메뉴 건너뛰기




Volumn 75, Issue , 2018, Pages 81-87

Characteristics of the interaction mechanism between tannic acid and sodium caseinate using multispectroscopic and thermodynamics methods

Author keywords

Complexes; Isothermal titration calorimetry; Sodium caseinate; Spectroscopy; Tannic acid

Indexed keywords


EID: 85029692896     PISSN: 0268005X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.foodhyd.2017.09.010     Document Type: Article
Times cited : (97)

References (55)
  • 1
    • 78049331373 scopus 로고    scopus 로고
    • The role of intercalated water in multilayered graphene oxide
    • Acik, M., Mattevi, C., Gong, C., Lee, G., Cho, K., Chhowalla, M., et al. The role of intercalated water in multilayered graphene oxide. ACS Nano 4:10 (2010), 5861–5868.
    • (2010) ACS Nano , vol.4 , Issue.10 , pp. 5861-5868
    • Acik, M.1    Mattevi, C.2    Gong, C.3    Lee, G.4    Cho, K.5    Chhowalla, M.6
  • 2
    • 78049434111 scopus 로고    scopus 로고
    • Antioxidative activity and emulsifying properties of cuttlefish skin gelatin–tannic acid complex as influenced by types of interaction
    • Aewsiri, T., Benjakul, S., Visessanguan, W., Wierenga, P.A., Gruppen, H., Antioxidative activity and emulsifying properties of cuttlefish skin gelatin–tannic acid complex as influenced by types of interaction. Innovative Food Science & Emerging Technologies 11:4 (2010), 712–720.
    • (2010) Innovative Food Science & Emerging Technologies , vol.11 , Issue.4 , pp. 712-720
    • Aewsiri, T.1    Benjakul, S.2    Visessanguan, W.3    Wierenga, P.A.4    Gruppen, H.5
  • 4
    • 43049114128 scopus 로고    scopus 로고
    • Preparation and characterization of nanoparticles formed by chitosan–caseinate interactions
    • Anal, A.K., Tobiassen, A., Flanagan, J., Singh, H., Preparation and characterization of nanoparticles formed by chitosan–caseinate interactions. Colloids and Surfaces B: Biointerfaces 64:1 (2008), 104–110.
    • (2008) Colloids and Surfaces B: Biointerfaces , vol.64 , Issue.1 , pp. 104-110
    • Anal, A.K.1    Tobiassen, A.2    Flanagan, J.3    Singh, H.4
  • 6
    • 67349222053 scopus 로고    scopus 로고
    • Effect of oxidised tannic acid on the gel properties of mackerel (Rastrelliger kanagurta) mince and surimi prepared by different washing processes
    • Balange, A.K., Benjakul, S., Effect of oxidised tannic acid on the gel properties of mackerel (Rastrelliger kanagurta) mince and surimi prepared by different washing processes. Food Hydrocolloids 23:7 (2009), 1693–1701.
    • (2009) Food Hydrocolloids , vol.23 , Issue.7 , pp. 1693-1701
    • Balange, A.K.1    Benjakul, S.2
  • 7
    • 84864365169 scopus 로고    scopus 로고
    • Recent developments on polyphenol-protein interactions: Effects on tea and coffee taste, antioxidant properties and the digestive system
    • Bandyopadhyay, P., Ghosh, A.K., Ghosh, C., Recent developments on polyphenol-protein interactions: Effects on tea and coffee taste, antioxidant properties and the digestive system. Food Function 3:6 (2012), 592–605.
    • (2012) Food Function , vol.3 , Issue.6 , pp. 592-605
    • Bandyopadhyay, P.1    Ghosh, A.K.2    Ghosh, C.3
  • 9
    • 34047274918 scopus 로고    scopus 로고
    • Physicochemical studies on Pepsin−CTAB Interaction:  energetics and structural changes
    • Chakraborty, T., Chakraborty, I., Moulik, S.P., Ghosh, S., Physicochemical studies on Pepsin−CTAB Interaction:  energetics and structural changes. The Journal of Physical Chemistry B 111:10 (2007), 2736–2746.
    • (2007) The Journal of Physical Chemistry B , vol.111 , Issue.10 , pp. 2736-2746
    • Chakraborty, T.1    Chakraborty, I.2    Moulik, S.P.3    Ghosh, S.4
  • 10
    • 77958186125 scopus 로고    scopus 로고
    • Surface hydration: Principles and applications toward low-fouling/nonfouling biomaterials
    • Chen, S., Li, L., Zhao, C., Zheng, J., Surface hydration: Principles and applications toward low-fouling/nonfouling biomaterials. Polymer 51:23 (2010), 5283–5293.
    • (2010) Polymer , vol.51 , Issue.23 , pp. 5283-5293
    • Chen, S.1    Li, L.2    Zhao, C.3    Zheng, J.4
  • 12
    • 0348114294 scopus 로고    scopus 로고
    • Casein micelle structure, functions and interactions
    • P.F. Fox P.L.H. McSweeney Springer US Boston, MA
    • De Kruif, C.G., Holt, C., Casein micelle structure, functions and interactions. Fox, P.F., McSweeney, P.L.H., (eds.) Advanced dairy Chemistry—1 proteins: Part A/Part B, 2003, Springer US, Boston, MA, 233–276.
    • (2003) Advanced dairy Chemistry—1 proteins: Part A/Part B , pp. 233-276
    • De Kruif, C.G.1    Holt, C.2
  • 13
    • 44049105911 scopus 로고    scopus 로고
    • Dissociation from the oligomeric state is the rate-limiting step in fibril formation by kappa-casein
    • Ecroyd, H., Koudelka, T., Thorn, D.C., Williams, D.M., Devlin, G., Hoffmann, P., et al. Dissociation from the oligomeric state is the rate-limiting step in fibril formation by kappa-casein. Journal of Biological Chemistry 283:14 (2008), 9012–9022.
    • (2008) Journal of Biological Chemistry , vol.283 , Issue.14 , pp. 9012-9022
    • Ecroyd, H.1    Koudelka, T.2    Thorn, D.C.3    Williams, D.M.4    Devlin, G.5    Hoffmann, P.6
  • 14
    • 0001917250 scopus 로고    scopus 로고
    • Fluorescence Quenching: Theory and applications
    • J.R. Lakowicz Springer US Boston, MA
    • Eftink, M.R., Fluorescence Quenching: Theory and applications. Lakowicz, J.R., (eds.) Topics in fluorescence spectroscopy: Principles, 2002, Springer US, Boston, MA, 53–126.
    • (2002) Topics in fluorescence spectroscopy: Principles , pp. 53-126
    • Eftink, M.R.1
  • 15
    • 0035177887 scopus 로고    scopus 로고
    • Secondary structural studies of bovine caseins: Temperature dependence of β-casein structure as analyzed by circular dichroism and FTIR spectroscopy and correlation with micellization
    • Farrell, H.M. Jr., Wickham, E.D., Unruh, J.J., Qi, P.X., Hoagland, P.D., Secondary structural studies of bovine caseins: Temperature dependence of β-casein structure as analyzed by circular dichroism and FTIR spectroscopy and correlation with micellization. Food Hydrocolloids 15:4–6 (2001), 341–354.
    • (2001) Food Hydrocolloids , vol.15 , Issue.4-6 , pp. 341-354
    • Farrell, H.M.1    Wickham, E.D.2    Unruh, J.J.3    Qi, P.X.4    Hoagland, P.D.5
  • 17
    • 84896953829 scopus 로고    scopus 로고
    • Large pore mesoporous silica nanoparticles by templating with a nonsurfactant molecule, tannic acid
    • Gao, Z., Zharov, I., Large pore mesoporous silica nanoparticles by templating with a nonsurfactant molecule, tannic acid. Chemistry of Materials 26:6 (2014), 2030–2037.
    • (2014) Chemistry of Materials , vol.26 , Issue.6 , pp. 2030-2037
    • Gao, Z.1    Zharov, I.2
  • 18
    • 0031257271 scopus 로고    scopus 로고
    • Characterization of edible oils and lard by fourier transform infrared spectroscopy. Relationships between composition and frequency of concrete bands in the fingerprint region
    • Guillén, M.D., Cabo, N., Characterization of edible oils and lard by fourier transform infrared spectroscopy. Relationships between composition and frequency of concrete bands in the fingerprint region. Journal of the American Oil Chemists’ Society 74:10 (1997), 1281–1286.
    • (1997) Journal of the American Oil Chemists’ Society , vol.74 , Issue.10 , pp. 1281-1286
    • Guillén, M.D.1    Cabo, N.2
  • 19
    • 79955471658 scopus 로고    scopus 로고
    • Variations of both bacterial community and extracellular polymers: The inducements of increase of cell hydrophobicity from biofloc to aerobic granule sludge
    • Guo, F., Zhang, S.-H., Yu, X., Wei, B., Variations of both bacterial community and extracellular polymers: The inducements of increase of cell hydrophobicity from biofloc to aerobic granule sludge. Bioresource Technology 102:11 (2011), 6421–6428.
    • (2011) Bioresource Technology , vol.102 , Issue.11 , pp. 6421-6428
    • Guo, F.1    Zhang, S.-H.2    Yu, X.3    Wei, B.4
  • 20
    • 84947768117 scopus 로고    scopus 로고
    • Isothermal titration calorimetric and spectroscopic studies of β-lactoglobulin-water-soluble fraction of Persian gum interaction in aqueous solution
    • Hadian, M., Hosseini, S.M.H., Farahnaky, A., Mesbahi, G.R., Yousefi, G.H., Saboury, A.A., Isothermal titration calorimetric and spectroscopic studies of β-lactoglobulin-water-soluble fraction of Persian gum interaction in aqueous solution. Food Hydrocolloids 55 (2016), 108–118.
    • (2016) Food Hydrocolloids , vol.55 , pp. 108-118
    • Hadian, M.1    Hosseini, S.M.H.2    Farahnaky, A.3    Mesbahi, G.R.4    Yousefi, G.H.5    Saboury, A.A.6
  • 21
    • 84859374607 scopus 로고    scopus 로고
    • Purification of pectin from apple pomace juice by using sodium caseinate and characterisation of their binding by isothermal titration calorimetry
    • Happi Emaga, T., Garna, H., Paquot, M., Deleu, M., Purification of pectin from apple pomace juice by using sodium caseinate and characterisation of their binding by isothermal titration calorimetry. Food Hydrocolloids 29:1 (2012), 211–218.
    • (2012) Food Hydrocolloids , vol.29 , Issue.1 , pp. 211-218
    • Happi Emaga, T.1    Garna, H.2    Paquot, M.3    Deleu, M.4
  • 24
    • 84918823965 scopus 로고    scopus 로고
    • Interactions of polyphenols with carbohydrates, lipids and proteins
    • Jakobek, L., Interactions of polyphenols with carbohydrates, lipids and proteins. Food Chemistry 175 (2015), 556–567.
    • (2015) Food Chemistry , vol.175 , pp. 556-567
    • Jakobek, L.1
  • 26
    • 84950139191 scopus 로고    scopus 로고
    • Binding of an oligomeric ellagitannin series to bovine serum albumin (BSA): Analysis by isothermal titration calorimetry (ITC)
    • Karonen, M., Oraviita, M., Mueller-Harvey, I., Salminen, J.-P., Green, R.J., Binding of an oligomeric ellagitannin series to bovine serum albumin (BSA): Analysis by isothermal titration calorimetry (ITC). Journal of Agricultural and Food Chemistry 63:49 (2015), 10647–10654.
    • (2015) Journal of Agricultural and Food Chemistry , vol.63 , Issue.49 , pp. 10647-10654
    • Karonen, M.1    Oraviita, M.2    Mueller-Harvey, I.3    Salminen, J.-P.4    Green, R.J.5
  • 27
    • 85014911536 scopus 로고    scopus 로고
    • Formulation for oral delivery of lactoferrin based on bovine serum albumin and tannic acid multilayer microcapsules
    • Kilic, E., Novoselova, M.V., Lim, S.H., Pyataev, N.A., Pinyaev, S.I., Kulikov, O.A., et al. Formulation for oral delivery of lactoferrin based on bovine serum albumin and tannic acid multilayer microcapsules. Scientific Reports, 7, 2017, 44159.
    • (2017) Scientific Reports , vol.7 , pp. 44159
    • Kilic, E.1    Novoselova, M.V.2    Lim, S.H.3    Pyataev, N.A.4    Pinyaev, S.I.5    Kulikov, O.A.6
  • 28
    • 57749191253 scopus 로고    scopus 로고
    • pH-Dependent interaction between sodium caseinate and xanthan gum
    • Kobori, T., Matsumoto, A., Sugiyama, S., pH-Dependent interaction between sodium caseinate and xanthan gum. Carbohydrate Polymers 75:4 (2009), 719–723.
    • (2009) Carbohydrate Polymers , vol.75 , Issue.4 , pp. 719-723
    • Kobori, T.1    Matsumoto, A.2    Sugiyama, S.3
  • 29
    • 85020271532 scopus 로고    scopus 로고
    • Protein-tannic acid multilayer films: A multifunctional material for microencapsulation of food-derived bioactives
    • Lau, H.H., Murney, R., Yakovlev, N.L., Novoselova, M.V., Lim, S.H., Roy, N., et al. Protein-tannic acid multilayer films: A multifunctional material for microencapsulation of food-derived bioactives. Journal of Colloid and Interface Science 505 (2017), 332–340.
    • (2017) Journal of Colloid and Interface Science , vol.505 , pp. 332-340
    • Lau, H.H.1    Murney, R.2    Yakovlev, N.L.3    Novoselova, M.V.4    Lim, S.H.5    Roy, N.6
  • 30
    • 84857382394 scopus 로고    scopus 로고
    • Interactions between polyphenols and Macromolecules: Quantification methods and mechanisms
    • Le Bourvellec, C., Renard, C.M.G.C., Interactions between polyphenols and Macromolecules: Quantification methods and mechanisms. Critical Reviews in Food Science and Nutrition 52:3 (2012), 213–248.
    • (2012) Critical Reviews in Food Science and Nutrition , vol.52 , Issue.3 , pp. 213-248
    • Le Bourvellec, C.1    Renard, C.M.G.C.2
  • 31
    • 46049093569 scopus 로고    scopus 로고
    • pH-dependent structures and properties of casein micelles
    • Liu, Y., Guo, R., pH-dependent structures and properties of casein micelles. Biophysical Chemistry 136:2–3 (2008), 67–73.
    • (2008) Biophysical Chemistry , vol.136 , Issue.2-3 , pp. 67-73
    • Liu, Y.1    Guo, R.2
  • 34
    • 33745610160 scopus 로고    scopus 로고
    • Interaction of (−)-epigallocatechin-3-gallate with human serum albumin: Fluorescence, fourier transform infrared, circular dichroism, and docking studies
    • Maiti, T.K., Ghosh, K.S., Dasgupta, S., Interaction of (−)-epigallocatechin-3-gallate with human serum albumin: Fluorescence, fourier transform infrared, circular dichroism, and docking studies. Proteins: Structure, Function, and Bioinformatics 64:2 (2006), 355–362.
    • (2006) Proteins: Structure, Function, and Bioinformatics , vol.64 , Issue.2 , pp. 355-362
    • Maiti, T.K.1    Ghosh, K.S.2    Dasgupta, S.3
  • 35
    • 1542380558 scopus 로고    scopus 로고
    • Characterization of protein–polyphenol interactions
    • Papadopoulou, A., Frazier, R.A., Characterization of protein–polyphenol interactions. Trends in Food Science & Technology 15:3–4 (2004), 186–190.
    • (2004) Trends in Food Science & Technology , vol.15 , Issue.3-4 , pp. 186-190
    • Papadopoulou, A.1    Frazier, R.A.2
  • 36
    • 50449088511 scopus 로고    scopus 로고
    • Aggregation of a proline-rich protein induced by epigallocatechin gallate and condensed Tannins: Effect of protein glycosylation
    • Pascal, C., Poncet-Legrand, C., Cabane, B., Vernhet, A., Aggregation of a proline-rich protein induced by epigallocatechin gallate and condensed Tannins: Effect of protein glycosylation. Journal of Agricultural and Food Chemistry 56:15 (2008), 6724–6732.
    • (2008) Journal of Agricultural and Food Chemistry , vol.56 , Issue.15 , pp. 6724-6732
    • Pascal, C.1    Poncet-Legrand, C.2    Cabane, B.3    Vernhet, A.4
  • 37
    • 84872062912 scopus 로고    scopus 로고
    • Colloidal complexation of a macromolecule with a small molecular weight natural polyphenol: Implications in modulating polymer functionalities
    • Patel, A.R., Seijen ten-Hoorn, J., Hazekamp, J., Blijdenstein, T.B.J., Velikov, K.P., Colloidal complexation of a macromolecule with a small molecular weight natural polyphenol: Implications in modulating polymer functionalities. Soft Matter 9:5 (2013), 1428–1436.
    • (2013) Soft Matter , vol.9 , Issue.5 , pp. 1428-1436
    • Patel, A.R.1    Seijen ten-Hoorn, J.2    Hazekamp, J.3    Blijdenstein, T.B.J.4    Velikov, K.P.5
  • 39
    • 36148980862 scopus 로고    scopus 로고
    • Interactions between flavan-3-ols and poly(l-proline) studied by isothermal titration Calorimetry: Effect of the tannin structure
    • Poncet-Legrand, C., Gautier, C., Cheynier, V., Imberty, A., Interactions between flavan-3-ols and poly(l-proline) studied by isothermal titration Calorimetry: Effect of the tannin structure. Journal of Agricultural and Food Chemistry 55:22 (2007), 9235–9240.
    • (2007) Journal of Agricultural and Food Chemistry , vol.55 , Issue.22 , pp. 9235-9240
    • Poncet-Legrand, C.1    Gautier, C.2    Cheynier, V.3    Imberty, A.4
  • 43
    • 84857963147 scopus 로고    scopus 로고
    • Spectroscopic and docking studies of the binding of two stereoisomeric antioxidant catechins to serum albumins
    • Roy, D., Dutta, S., Maity, S.S., Ghosh, S., Singha Roy, A., Ghosh, K.S., et al. Spectroscopic and docking studies of the binding of two stereoisomeric antioxidant catechins to serum albumins. Journal of Luminescence 132:6 (2012), 1364–1375.
    • (2012) Journal of Luminescence , vol.132 , Issue.6 , pp. 1364-1375
    • Roy, D.1    Dutta, S.2    Maity, S.S.3    Ghosh, S.4    Singha Roy, A.5    Ghosh, K.S.6
  • 44
    • 84857140961 scopus 로고    scopus 로고
    • Kinetics and binding capacity of six soils for structurally defined hydrolyzable and condensed tannins and related phenols
    • Schmidt, M.A., Halvorson, J.J., Gonzalez, J.M., Hagerman, A.E., Kinetics and binding capacity of six soils for structurally defined hydrolyzable and condensed tannins and related phenols. Journal of Soils and Sediments 12:3 (2012), 366–375.
    • (2012) Journal of Soils and Sediments , vol.12 , Issue.3 , pp. 366-375
    • Schmidt, M.A.1    Halvorson, J.J.2    Gonzalez, J.M.3    Hagerman, A.E.4
  • 45
    • 77955052598 scopus 로고    scopus 로고
    • Thermally-induced protein–polyphenol co-assemblies: Beta lactoglobulin-based nanocomplexes as protective nanovehicles for EGCG
    • 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.
    • (2010) Food Hydrocolloids , vol.24 , Issue.8 , pp. 735-743
    • Shpigelman, A.1    Israeli, G.2    Livney, Y.D.3
  • 47
    • 34548051331 scopus 로고    scopus 로고
    • Interaction of different polyphenols with bovine serum albumin (BSA) and human salivary α-amylase (HSA) by fluorescence quenching
    • Soares, S., Mateus, N., de Freitas, V., Interaction of different polyphenols with bovine serum albumin (BSA) and human salivary α-amylase (HSA) by fluorescence quenching. Journal of Agricultural and Food Chemistry 55:16 (2007), 6726–6735.
    • (2007) Journal of Agricultural and Food Chemistry , vol.55 , Issue.16 , pp. 6726-6735
    • Soares, S.1    Mateus, N.2    de Freitas, V.3
  • 48
    • 0000003203 scopus 로고
    • Fourier transform infrared spectroscopy applied to food analysis
    • van de Voort, F.R., Fourier transform infrared spectroscopy applied to food analysis. Food Research International 25:5 (1992), 397–403.
    • (1992) Food Research International , vol.25 , Issue.5 , pp. 397-403
    • van de Voort, F.R.1
  • 50
    • 33744498149 scopus 로고    scopus 로고
    • Formation of stable nanoparticles via electrostatic complexation between sodium caseinate and gum Arabic
    • Ye, A., Flanagan, J., Singh, H., Formation of stable nanoparticles via electrostatic complexation between sodium caseinate and gum Arabic. Biopolymers 82:2 (2006), 121–133.
    • (2006) Biopolymers , vol.82 , Issue.2 , pp. 121-133
    • Ye, A.1    Flanagan, J.2    Singh, H.3
  • 51
    • 84884647287 scopus 로고    scopus 로고
    • Antioxidant and antimicrobial properties of phenolic rich fraction of Seabuckthorn (Hippophae rhamnoides L.) leaves in vitro
    • Yogendra Kumar, M.S., Tirpude, R.J., Maheshwari, D.T., Bansal, A., Misra, K., Antioxidant and antimicrobial properties of phenolic rich fraction of Seabuckthorn (Hippophae rhamnoides L.) leaves in vitro. Food Chemistry 141:4 (2013), 3443–3450.
    • (2013) Food Chemistry , vol.141 , Issue.4 , pp. 3443-3450
    • Yogendra Kumar, M.S.1    Tirpude, R.J.2    Maheshwari, D.T.3    Bansal, A.4    Misra, K.5
  • 52
    • 85014087723 scopus 로고    scopus 로고
    • Assessment of anti-cancerous potential of 6-gingerol (Tongling White Ginger) and its synergy with drugs on human cervical adenocarcinoma cells
    • (In Press)
    • Zhang, F., Zhang, J.-G., Qu, J., Zhang, Q., Prasad, C., Wei, Z.-J., Assessment of anti-cancerous potential of 6-gingerol (Tongling White Ginger) and its synergy with drugs on human cervical adenocarcinoma cells. Food and Chemical Toxicology, 2017, 10.1016/j.fct.2017.02.038 (In Press).
    • (2017) Food and Chemical Toxicology
    • Zhang, F.1    Zhang, J.-G.2    Qu, J.3    Zhang, Q.4    Prasad, C.5    Wei, Z.-J.6
  • 53
    • 85023627135 scopus 로고    scopus 로고
    • Molecular mechanism of anti-cancerous potential of Morin extracted from mulberry in Hela cells
    • (In Press)
    • Zhang, Q., Zhang, F., Thakur, K., Wang, J., Wang, H., Hu, F., et al. Molecular mechanism of anti-cancerous potential of Morin extracted from mulberry in Hela cells. Food and Chemical Toxicology, 2017, 10.1016/j.fct.2017.07.002 (In Press).
    • (2017) Food and Chemical Toxicology
    • Zhang, Q.1    Zhang, F.2    Thakur, K.3    Wang, J.4    Wang, H.5    Hu, F.6
  • 54
    • 38149063714 scopus 로고    scopus 로고
    • Fluorescence study on the interaction of bovine serum albumin with P-Aminoazobenzene
    • Zhang, Y.-Z., Zhou, B., Liu, Y.-X., Zhou, C.-X., Ding, X.-L., Liu, Y., Fluorescence study on the interaction of bovine serum albumin with P-Aminoazobenzene. Journal of Fluorescence 18:1 (2008), 109–118.
    • (2008) Journal of Fluorescence , vol.18 , Issue.1 , pp. 109-118
    • Zhang, Y.-Z.1    Zhou, B.2    Liu, Y.-X.3    Zhou, C.-X.4    Ding, X.-L.5    Liu, Y.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.