a,b  

^a NORTHEAST AGRICULTURAL UNIVERSITY   (China)

^b National Research Center of Soybean Engineering and Technology   (China)

Author keywords

Anthocyanin rich black rice extracts; Protein digestibility; Protein secondary structure; Simulated in vitro digestion; Soybean protein isolate

Indexed keywords

ANTHOCYANINS; CIRCULAR DICHROISM SPECTROSCOPY; DICHROISM; FLUORESCENCE; FLUORESCENCE SPECTROSCOPY;

FOURIER TRANSFORM INFRA REDS; IN-VITRO DIGESTIONS; NUTRITIONAL QUALITIES; PROTEIN DIGESTIBILITY; PROTEIN SECONDARY STRUCTURE; SECONDARY STRUCTURES; SOYBEAN PROTEIN ISOLATES; SOYBEAN PROTEIN ISOLATES (SPI);

PROTEINS;

ANTHOCYANIN; PROTEIN BINDING; SOYBEAN PROTEIN;

ALPHA HELIX; BETA SHEET; BINDING SITE; CHEMISTRY; CIRCULAR DICHROISM; DIGESTION; FOOD HANDLING; HEAT; INFRARED SPECTROSCOPY; INTESTINAL SECRETIONS; NUTRITIONAL VALUE; PROCEDURES; PROTEIN DENATURATION; SPECTROFLUOROMETRY; STOMACH JUICE;

ANTHOCYANINS; BINDING SITES; CIRCULAR DICHROISM; DIGESTION; FOOD HANDLING; GASTRIC JUICE; HOT TEMPERATURE; INTESTINAL SECRETIONS; NUTRITIVE VALUE; PROTEIN BINDING; PROTEIN CONFORMATION, ALPHA-HELICAL; PROTEIN CONFORMATION, BETA-STRAND; PROTEIN DENATURATION; SOYBEAN PROTEINS; SPECTROMETRY, FLUORESCENCE; SPECTROSCOPY, FOURIER TRANSFORM INFRARED;

EID: 85041479689     PISSN: 09639969     EISSN: 18737145     Source Type: Journal    
DOI: 10.1016/j.foodres.2018.01.040     Document Type: Article

References (43)

1. Bhattacharjee, C., Saha, S., Biswas, A., Kundu, M., Ghosh, L., Das, K.P., Structural changes of β-lactoglobulin during thermal unfolding and refolding-an FT-IR and circular dichroism study. The Protein Journal 24 (2005), 27–35.
2. Calero, M., Gasset, M., Fourier transform infrared and circular dichroism spectroscopies for amyloid studies. Sigurdsson, E.M., (eds.) Amyloid proteins: Methods and protocols, 2005, Humana Press, Totowa, NJ.
3. Collins, B., Hoffman, J., Martinez, K., Grace, M., Lila, M.A., Cockrell, C., McIntosh, M., A polyphenol-rich fraction obtained from table grapes decreases adiposity, insulin resistance and markers of inflammation and impacts gut microbiota in high-fat-fed mice. The Journal of Nutritional Biochemistry 31 (2016), 150–165.
4. Emmambux, N.M., Taylor, J.R.N., Sorghum kafirin interaction with various phenolic compounds. Journal of the Science of Food and Agriculture 83 (2003), 402–407.
5. Faridbod, F., Ganjali, M.R., Larijani, B., Riahi, S., Saboury, A.A., Hosseini, M., Pillip, C., Interaction study of pioglitazone with albumin by fluorescence spectroscopy and molecular docking. Spectrochimica Acta Part A, Molecular and Biomolecular Spectroscopy 78 (2011), 96–101.
6. Gao, D.J., Tian, Y., Bi, S.Y., Chen, Y.H., Yu, A.M., Zhang, H.Q., Studies on the interaction of colloidal gold and serum albumins by spectral methods. Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy 62 (2005), 1203–1208.
7. Guimarães Drummond e Silva, F., Miralles, B., Hernández-Ledesma, B., Amigo, L., Iglesias, A.H., Reyes Reyes, F.G., Netto, F.M., Influence of protein–phenolic complex on the antioxidant capacity of flaxseed (linum usitatissimum L.) products. Journal of Agricultural and Food Chemistry 65 (2017), 800–809.
8. He, Z., Zhu, H., Xu, M., Zeng, M., Qin, F., Chen, J., Complexation of bovine beta-lactoglobulin with malvidin-3-O-glucoside and its effect on the stability of grape skin anthocyanin extracts. Food Chemistry 209 (2016), 234–240.
9. Hou, Z.H., Qin, P.Y., Zhang, Y., Cui, S.H., Ren, G.X., Identification of anthocyanins isolated from black rice (Oryza sativa L.) and their degradation kinetics. Food Research International 50 (2013), 691–697.
10. Jennings, A., Welch, A.A., Fairweather-Tait, S.J., Kay, C., Minihane, A.M., Chowienczyk, P., Cassidy, A., Higher anthocyanin intake is associated with lower arterial stiffness and central blood pressure in women. American Journal of Clinical Nutrition 96 (2012), 781–788.
11. Jia, J., Gao, X., Hao, M., Tang, L., Comparison of binding interaction between beta-lactoglobulin and three common polyphenols using multi-spectroscopy and modeling methods. Food Chemistry 228 (2017), 143–151.
12. Kanakis, C.D., Hasni, I., Bourassa, P., Tarantilis, P.A., Polissiou, M.G., Tajmir-Riahi, H.-A., Milk β-lactoglobulin complexes with tea polyphenols. Food Chemistry 127 (2011), 1046–1055.
13. Konczak, I., Zhang, W., Anthocyanins - more than nature's colours. Journal of Biomedicine and Biotechnology(5), 2004, 239–240.
14. Lakowicz, J.R., Principles of fluorescence spectroscopy. 3rd ed., 2006, Springer, New York.
15. Ling, W., Cheng, Q., Ma, J., Red and black rice decrease atherosclerotic plaque formation and increase antioxidant status in rabbits. The Journal of Nutrition 131 (2001), 1421–1426.
16. Ling, W., Wang, L., Ma, J., Supplementation of the black rice outer layer fraction to rabbits decreases atherosclerotic plaque formation and increases antioxidant status. The Journal of Nutrition 132 (2002), 20–26.
17. Minekus, M., Alminger, M., Alvito, P., Ballance, S., Bohn, T., Bourlieu, C., Brodkorb, A., A standardised static in vitro digestion method suitable for food-an international consensus. Food & Function 5 (2014), 1113–1124.
18. Moras, B., Rey, S., Vilarem, G., Pontalier, P.Y., Pressurized water extraction of isoflavones by experimental design from soybean flour and soybean protein isolate. Food Chemistry 214 (2017), 9–15.
19. Nanda, R.K., Sarkar, N., Banerjee, R., Probing the interaction of ellagic acid with human serum albumin: A fluorescence spectroscopic study. Journal of Photochemistry and Photobiology A: Chemistry 192 (2007), 152–158.
20. Ozdal, T., Capanoglu, E., Altay, F., A review on protein–phenolic interactions and associated changes. Food Research International 51 (2013), 954–970.
21. Pineda-Vadillo, C., Nau, F., Guerin-Dubiard, C., Jardin, J., Lechevalier, V., Sanz-Buenhombre, M., Dupont, D., The food matrix affects the anthocyanin profile of fortified egg and dairy matrices during processing and in vitro digestion. Food Chemistry 214 (2017), 486–496.
22. Pribic, R., Vanstokkum, I.H.M., Chapman, D., Haris, P.I., Bloemendal, M., Protein secondary structure from Fourier transform infrared and/or circular dichroism spectra. Analytical Biochemistry 214 (1993), 366–378.
23. Pu, H.L., Jiang, H., Chen, R.R., Wang, H.C., Studies on the interaction between vincamine and human serum albumin: A spectroscopic approach. Luminescence 29 (2014), 471–479.
24. Pursell, D.P., Introduction to general, organic, and biochemistry, 9th edition (by Frederick A. Bettelheim, William H. Brown, Mary K. Campbell, and Shawn O. Farrell) and general, organic, and biological chemistry, 5th edition (by H. Stephen Stoker). Journal of Chemical Education, 86, 2009, 1274.
25. Rahmelow, K., Hübner, W., Secondary structure determination of proteins in aqueous solution by infrared spectroscopy: A comparison of multivariate data analysis methods. Analytical Biochemistry 241 (1996), 5–13.
26. Rawel, H.A., Meidtner, K., Kroll, J., Binding of selected phenolic compounds to proteins. Journal of Agricultural and Food Chemistry 53 (2005), 4228–4235.
27. Roy, D., Dutta, S., Malty, S.S., Ghosh, S., Roy, A.S., Ghosh, K.S., Dasgupta, S., Spectroscopic and docking studies of the binding of two stereoisomeric antioxidant catechins to serum albumins. Journal of Luminescence 132 (2012), 1364–1375.
28. Shen, F., Niu, F., Li, J., Su, Y., Liu, Y., Yang, Y., Interactions between tea polyphenol and two kinds of typical egg white proteins-ovalbumin and lysozyme: Effect on the gastrointestinal digestion of both proteins in vitro. Food Research International 59 (2014), 100–107.
29. Shen, L.-L., Zhu, Q.-Q., Huang, F.-W., Xu, H., Wu, X.-L., Xiao, H.-F., Liu, Z.-G., Effect of heat treatment on structure and immunogenicity of recombinant peanut protein Ara h 2.01. LWT - Food Science and Technology 60 (2015), 964–969.
30. Sorgentini, D.A., Wagner, J.R., Aiidn, M.C., Effects of thermal treatment of soy protein isolate on the characteristics and structure-function relationship of soluble and insoluble fractions. Journal of Agricultural and Food Chemistry 43 (1995), 2471–2479.
31. Stojadinovic, M., Radosavljevic, J., Ognjenovic, J., Vesic, J., Prodic, I., Stanic-Vucinic, D., Cirkovic Velickovic, T., 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 (2013), 1263–1271.
32. Sui, X., Bi, S., Qi, B., Wang, Z., Zhang, M., Li, Y., Jiang, L., Impact of ultrasonic treatment on an emulsion system stabilized with soybean protein isolate and lecithin: Its emulsifying property and emulsion stability. Food Hydrocolloids 63 (2017), 727–734.
33. Sui, X., Dong, X., Zhou, W., Combined effect of pH and high temperature on the stability and antioxidant capacity of two anthocyanins in aqueous solution. Food Chemistry 163 (2014), 163–170.
34. Sui, X., Sun, H., Qi, B., Zhang, M., Li, Y., Jiang, L., Functional and conformational changes to soy proteins accompanying anthocyanins: Focus on covalent and non-covalent interactions. Food Chemistry 245 (2018), 871–878.
35. Tagliazucchi, D., Verzelloni, E., Conte, A., Effect of some phenolic compounds and beverages on pepsin activity during simulated gastric digestion. Journal of Agricultural and Food Chemistry 53 (2005), 8706–8713.
36. Tang, J., Luan, F., Chen, X., Binding analysis of glycyrrhetinic acid to human serum albumin: Fluorescence spectroscopy, FTIR, and molecular modeling. Bioorganic & Medicinal Chemistry 14 (2006), 3210–3217.
37. Tang, L., Zuo, H.J., Li, S., Comparison of the interaction between three anthocyanins and human serum albumins by spectroscopy. Journal of Luminescence 153 (2014), 54–63.
38. Tantoush, Z., Apostolovic, D., Kravic, B., Prodic, I., Mihajlovic, L., Stanic-Vucinic, D., Velickovic, T.C., Green tea catechins of food, supplements facilitate pepsin digestion of major food allergens, but hampers their digestion if oxidized by phenol oxidase. Journal of Functional Foods 4 (2012), 650–660.
39. Tiwari, B.K., O'Donnell, C.P., Muthukumarappan, K., Cullen, P.J., Anthocyanin and colour degradation in ozone treated blackberry juice. Innovative Food Science & Emerging Technologies 10 (2009), 70–75.
40. Tsuda, T., Dietary anthocyanin-rich plants: Biochemical basis and recent progress in health benefits studies. Molecular Nutrition & Food Research 56 (2012), 159–170.
41. Utsumi, S., Kinsella, J.E., Structure-function relationships in food proteins: Subunit interactions in heat-induced gelation of 7S, 11S, and soy isolate proteins. Journal of Agricultural and Food Chemistry 33 (1985), 297–303.
42. Venkatachalam, M., Sathe, S.K., Phaseolin in vitro pepsin digestibility: Role of acids and phenolic compounds. Journal of Agricultural and Food Chemistry 51 (2003), 3466–3472.
43. Wang, Y.Q., Zhang, H.M., Zhang, G.C., Tao, W.H., Tang, S.H., Interaction of the flavonoid hesperidin with bovine serum albumin: A fluorescence quenching study. Journal of Luminescence 126 (2007), 211–218.