메뉴 건너뛰기




Volumn 62, Issue 20, 2014, Pages 4677-4684

Fabrication of epigallocatechin-3-gallate nanocarrier based on glycosylated casein: Stability and interaction mechanism

Author keywords

casein; epigallocatechin 3 gallate; fluorescence quenching; glycosylation; Maillard reaction; nanocarrier; stability

Indexed keywords

ALKALINITY; BINDING ENERGY; CONVERGENCE OF NUMERICAL METHODS; ESTERIFICATION; GLYCOSYLATION; PROTEINS; QUENCHING; CHEMICAL REACTIONS; FLUORESCENCE;

EID: 84901246286     PISSN: 00218561     EISSN: 15205118     Source Type: Journal    
DOI: 10.1021/jf405157x     Document Type: Article
Times cited : (81)

References (44)
  • 1
    • 84862068411 scopus 로고    scopus 로고
    • The effects of green tea polyphenols on drug metabolism
    • Yang, C. S.; Pan, E. The effects of green tea polyphenols on drug metabolism Expert Opin. Drug Met. 2012, 8, 677-689
    • (2012) Expert Opin. Drug Met. , vol.8 , pp. 677-689
    • Yang, C.S.1    Pan, E.2
  • 2
    • 34447337251 scopus 로고    scopus 로고
    • Investigation of adsorption behavior of (-)-epigallocatechin gallate on bovine serum albumin surface using quartz crystal microbalance with dissipation monitoring
    • Wang, X.; Ho, C.-T.; Huang, Q. Investigation of adsorption behavior of (-)-epigallocatechin gallate on bovine serum albumin surface using quartz crystal microbalance with dissipation monitoring J. Agric. Food Chem. 2007, 55, 4987-4992
    • (2007) J. Agric. Food Chem. , vol.55 , pp. 4987-4992
    • Wang, X.1    Ho, C.-T.2    Huang, Q.3
  • 3
    • 84865144756 scopus 로고    scopus 로고
    • Green tea epigallocatechin-3-gallate (EGCG) promotes neural progenitor cell proliferation and sonic hedgehog pathway activation during adult hippocampal neurogenesis
    • Wang, Y.; Li, M.; Xu, X.; Song, M.; Tao, H.; Bai, Y. Green tea epigallocatechin-3-gallate (EGCG) promotes neural progenitor cell proliferation and sonic hedgehog pathway activation during adult hippocampal neurogenesis Mol. Nutr. Food Res. 2012, 56, 1292-1303
    • (2012) Mol. Nutr. Food Res. , vol.56 , pp. 1292-1303
    • Wang, Y.1    Li, M.2    Xu, X.3    Song, M.4    Tao, H.5    Bai, Y.6
  • 4
    • 0042622256 scopus 로고    scopus 로고
    • Stability of tea theaflavins and catechins
    • Su, Y. L.; Leung, L. K.; Huang, Y.; Chen, Z.-Y. Stability of tea theaflavins and catechins Food Chem. 2003, 83, 189-195
    • (2003) Food Chem. , vol.83 , pp. 189-195
    • Su, Y.L.1    Leung, L.K.2    Huang, Y.3    Chen, Z.-Y.4
  • 6
    • 1842831532 scopus 로고    scopus 로고
    • Effects of external factors on the interaction of tea catechins with lipid bilayers
    • Kajiya, K.; Kumazawa, S.; Nakayama, T. Effects of external factors on the interaction of tea catechins with lipid bilayers Biosci., Biotechnol., Biochem. 2002, 66, 2330-2335
    • (2002) Biosci., Biotechnol., Biochem. , vol.66 , pp. 2330-2335
    • Kajiya, K.1    Kumazawa, S.2    Nakayama, T.3
  • 7
    • 80155183160 scopus 로고    scopus 로고
    • Coating effects of tea polyphenol and rosemary extract combined with chitosan on the storage quality of large yellow croaker (Pseudosciaena crocea)
    • Li, T.; Hu, W.; Li, J.; Zhang, X.; Zhu, J.; Li, X. Coating effects of tea polyphenol and rosemary extract combined with chitosan on the storage quality of large yellow croaker (Pseudosciaena crocea) Food Control 2012, 25, 101-106
    • (2012) Food Control , vol.25 , pp. 101-106
    • Li, T.1    Hu, W.2    Li, J.3    Zhang, X.4    Zhu, J.5    Li, X.6
  • 8
    • 77955052598 scopus 로고    scopus 로고
    • Thermally-induced protein-polyphenol co-assemblies: β-lactoglobulin- based nanocomplexes as protective nanovehicles for EGCG
    • Shpigelman, A.; Israeli, G.; Livney, Y. D. Thermally-induced protein-polyphenol co-assemblies: β-lactoglobulin-based nanocomplexes as protective nanovehicles for EGCG Food Hydrocolloids 2010, 24, 735-743
    • (2010) Food Hydrocolloids , vol.24 , pp. 735-743
    • Shpigelman, A.1    Israeli, G.2    Livney, Y.D.3
  • 9
    • 0032967327 scopus 로고    scopus 로고
    • Effects of protein-polyphenol interactions on beverage haze, stabilization, and analysis
    • Siebert, K. J. Effects of protein-polyphenol interactions on beverage haze, stabilization, and analysis J. Agric. Food Chem. 1999, 47, 353-362
    • (1999) J. Agric. Food Chem. , vol.47 , pp. 353-362
    • Siebert, K.J.1
  • 10
    • 33745753267 scopus 로고    scopus 로고
    • Noncovalent cross-linking of casein by epigallocatechin gallate characterized by single molecule force microscopy
    • Jöbstl, E.; Howse, J. R.; Fairclough, J. P. A.; Williamson, M. P. Noncovalent cross-linking of casein by epigallocatechin gallate characterized by single molecule force microscopy J. Agric. Food Chem. 2006, 54, 4077-4081
    • (2006) J. Agric. Food Chem. , vol.54 , pp. 4077-4081
    • Jöbstl, E.1    Howse, J.R.2    Fairclough, J.P.A.3    Williamson, M.P.4
  • 12
    • 2542585365 scopus 로고    scopus 로고
    • Molecular model for astringency produced by polyphenol/protein interactions
    • Jöbstl, E.; O'Connell, J.; Fairclough, J. P. A.; Williamson, M. Molecular model for astringency produced by polyphenol/protein interactions Biomacromolecules 2004, 5, 942-949
    • (2004) Biomacromolecules , vol.5 , pp. 942-949
    • Jöbstl, E.1    O'Connell, J.2    Fairclough, J.P.A.3    Williamson, M.4
  • 13
    • 57049184159 scopus 로고    scopus 로고
    • Interactions between adsorbed layers of α S1 -casein with covalently bound side chains: A self-consistent field study
    • Akinshina, A.; Ettelaie, R.; Dickinson, E.; Smyth, G. Interactions between adsorbed layers of α S1 -casein with covalently bound side chains: a self-consistent field study Biomacromolecules 2008, 9, 3188-3200
    • (2008) Biomacromolecules , vol.9 , pp. 3188-3200
    • Akinshina, A.1    Ettelaie, R.2    Dickinson, E.3    Smyth, G.4
  • 14
    • 60849118125 scopus 로고    scopus 로고
    • Effects of casein, ovalbumin, and dextran on the astringency of tea polyphenols determined by quartz crystal microbalance with dissipation
    • Yan, Y.; Hu, J.; Yao, P. Effects of casein, ovalbumin, and dextran on the astringency of tea polyphenols determined by quartz crystal microbalance with dissipation Langmuir 2009, 25, 397-402
    • (2009) Langmuir , vol.25 , pp. 397-402
    • Yan, Y.1    Hu, J.2    Yao, P.3
  • 15
    • 84255176251 scopus 로고    scopus 로고
    • Chemical and antioxidant properties of casein peptide and its glucose Maillard reaction products in fish oil-in-water emulsions
    • Dong, S.; Wei, B.; Chen, B.; McClements, D. J.; Decker, E. A. Chemical and antioxidant properties of casein peptide and its glucose Maillard reaction products in fish oil-in-water emulsions J. Agric. Food Chem. 2011, 59, 13311-13317
    • (2011) J. Agric. Food Chem. , vol.59 , pp. 13311-13317
    • Dong, S.1    Wei, B.2    Chen, B.3    McClements, D.J.4    Decker, E.A.5
  • 16
    • 29844445747 scopus 로고    scopus 로고
    • Effect of Maillard-based conjugation with dextran on the functional properties of lysozyme and casein
    • Aminlari, M.; Ramezani, R.; Jadidi, F. Effect of Maillard-based conjugation with dextran on the functional properties of lysozyme and casein J. Sci. Food Agric. 2005, 85, 2617-2624
    • (2005) J. Sci. Food Agric. , vol.85 , pp. 2617-2624
    • Aminlari, M.1    Ramezani, R.2    Jadidi, F.3
  • 17
    • 84879376037 scopus 로고    scopus 로고
    • A study of controlled uptake and release of anthocyanins by oxidized starch microgels
    • Wang, Z.; Li, Y.; Chen, L.; xiulan, X.; Yuan, Q. A study of controlled uptake and release of anthocyanins by oxidized starch microgels J. Agric. Food Chem. 2013, 61, 5880-5887
    • (2013) J. Agric. Food Chem. , vol.61 , pp. 5880-5887
    • Wang, Z.1    Li, Y.2    Chen, L.3    Xiulan, X.4    Yuan, Q.5
  • 20
    • 33751500314 scopus 로고
    • New antimicrobial characteristics of lysozyme-dextran conjugate
    • Nakamura, S.; Kato, A.; Kobayashi, K. New antimicrobial characteristics of lysozyme-dextran conjugate J. Agric. Food Chem. 1991, 39, 647-650
    • (1991) J. Agric. Food Chem. , vol.39 , pp. 647-650
    • Nakamura, S.1    Kato, A.2    Kobayashi, K.3
  • 21
    • 0000651004 scopus 로고
    • Emulsion stabilization by polysaccharides and protein-polysaccharide complexes
    • In; Dekker: New York
    • Dickinson, E. Emulsion stabilization by polysaccharides and protein-polysaccharide complexes. In Food Science and Technology; Dekker: New York, 1995; p 501.
    • (1995) Food Science and Technology , pp. 501
    • Dickinson, E.1
  • 22
    • 84867527247 scopus 로고    scopus 로고
    • Fabrication of biopolymeric complex coacervation core micelles for efficient tea polyphenol delivery via a green process
    • 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 2012, 28, 14553-14561
    • (2012) Langmuir , vol.28 , pp. 14553-14561
    • Zhou, H.1    Sun, X.2    Zhang, L.3    Zhang, P.4    Li, J.5    Liu, Y.-N.6
  • 23
    • 0001244556 scopus 로고    scopus 로고
    • Interaction and stabilization of acidified casein dispersions with low and high methoxyl pectins
    • Pereyra, R.; Schmidt, K. A.; Wicker, L. Interaction and stabilization of acidified casein dispersions with low and high methoxyl pectins J. Agric. Food Chem. 1997, 45, 3448-3451
    • (1997) J. Agric. Food Chem. , vol.45 , pp. 3448-3451
    • Pereyra, R.1    Schmidt, K.A.2    Wicker, L.3
  • 24
    • 33749581222 scopus 로고    scopus 로고
    • Acacia senegal gum: Continuum of molecular species differing by their protein to sugar ratio, molecular weight, and charges
    • Renard, D.; Lavenant-Gourgeon, L.; Ralet, M.-C.; Sanchez, C. Acacia senegal gum: continuum of molecular species differing by their protein to sugar ratio, molecular weight, and charges Biomacromolecules 2006, 7, 2637-2649
    • (2006) Biomacromolecules , vol.7 , pp. 2637-2649
    • Renard, D.1    Lavenant-Gourgeon, L.2    Ralet, M.-C.3    Sanchez, C.4
  • 25
    • 84859395894 scopus 로고    scopus 로고
    • Preservation of (-)-epigallocatechin-3-gallate antioxidant properties loaded in heat treated β-lactoglobulin nanoparticles
    • Li, B.; Du, W.; Jin, J.; Du, Q. Preservation of (-)-epigallocatechin-3- gallate antioxidant properties loaded in heat treated β-lactoglobulin nanoparticles J. Agric. Food Chem. 2012, 60, 3477-3484
    • (2012) J. Agric. Food Chem. , vol.60 , pp. 3477-3484
    • Li, B.1    Du, W.2    Jin, J.3    Du, Q.4
  • 26
    • 84880356325 scopus 로고    scopus 로고
    • Dual effects of chitosan decoration on the liposomal membrane physicochemical properties as affected by chitosan concentration and molecular conformation
    • Tan, C.; Xue, J.; Eric, K.; Feng, B.; Zhang, X.; Xia, S. Dual effects of chitosan decoration on the liposomal membrane physicochemical properties as affected by chitosan concentration and molecular conformation J. Agric. Food Chem. 2013, 61, 6901-6910
    • (2013) J. Agric. Food Chem. , vol.61 , pp. 6901-6910
    • Tan, C.1    Xue, J.2    Eric, K.3    Feng, B.4    Zhang, X.5    Xia, S.6
  • 27
    • 79952994068 scopus 로고    scopus 로고
    • PEG-coated lyophilized proliposomes: Preparation, characterizations and in vitro release evaluation of vitamin e
    • Zhao, L.; Xiong, H.; Peng, H.; Wang, Q.; Han, D.; Bai, C.; Liu, Y.; Shi, S.; Deng, B. PEG-coated lyophilized proliposomes: preparation, characterizations and in vitro release evaluation of vitamin E Eur. Food Res. Technol. 2011, 232, 647-654
    • (2011) Eur. Food Res. Technol. , vol.232 , pp. 647-654
    • Zhao, L.1    Xiong, H.2    Peng, H.3    Wang, Q.4    Han, D.5    Bai, C.6    Liu, Y.7    Shi, S.8    Deng, B.9
  • 28
    • 64549121131 scopus 로고    scopus 로고
    • Preparation and pH stability of ferrous glycinate liposomes
    • Ding, B.; Xia, S.; Hayat, K.; Zhang, X. Preparation and pH stability of ferrous glycinate liposomes J. Agric. Food Chem. 2009, 57, 2938-2944
    • (2009) J. Agric. Food Chem. , vol.57 , pp. 2938-2944
    • Ding, B.1    Xia, S.2    Hayat, K.3    Zhang, X.4
  • 30
    • 80052571315 scopus 로고    scopus 로고
    • Effect of saccharide structure and size on the degree of substitution and product dispersity of α-lactalbumin glycated via the Maillard reaction
    • ter Haar, R.; Schols, H. A.; Gruppen, H. Effect of saccharide structure and size on the degree of substitution and product dispersity of α-lactalbumin glycated via the Maillard reaction J. Agric. Food Chem. 2011, 59, 9378-9385
    • (2011) J. Agric. Food Chem. , vol.59 , pp. 9378-9385
    • Ter Haar, R.1    Schols, H.A.2    Gruppen, H.3
  • 31
    • 0035134979 scopus 로고    scopus 로고
    • Caseins and casein hydrolysates. 1. Lipoxygenase inhibitory properties
    • Rival, S. G.; Fornaroli, S.; Boeriu, C. G.; Wichers, H. J. Caseins and casein hydrolysates. 1. Lipoxygenase inhibitory properties J. Agric. Food Chem. 2001, 49, 287-294
    • (2001) J. Agric. Food Chem. , vol.49 , pp. 287-294
    • Rival, S.G.1    Fornaroli, S.2    Boeriu, C.G.3    Wichers, H.J.4
  • 32
    • 0037382068 scopus 로고    scopus 로고
    • Evolution of available lysine and furosine contents in milk-based infant formulas throughout the shelf-life storage period
    • Ferrer, E.; Alegría, A.; Farré, R.; Abellán, P.; Romero, F.; Clemente, G. Evolution of available lysine and furosine contents in milk-based infant formulas throughout the shelf-life storage period J. Sci. Food Agric. 2003, 83, 465-472
    • (2003) J. Sci. Food Agric. , vol.83 , pp. 465-472
    • Ferrer, E.1    Alegría, A.2    Farré, R.3    Abellán, P.4    Romero, F.5    Clemente, G.6
  • 34
    • 34250775903 scopus 로고    scopus 로고
    • Interactions between a non glycosylated human proline-rich protein and flavan-3-ols are affected by protein concentration and polyphenol/protein ratio
    • Pascal, C.; Poncet-Legrand, C.; Imberty, A.; Gautier, C.; Sarni-Manchado, P.; Cheynier, V.; Vernhet, A. Interactions between a non glycosylated human proline-rich protein and flavan-3-ols are affected by protein concentration and polyphenol/protein ratio J. Agric. Food Chem. 2007, 55, 4895-4901
    • (2007) J. Agric. Food Chem. , vol.55 , pp. 4895-4901
    • Pascal, C.1    Poncet-Legrand, C.2    Imberty, A.3    Gautier, C.4    Sarni-Manchado, P.5    Cheynier, V.6    Vernhet, A.7
  • 35
    • 84881040549 scopus 로고    scopus 로고
    • Protonation of epigallocatechin-3-gallate (EGCG) results in massive aggregation and reduced oral bioavailability of EGCG-dispersed selenium nanoparticles
    • Wu, S.; Sun, K.; Wang, X.; Wang, D.; Wan, X.; Zhang, J. Protonation of epigallocatechin-3-gallate (EGCG) results in massive aggregation and reduced oral bioavailability of EGCG-dispersed selenium nanoparticles J. Agric. Food Chem. 2013, 61, 7268-7275
    • (2013) J. Agric. Food Chem. , vol.61 , pp. 7268-7275
    • Wu, S.1    Sun, K.2    Wang, X.3    Wang, D.4    Wan, X.5    Zhang, J.6
  • 36
    • 79959261640 scopus 로고    scopus 로고
    • Lipophilized epigallocatechin gallate (EGCG) derivatives as novel antioxidants
    • Zhong, Y.; Shahidi, F. Lipophilized epigallocatechin gallate (EGCG) derivatives as novel antioxidants J. Agric. Food Chem. 2011, 59, 6526-6533
    • (2011) J. Agric. Food Chem. , vol.59 , pp. 6526-6533
    • Zhong, Y.1    Shahidi, F.2
  • 37
    • 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. l.; Cabane, B.; Vernhet, A. Aggregation of a proline-rich protein induced by epigallocatechin gallate and condensed tannins: effect of protein glycosylation J. Agric. Food Chem. 2008, 56, 6724-6732
    • (2008) J. Agric. Food Chem. , vol.56 , pp. 6724-6732
    • Pascal, C.1    Cabane, B.2    Vernhet, A.3
  • 38
    • 69949161222 scopus 로고    scopus 로고
    • Degradation and metabolism of catechin, epigallocatechin-3-gallate (EGCG), and related compounds by the intestinal microbiota in the pig cecum model
    • van't Slot, G.; Humpf, H.-U. Degradation and metabolism of catechin, epigallocatechin-3-gallate (EGCG), and related compounds by the intestinal microbiota in the pig cecum model J. Agric. Food Chem. 2009, 57, 8041-8048
    • (2009) J. Agric. Food Chem. , vol.57 , pp. 8041-8048
    • Van'T Slot, G.1    Humpf, H.-U.2
  • 39
    • 80052541265 scopus 로고    scopus 로고
    • Stabilisation and controlled release of silibinin from pH responsive shellac colloidal particles
    • Patel, A.; Heussen, P.; Hazekamp, J.; Velikov, K. P. Stabilisation and controlled release of silibinin from pH responsive shellac colloidal particles Soft Matter 2011, 7, 8549-8555
    • (2011) Soft Matter , vol.7 , pp. 8549-8555
    • Patel, A.1    Heussen, P.2    Hazekamp, J.3    Velikov, K.P.4
  • 40
    • 80054708616 scopus 로고    scopus 로고
    • Colloidal complexes from associated water soluble cellulose derivative (methylcellulose) and green tea polyphenol (epigallocatechin gallate)
    • Patel, A. R.; Seijen-ten-Hoorn, J.; Velikov, K. P. Colloidal complexes from associated water soluble cellulose derivative (methylcellulose) and green tea polyphenol (epigallocatechin gallate) J. Colloid Interface Sci. 2011, 364, 317-323
    • (2011) J. Colloid Interface Sci. , vol.364 , pp. 317-323
    • Patel, A.R.1    Seijen-Ten-Hoorn, J.2    Velikov, K.P.3
  • 41
    • 57049145802 scopus 로고    scopus 로고
    • Bioavailability of nanoparticles in nutrient and nutraceutical delivery
    • Acosta, E. Bioavailability of nanoparticles in nutrient and nutraceutical delivery Curr. Opin. Colloid Interface Sci. 2009, 14, 3-15
    • (2009) Curr. Opin. Colloid Interface Sci. , vol.14 , pp. 3-15
    • Acosta, E.1
  • 42
    • 84873453386 scopus 로고    scopus 로고
    • Binding sites of resveratrol, genistein, and curcumin with milk α-and β-caseins
    • Bourassa, P.; Bariyanga, J.; Tajmir-Riahi, H. Binding sites of resveratrol, genistein, and curcumin with milk α-and β-caseins J. Phys. Chem. B 2013, 117, 1287-1295
    • (2013) J. Phys. Chem. B , vol.117 , pp. 1287-1295
    • Bourassa, P.1    Bariyanga, J.2    Tajmir-Riahi, H.3
  • 43
    • 0028895804 scopus 로고
    • Quenching-resolved emission anisotropy: A steady state fluorescence method to study protein dynamics
    • Lakos, Z.; Szarka, á.; Koszorús, L.; Somogyi, B. Quenching-resolved emission anisotropy: a steady state fluorescence method to study protein dynamics J. Photochem. Photobiol. B 1995, 27, 55-60
    • (1995) J. Photochem. Photobiol. B , vol.27 , pp. 55-60
    • Lakos, Z.1    Szarka, A.2    Koszorús, L.3    Somogyi, B.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.