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Volumn 62, Issue , 2014, Pages 183-192

Encapsulation of anthocyanin molecules within a ferritin nanocage increases their stability and cell uptake efficiency

Author keywords

Anthocyanin; Caco 2; Encapsulation; Ferritin; Stabilization

Indexed keywords

ENCAPSULATION; MOLECULES; PROTEINS; STABILIZATION; THERMODYNAMIC STABILITY;

EID: 84896535550     PISSN: 09639969     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.foodres.2014.02.041     Document Type: Article
Times cited : (124)

References (54)
  • 1
    • 67349100157 scopus 로고    scopus 로고
    • Ferritins: A family of molecules for iron storage, antioxidation and more
    • Arosio P., Ingrassia R., Cavadini P. Ferritins: A family of molecules for iron storage, antioxidation and more. Biochimica et Biophysica Acta 2009, 1790(7):589-599.
    • (2009) Biochimica et Biophysica Acta , vol.1790 , Issue.7 , pp. 589-599
    • Arosio, P.1    Ingrassia, R.2    Cavadini, P.3
  • 2
    • 3543081719 scopus 로고    scopus 로고
    • Anti-angiogenic, antioxidant, and anti-carcinogenic properties of a novel anthocyanin-rich berry extract formula
    • (71 p preceding 75)
    • Bagchi D., Sen C.K., Bagchi M., Atalay M. Anti-angiogenic, antioxidant, and anti-carcinogenic properties of a novel anthocyanin-rich berry extract formula. Biochemistry (Mosc) 2004, 69(1):75-80. (71 p preceding 75).
    • (2004) Biochemistry (Mosc) , vol.69 , Issue.1 , pp. 75-80
    • Bagchi, D.1    Sen, C.K.2    Bagchi, M.3    Atalay, M.4
  • 3
    • 0037409187 scopus 로고    scopus 로고
    • The effects of heating, UV irradiation, and storage on stability of the anthocyanin-polyphenol copigment complex
    • Bakowska A., Kucharska A.Z., Oszmiański J. The effects of heating, UV irradiation, and storage on stability of the anthocyanin-polyphenol copigment complex. Food Chemistry 2003, 81(3):349-355.
    • (2003) Food Chemistry , vol.81 , Issue.3 , pp. 349-355
    • Bakowska, A.1    Kucharska, A.Z.2    Oszmiański, J.3
  • 4
    • 34249021014 scopus 로고    scopus 로고
    • Gastric digestion of pea ferritin and modulation of its iron bioavailability by ascorbic and phytic acids in caco-2 cells
    • Bejjani S., Pullakhandam R., Punjal R., Nair M.K. Gastric digestion of pea ferritin and modulation of its iron bioavailability by ascorbic and phytic acids in caco-2 cells. World Journal of Gastroenterology 2007, 13(14):2083-2088.
    • (2007) World Journal of Gastroenterology , vol.13 , Issue.14 , pp. 2083-2088
    • Bejjani, S.1    Pullakhandam, R.2    Punjal, R.3    Nair, M.K.4
  • 5
    • 0033992652 scopus 로고    scopus 로고
    • Colour and stability of the six common anthocyanidin 3-glucosides in aqueous solutions
    • Cabrita L., Fossen T., Andersen Ø.M. Colour and stability of the six common anthocyanidin 3-glucosides in aqueous solutions. Food Chemistry 2000, 68(1):101-107.
    • (2000) Food Chemistry , vol.68 , Issue.1 , pp. 101-107
    • Cabrita, L.1    Fossen, T.2    Andersen, O.M.3
  • 6
    • 0033617958 scopus 로고    scopus 로고
    • Mineralization in ferritin: An efficient means of iron storage
    • Chasteen N.D., Harrison P.M. Mineralization in ferritin: An efficient means of iron storage. Journal of Structural Biology 1999, 126(3):182-194.
    • (1999) Journal of Structural Biology , vol.126 , Issue.3 , pp. 182-194
    • Chasteen, N.D.1    Harrison, P.M.2
  • 7
    • 0001065258 scopus 로고
    • Structural aspects of anthocyanin-flavonoid complex formation and its role in plant color
    • Chen L.-J., Hrazdina G. Structural aspects of anthocyanin-flavonoid complex formation and its role in plant color. Phytochemistry 1981, 20(2):297-303.
    • (1981) Phytochemistry , vol.20 , Issue.2 , pp. 297-303
    • Chen, L.-J.1    Hrazdina, G.2
  • 8
    • 0015633689 scopus 로고
    • Subunit interactions in horse spleen apoferritin. Dissociation by extremes of pH
    • Crichton R.R., Bryce C.F. Subunit interactions in horse spleen apoferritin. Dissociation by extremes of pH. Biochemical Journal 1973, 133(2):289-299.
    • (1973) Biochemical Journal , vol.133 , Issue.2 , pp. 289-299
    • Crichton, R.R.1    Bryce, C.F.2
  • 9
    • 0001723583 scopus 로고
    • Copigmentation of simple and acylated anthocyanins with colorless phenolic compounds
    • Davies A.J., Mazza G. Copigmentation of simple and acylated anthocyanins with colorless phenolic compounds. Journal of Agricultural and Food Chemistry 1993, 41(5):716-720.
    • (1993) Journal of Agricultural and Food Chemistry , vol.41 , Issue.5 , pp. 716-720
    • Davies, A.J.1    Mazza, G.2
  • 10
    • 77955818652 scopus 로고    scopus 로고
    • Applications of peptide and protein-based materials in bionanotechnology
    • de la Rica R., Matsui H. Applications of peptide and protein-based materials in bionanotechnology. Chemical Society Reviews 2010, 39(9):3499-3509.
    • (2010) Chemical Society Reviews , vol.39 , Issue.9 , pp. 3499-3509
    • de la Rica, R.1    Matsui, H.2
  • 11
    • 75249102786 scopus 로고    scopus 로고
    • Comparative study on iron release from soybean (Glycine max) seed ferritin induced by anthocyanins and ascorbate
    • Deng J., Cheng J., Liao X., Zhang T., Leng X., Zhao G. Comparative study on iron release from soybean (Glycine max) seed ferritin induced by anthocyanins and ascorbate. Journal of Agricultural and Food Chemistry 2010, 58(1):635-641.
    • (2010) Journal of Agricultural and Food Chemistry , vol.58 , Issue.1 , pp. 635-641
    • Deng, J.1    Cheng, J.2    Liao, X.3    Zhang, T.4    Leng, X.5    Zhao, G.6
  • 12
    • 77957819609 scopus 로고    scopus 로고
    • Role of H-1 and H-2 subunits of soybean seed ferritin in oxidative deposition of iron in protein
    • Deng J., Liao X., Yang H., Zhang X., Hua Z., Masuda T., et al. Role of H-1 and H-2 subunits of soybean seed ferritin in oxidative deposition of iron in protein. Journal of Biological Chemistry 2010, 285(42):32075-32086.
    • (2010) Journal of Biological Chemistry , vol.285 , Issue.42 , pp. 32075-32086
    • Deng, J.1    Liao, X.2    Yang, H.3    Zhang, X.4    Hua, Z.5    Masuda, T.6
  • 17
    • 0032439632 scopus 로고    scopus 로고
    • Colour and stability of pure anthocyanins influenced by pH including the alkaline region
    • Fossen T., Cabrita L., Andersen O.M. Colour and stability of pure anthocyanins influenced by pH including the alkaline region. Food Chemistry 1998, 63(4):435-440.
    • (1998) Food Chemistry , vol.63 , Issue.4 , pp. 435-440
    • Fossen, T.1    Cabrita, L.2    Andersen, O.M.3
  • 19
    • 77952778704 scopus 로고    scopus 로고
    • A novel EP-involved pathway for iron release from soya bean seed ferritin
    • Fu X., Deng J., Yang H., Masuda T., Goto F., Yoshihara T., et al. A novel EP-involved pathway for iron release from soya bean seed ferritin. Biochemical Journal 2010, 427(2):313-321.
    • (2010) Biochemical Journal , vol.427 , Issue.2 , pp. 313-321
    • Fu, X.1    Deng, J.2    Yang, H.3    Masuda, T.4    Goto, F.5    Yoshihara, T.6
  • 21
    • 3543022686 scopus 로고    scopus 로고
    • In vivo cancer targeting and imaging with semiconductor quantum dots
    • Gao X., Cui Y., Levenson R.M., Chung L.W., Nie S. In vivo cancer targeting and imaging with semiconductor quantum dots. Nature Biotechnology 2004, 22(8):969-976.
    • (2004) Nature Biotechnology , vol.22 , Issue.8 , pp. 969-976
    • Gao, X.1    Cui, Y.2    Levenson, R.M.3    Chung, L.W.4    Nie, S.5
  • 22
    • 0030608152 scopus 로고    scopus 로고
    • The ferritins: Molecular properties, iron storage function and cellular regulation
    • Harrison P.M., Arosio P. The ferritins: Molecular properties, iron storage function and cellular regulation. Biochimica et Biophysica Acta 1996, 1275(3):161-203.
    • (1996) Biochimica et Biophysica Acta , vol.1275 , Issue.3 , pp. 161-203
    • Harrison, P.M.1    Arosio, P.2
  • 23
    • 0014408017 scopus 로고
    • Reassembly of apoferritin molecules from subunits
    • Harrison P.M., Gregory D.W. Reassembly of apoferritin molecules from subunits. Nature 1968, 220(5167):578-580.
    • (1968) Nature , vol.220 , Issue.5167 , pp. 578-580
    • Harrison, P.M.1    Gregory, D.W.2
  • 24
    • 0024593744 scopus 로고
    • Characterization of the human colon carcinoma cell line (Caco-2) as a model system for intestinal epithelial permeability
    • Hidalgo I.J., Raub T.J., Borchardt R.T. Characterization of the human colon carcinoma cell line (Caco-2) as a model system for intestinal epithelial permeability. Gastroenterology 1989, 96(3):736-749.
    • (1989) Gastroenterology , vol.96 , Issue.3 , pp. 736-749
    • Hidalgo, I.J.1    Raub, T.J.2    Borchardt, R.T.3
  • 26
    • 61749102565 scopus 로고    scopus 로고
    • Receptor-mediated uptake of ferritin-bound iron by human intestinal Caco-2 cells
    • Kalgaonkar S., Lonnerdal B. Receptor-mediated uptake of ferritin-bound iron by human intestinal Caco-2 cells. Journal of Nutritional Biochemistry 2009, 20(4):304-311.
    • (2009) Journal of Nutritional Biochemistry , vol.20 , Issue.4 , pp. 304-311
    • Kalgaonkar, S.1    Lonnerdal, B.2
  • 27
    • 57549103949 scopus 로고    scopus 로고
    • Controlled assembly of bifunctional chimeric protein cages and composition analysis using noncovalent mass spectrometry
    • Kang S., Oltrogge L.M., Broomell C.C., Liepold L.O., Prevelige P.E., Young M., et al. Controlled assembly of bifunctional chimeric protein cages and composition analysis using noncovalent mass spectrometry. Journal of the American Chemical Society 2008, 130(49):16527-16529.
    • (2008) Journal of the American Chemical Society , vol.130 , Issue.49 , pp. 16527-16529
    • Kang, S.1    Oltrogge, L.M.2    Broomell, C.C.3    Liepold, L.O.4    Prevelige, P.E.5    Young, M.6
  • 30
    • 84872050781 scopus 로고    scopus 로고
    • Different effects of temperature on supramolecular protein and non-protein materials in hydrogen storage
    • Liao X., Zhang T., Xiao Q., Yang H., Zhao G., Leng X. Different effects of temperature on supramolecular protein and non-protein materials in hydrogen storage. International Journal of Hydrogen Energy 2013, 38(2):991-998.
    • (2013) International Journal of Hydrogen Energy , vol.38 , Issue.2 , pp. 991-998
    • Liao, X.1    Zhang, T.2    Xiao, Q.3    Yang, H.4    Zhao, G.5    Leng, X.6
  • 31
    • 15244358126 scopus 로고    scopus 로고
    • Anthocyanins and human health: An in vitro investigative approach
    • Lila M.A. Anthocyanins and human health: An in vitro investigative approach. Journal of Biomedicine and Biotechnology 2004, 2004(5):306-313.
    • (2004) Journal of Biomedicine and Biotechnology , vol.2004 , Issue.5 , pp. 306-313
    • Lila, M.A.1
  • 33
    • 33748536103 scopus 로고    scopus 로고
    • Apoferritin-templated synthesis of metal phosphate nanoparticle labels for electrochemical immunoassay
    • Liu G., Wu H., Wang J., Lin Y. Apoferritin-templated synthesis of metal phosphate nanoparticle labels for electrochemical immunoassay. Small 2006, 2(10):1139-1143.
    • (2006) Small , vol.2 , Issue.10 , pp. 1139-1143
    • Liu, G.1    Wu, H.2    Wang, J.3    Lin, Y.4
  • 34
    • 0029761744 scopus 로고    scopus 로고
    • Synthesis of inorganic materials with complex form
    • Mann S., Ozin G.A. Synthesis of inorganic materials with complex form. Nature 1996, 382(6589):313-318.
    • (1996) Nature , vol.382 , Issue.6589 , pp. 313-318
    • Mann, S.1    Ozin, G.A.2
  • 36
    • 0035379652 scopus 로고    scopus 로고
    • A novel plant ferritin subunit from soybean that is related to a mechanism in iron release
    • Masuda T., Goto F., Yoshihara T. A novel plant ferritin subunit from soybean that is related to a mechanism in iron release. Journal of Biological Chemistry 2001, 276(22):19575-19579.
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.22 , pp. 19575-19579
    • Masuda, T.1    Goto, F.2    Yoshihara, T.3
  • 37
    • 77950463631 scopus 로고    scopus 로고
    • Crystal structure of plant ferritin reveals a novel metal binding site that functions as a transit site for metal transfer in ferritin
    • Masuda T., Goto F., Yoshihara T., Mikami B. Crystal structure of plant ferritin reveals a novel metal binding site that functions as a transit site for metal transfer in ferritin. Journal of Biological Chemistry 2010, 285(6):4049-4059.
    • (2010) Journal of Biological Chemistry , vol.285 , Issue.6 , pp. 4049-4059
    • Masuda, T.1    Goto, F.2    Yoshihara, T.3    Mikami, B.4
  • 38
    • 45949123645 scopus 로고
    • Recent developments in the stabilization of anthocyanins in food products
    • Mazza G., Brouillard R. Recent developments in the stabilization of anthocyanins in food products. Food Chemistry 1987, 25(3):207-225.
    • (1987) Food Chemistry , vol.25 , Issue.3 , pp. 207-225
    • Mazza, G.1    Brouillard, R.2
  • 39
    • 0000934597 scopus 로고
    • The mechanism of co-pigmentation of anthocyanins in aqueous solutions
    • Mazza G., Brouillard R. The mechanism of co-pigmentation of anthocyanins in aqueous solutions. Phytochemistry 1990, 29(4):1097-1102.
    • (1990) Phytochemistry , vol.29 , Issue.4 , pp. 1097-1102
    • Mazza, G.1    Brouillard, R.2
  • 40
    • 84896501664 scopus 로고
    • Synthesis of inorganic nanophase materials in supramolecular protein cages
    • Meldrum F.C., Wade V.J., Nimmo D.L., Heywood B.R., Mann S. Synthesis of inorganic nanophase materials in supramolecular protein cages. Nature 1991, 39(21):4.
    • (1991) Nature , vol.39 , Issue.21 , pp. 4
    • Meldrum, F.C.1    Wade, V.J.2    Nimmo, D.L.3    Heywood, B.R.4    Mann, S.5
  • 41
    • 17944366258 scopus 로고    scopus 로고
    • Nanostructures in biodiagnostics
    • Rosi N.L., Mirkin C.A. Nanostructures in biodiagnostics. Chemical Reviews 2005, 105(4):1547-1562.
    • (2005) Chemical Reviews , vol.105 , Issue.4 , pp. 1547-1562
    • Rosi, N.L.1    Mirkin, C.A.2
  • 42
    • 0037369028 scopus 로고    scopus 로고
    • Photostabilization of phycocyanin and anthocyanin in the presence of biopterin-alpha-glucoside from Spirulina platensis under ultraviolet ray
    • Saito T., Ishikura H., Hada Y., Fukui K., Kodera Y., Matsushim A., et al. Photostabilization of phycocyanin and anthocyanin in the presence of biopterin-alpha-glucoside from Spirulina platensis under ultraviolet ray. Dyes and Pigments 2003, 56(3):203-207.
    • (2003) Dyes and Pigments , vol.56 , Issue.3 , pp. 203-207
    • Saito, T.1    Ishikura, H.2    Hada, Y.3    Fukui, K.4    Kodera, Y.5    Matsushim, A.6
  • 43
    • 41549147443 scopus 로고    scopus 로고
    • Caco-2 intestinal epithelial cells absorb soybean ferritin by mu2 (AP2)-dependent endocytosis
    • San Martin C.D., Garri C., Pizarro F., Walter T., Theil E.C., Nunez M.T. Caco-2 intestinal epithelial cells absorb soybean ferritin by mu2 (AP2)-dependent endocytosis. Journal of Nutrition 2008, 138(4):659-666.
    • (2008) Journal of Nutrition , vol.138 , Issue.4 , pp. 659-666
    • San Martin, C.D.1    Garri, C.2    Pizarro, F.3    Walter, T.4    Theil, E.C.5    Nunez, M.T.6
  • 45
    • 47849094565 scopus 로고    scopus 로고
    • Absorption of black currant anthocyanins by monolayers of human intestinal epithelial Caco-2 cells mounted in using type chambers
    • Steinert R.E., Ditscheid B., Netzel M., Jahreis G. Absorption of black currant anthocyanins by monolayers of human intestinal epithelial Caco-2 cells mounted in using type chambers. Journal of Agricultural and Food Chemistry 2008, 56(13):4995-5001.
    • (2008) Journal of Agricultural and Food Chemistry , vol.56 , Issue.13 , pp. 4995-5001
    • Steinert, R.E.1    Ditscheid, B.2    Netzel, M.3    Jahreis, G.4
  • 46
    • 74849133694 scopus 로고    scopus 로고
    • Comparative analyses of copigmentation of cyanidin 3-glucoside and cyanidin 3-sophoroside from red raspberry fruits
    • Sun J., Cao X., Bai w, Liao X., Hu X. Comparative analyses of copigmentation of cyanidin 3-glucoside and cyanidin 3-sophoroside from red raspberry fruits. Food Chemistry 2010, 120(4):1131-1137.
    • (2010) Food Chemistry , vol.120 , Issue.4 , pp. 1131-1137
    • Sun, J.1    Cao, X.2    Bai, W.3    Liao, X.4    Hu, X.5
  • 49
    • 42549160385 scopus 로고    scopus 로고
    • High-yield anthocyanin biosynthesis in engineered Escherichia coli
    • Yan Y., Li Z., Koffas M.A. High-yield anthocyanin biosynthesis in engineered Escherichia coli. Biotechnology and Bioengineering 2008, 100(1):126-140.
    • (2008) Biotechnology and Bioengineering , vol.100 , Issue.1 , pp. 126-140
    • Yan, Y.1    Li, Z.2    Koffas, M.A.3
  • 50
    • 77951833932 scopus 로고    scopus 로고
    • Cellular uptake and photodynamic activity of protein nanocages containing methylene blue photosensitizing drug
    • Yan F., Zhang Y., Kim K.S., Yuan H.K., Vo-Dinh T. Cellular uptake and photodynamic activity of protein nanocages containing methylene blue photosensitizing drug. Photochemistry and Photobiology 2010, 86(3):662-666.
    • (2010) Photochemistry and Photobiology , vol.86 , Issue.3 , pp. 662-666
    • Yan, F.1    Zhang, Y.2    Kim, K.S.3    Yuan, H.K.4    Vo-Dinh, T.5
  • 51
    • 78249282259 scopus 로고    scopus 로고
    • Protein association and dissociation regulated by extension peptide: A mode for iron control by phytoferritin in seeds
    • Yang H., Fu X., Li M., Leng X., Chen B., Zhao G. Protein association and dissociation regulated by extension peptide: A mode for iron control by phytoferritin in seeds. Plant Physiology 2010, 154(3):1481-1491.
    • (2010) Plant Physiology , vol.154 , Issue.3 , pp. 1481-1491
    • Yang, H.1    Fu, X.2    Li, M.3    Leng, X.4    Chen, B.5    Zhao, G.6
  • 53
    • 77953811022 scopus 로고    scopus 로고
    • Phytoferritin and its implications for human health and nutrition
    • Zhao G. Phytoferritin and its implications for human health and nutrition. Biochimica et Biophysica Acta 2010, 1800(8):815-823.
    • (2010) Biochimica et Biophysica Acta , vol.1800 , Issue.8 , pp. 815-823
    • Zhao, G.1


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