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Volumn 29, Issue 1, 2012, Pages 57-67

Thermally-induced β-lactoglobulin-EGCG nanovehicles: Loading, stability, sensory and digestive-release study

Author keywords

( ) Epigallocatechin 3 gallate (EGCG); Delivery; Green tea; Nutraceutical; Simulated gastric digestion; lactoglobulin ( Lg)

Indexed keywords


EID: 84857766775     PISSN: 0268005X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.foodhyd.2012.01.016     Document Type: Article
Times cited : (182)

References (68)
  • 1
    • 34547800192 scopus 로고    scopus 로고
    • Freeze-drying of nanoparticles: formulation, process and storage considerations
    • Abdelwahed W., Degobert G., Stainmesse S., Fessi H. Freeze-drying of nanoparticles: formulation, process and storage considerations. Advanced Drug Delivery Reviews 2006, 58(15):1688-1713.
    • (2006) Advanced Drug Delivery Reviews , vol.58 , Issue.15 , pp. 1688-1713
    • Abdelwahed, W.1    Degobert, G.2    Stainmesse, S.3    Fessi, H.4
  • 2
    • 85170487701 scopus 로고
    • ASTM D 4187-82 zeta potential of colloids in water and waste water
    • ASTM, American Society for Testing and Materials
    • ASTM ASTM D 4187-82 zeta potential of colloids in water and waste water. The annual book of ASTM standards 1985, American Society for Testing and Materials.
    • (1985) The annual book of ASTM standards
  • 3
    • 0029764078 scopus 로고    scopus 로고
    • Stability of food allergens to digestion in vitro
    • Astwood J.D., Leach J.N., Fuchs R.L. Stability of food allergens to digestion in vitro. Nature Biotechnology 1996, 14(10):1269-1273.
    • (1996) Nature Biotechnology , vol.14 , Issue.10 , pp. 1269-1273
    • Astwood, J.D.1    Leach, J.N.2    Fuchs, R.L.3
  • 7
    • 77953170193 scopus 로고    scopus 로고
    • Novel technology for the preparation of self-assembled catechin/gelatin nanoparticles and their characterization
    • Chen Y.C., Yu S.H., Tsai G.J., Tang D.W., Mi F.L., Peng Y.P. Novel technology for the preparation of self-assembled catechin/gelatin nanoparticles and their characterization. Journal of Agricultural and Food Chemistry 2010, 58(11):6728-6734.
    • (2010) Journal of Agricultural and Food Chemistry , vol.58 , Issue.11 , pp. 6728-6734
    • Chen, Y.C.1    Yu, S.H.2    Tsai, G.J.3    Tang, D.W.4    Mi, F.L.5    Peng, Y.P.6
  • 8
    • 79959561463 scopus 로고    scopus 로고
    • Tea and cardiovascular disease
    • Deka A., Vita J.A. Tea and cardiovascular disease. Pharmacological Research 2011, 64(2):136-145.
    • (2011) Pharmacological Research , vol.64 , Issue.2 , pp. 136-145
    • Deka, A.1    Vita, J.A.2
  • 10
    • 77951665844 scopus 로고    scopus 로고
    • Effective use of reducing agents and nanoparticle encapsulation in stabilizing catechins in alkaline solution
    • Dube A., Ng K., Nicolazzo J.A., Larson I. Effective use of reducing agents and nanoparticle encapsulation in stabilizing catechins in alkaline solution. Food Chemistry 2010, 122(3):662-667.
    • (2010) Food Chemistry , vol.122 , Issue.3 , pp. 662-667
    • Dube, A.1    Ng, K.2    Nicolazzo, J.A.3    Larson, I.4
  • 12
    • 38649127868 scopus 로고    scopus 로고
    • Spectrophotometric studies on the interaction between (-)-epigallocatechin gallate and lysozyme
    • Ghosh K.S., Sahoo B.K., Dasgupta S. Spectrophotometric studies on the interaction between (-)-epigallocatechin gallate and lysozyme. Chemical Physics Letters 2008, 452(1-3):193-197.
    • (2008) Chemical Physics Letters , vol.452 , Issue.1-3 , pp. 193-197
    • Ghosh, K.S.1    Sahoo, B.K.2    Dasgupta, S.3
  • 13
    • 80054991836 scopus 로고    scopus 로고
    • Dietary phytochemicals and their potential effects on obesity: A review
    • González-Castejón M., Rodriguez-Casado A. Dietary phytochemicals and their potential effects on obesity: A review. Pharmacological Research 2011, 64(5):438-455.
    • (2011) Pharmacological Research , vol.64 , Issue.5 , pp. 438-455
    • González-Castejón, M.1    Rodriguez-Casado, A.2
  • 14
    • 0037126101 scopus 로고    scopus 로고
    • Novel amyloid fibrillar networks derived from a globular protein: β-lactoglobulin†
    • Gosal W.S., Clark A.H., Pudney P.D.A., Ross-Murphy S.B. Novel amyloid fibrillar networks derived from a globular protein: β-lactoglobulin†. Langmuir 2002, 18(19):7174-7181.
    • (2002) Langmuir , vol.18 , Issue.19 , pp. 7174-7181
    • Gosal, W.S.1    Clark, A.H.2    Pudney, P.D.A.3    Ross-Murphy, S.B.4
  • 15
    • 0029398314 scopus 로고
    • Susceptibility of [beta]-lactoglobulin and sodium caseinate to proteolysis by pepsin and trypsin
    • Guo M.R., Fox P.F., Flynn A., Kindstedt P.S. Susceptibility of [beta]-lactoglobulin and sodium caseinate to proteolysis by pepsin and trypsin. Journal of Dairy Science 1995, 78(11):2336-2344.
    • (1995) Journal of Dairy Science , vol.78 , Issue.11 , pp. 2336-2344
    • Guo, M.R.1    Fox, P.F.2    Flynn, A.3    Kindstedt, P.S.4
  • 16
    • 23944492427 scopus 로고    scopus 로고
    • Reduction of catechin astringency by the complexation of gallate-type catechins with pectin
    • Hayashi N., Ujihara T., Kohata K. Reduction of catechin astringency by the complexation of gallate-type catechins with pectin. Bioscience, Biotechnology, and Biochemistry 2005, 69(7):1306-1310.
    • (2005) Bioscience, Biotechnology, and Biochemistry , vol.69 , Issue.7 , pp. 1306-1310
    • Hayashi, N.1    Ujihara, T.2    Kohata, K.3
  • 17
    • 33748773870 scopus 로고    scopus 로고
    • Effects of tea polyphenols on the activities of [alpha]-amylase, pepsin, trypsin and lipase
    • He Q., Lv Y., Yao K. Effects of tea polyphenols on the activities of [alpha]-amylase, pepsin, trypsin and lipase. Food Chemistry 2007, 101(3):1178-1182.
    • (2007) Food Chemistry , vol.101 , Issue.3 , pp. 1178-1182
    • He, Q.1    Lv, Y.2    Yao, K.3
  • 18
    • 80054996443 scopus 로고    scopus 로고
    • Emerging role of bioflavonoids in gastroenterology: especially their effects on intestinal neoplasia
    • Hoensch H.P., Oertel R. Emerging role of bioflavonoids in gastroenterology: especially their effects on intestinal neoplasia. World Journal of Gastrointestinal Oncology 2011, 3(5):71-74.
    • (2011) World Journal of Gastrointestinal Oncology , vol.3 , Issue.5 , pp. 71-74
    • Hoensch, H.P.1    Oertel, R.2
  • 19
    • 0037115556 scopus 로고    scopus 로고
    • Stability, cellular uptake, biotransformation, and efflux of tea polyphenol (-)-epigallocatechin-3-gallate in HT-29 human colon adenocarcinoma cells
    • Hong J., Lu H., Meng X., Ryu J.-H., Hara Y., Yang C.S. Stability, cellular uptake, biotransformation, and efflux of tea polyphenol (-)-epigallocatechin-3-gallate in HT-29 human colon adenocarcinoma cells. Cancer Research 2002, 62(24):7241-7246.
    • (2002) Cancer Research , vol.62 , Issue.24 , pp. 7241-7246
    • Hong, J.1    Lu, H.2    Meng, X.3    Ryu, J.-H.4    Hara, Y.5    Yang, C.S.6
  • 20
    • 0036124772 scopus 로고    scopus 로고
    • Proteolysis of bovine β-lactoglobulin during thermal treatment in subdenaturing conditions highlights some structural features of the temperature-modified protein and yields fragments with low immunoreactivity
    • Iametti S., Rasmussen P., Frøkiær H., Ferranti P., Addeo F., Bonomi F. Proteolysis of bovine β-lactoglobulin during thermal treatment in subdenaturing conditions highlights some structural features of the temperature-modified protein and yields fragments with low immunoreactivity. European Journal of Biochemistry 2002, 269(5):1362-1372.
    • (2002) European Journal of Biochemistry , vol.269 , Issue.5 , pp. 1362-1372
    • Iametti, S.1    Rasmussen, P.2    Frøkiær, H.3    Ferranti, P.4    Addeo, F.5    Bonomi, F.6
  • 21
    • 78951472957 scopus 로고    scopus 로고
    • Human serum albumin as an antioxidant in the oxidation of (-)-epigallocatechin gallate: participation of reversible covalent binding for interaction and stabilization
    • Ishii T., T I. Human serum albumin as an antioxidant in the oxidation of (-)-epigallocatechin gallate: participation of reversible covalent binding for interaction and stabilization. Bioscience, Biotechnology, and Biochemistry 2011, 75(1):100-106.
    • (2011) Bioscience, Biotechnology, and Biochemistry , vol.75 , Issue.1 , pp. 100-106
    • Ishii, T.1    T, I.2
  • 22
    • 77955607600 scopus 로고    scopus 로고
    • Self-assembled [beta]-lactoglobulin-conjugated linoleic acid complex for colon cancer-targeted substance
    • Jiang H.R., Liu N. Self-assembled [beta]-lactoglobulin-conjugated linoleic acid complex for colon cancer-targeted substance. Journal of Dairy Science 2010, 93(9):3931-3939.
    • (2010) Journal of Dairy Science , vol.93 , Issue.9 , pp. 3931-3939
    • Jiang, H.R.1    Liu, N.2
  • 23
    • 84860365540 scopus 로고    scopus 로고
    • Preparation and physicochemical characterization of trans-resveratrol nanoparticles by temperature-controlled antisolvent precipitation
    • Kim S., Ng W.K., Dong Y., Das S., Tan R.B.H. Preparation and physicochemical characterization of trans-resveratrol nanoparticles by temperature-controlled antisolvent precipitation. Journal of Food Engineering 2012, 108:37-42.
    • (2012) Journal of Food Engineering , vol.108 , pp. 37-42
    • Kim, S.1    Ng, W.K.2    Dong, Y.3    Das, S.4    Tan, R.B.H.5
  • 24
    • 0000420114 scopus 로고    scopus 로고
    • Digestibility of bovine milk whey protein and β-lactoglobulin in vitro and in vivo
    • Kitabatake N., Kinekawa Y.-I. Digestibility of bovine milk whey protein and β-lactoglobulin in vitro and in vivo. Journal of Agricultural and Food Chemistry 1998, 46(12):4917-4923.
    • (1998) Journal of Agricultural and Food Chemistry , vol.46 , Issue.12 , pp. 4917-4923
    • Kitabatake, N.1    Kinekawa, Y.-I.2
  • 25
    • 4243120936 scopus 로고    scopus 로고
    • Invited review: beta-lactoglobulin: binding properties, structure, and function
    • Kontopidis G., Holt C., Sawyer L. Invited review: beta-lactoglobulin: binding properties, structure, and function. Journal of Dairy Science 2004, 87(4):785-796.
    • (2004) Journal of Dairy Science , vol.87 , Issue.4 , pp. 785-796
    • Kontopidis, G.1    Holt, C.2    Sawyer, L.3
  • 26
    • 0036212584 scopus 로고    scopus 로고
    • Antioxidant activity of black tea vs. green tea
    • author reply 786
    • Lee K.W., Lee H.J., Lee C.Y. Antioxidant activity of black tea vs. green tea. The Journal of Nutrition 2002, 132(4):785. author reply 786.
    • (2002) The Journal of Nutrition , vol.132 , Issue.4 , pp. 785
    • Lee, K.W.1    Lee, H.J.2    Lee, C.Y.3
  • 27
    • 0034829797 scopus 로고    scopus 로고
    • Rapid method for the discrimination of red wine cultivars based on mid-infrared spectroscopy of phenolic wine extracts
    • Lendl B., Edelmann A., Diewok J., Schuster K.C. Rapid method for the discrimination of red wine cultivars based on mid-infrared spectroscopy of phenolic wine extracts. Journal of Agricultural and Food Chemistry 2001, 49(3):1139-1145.
    • (2001) Journal of Agricultural and Food Chemistry , vol.49 , Issue.3 , pp. 1139-1145
    • Lendl, B.1    Edelmann, A.2    Diewok, J.3    Schuster, K.C.4
  • 28
    • 79955008104 scopus 로고    scopus 로고
    • Fabrication of nanoparticles using partially purified pomegranate ellagitannins and gelatin and their apoptotic effects
    • Li Z., Percival S.S., Bonard S., Gu L. Fabrication of nanoparticles using partially purified pomegranate ellagitannins and gelatin and their apoptotic effects. Molecular Nutrition & Food Research 2011, 55(7):1096-1103.
    • (2011) Molecular Nutrition & Food Research , vol.55 , Issue.7 , pp. 1096-1103
    • Li, Z.1    Percival, S.S.2    Bonard, S.3    Gu, L.4
  • 29
    • 67649939005 scopus 로고    scopus 로고
    • Emulsification alters simulated gastrointestinal proteolysis of [small beta]-casein and [small beta]-lactoglobulin
    • Macierzanka A., Sancho A.I., Mills E.N.C., Rigby N.M., Mackie A.R. Emulsification alters simulated gastrointestinal proteolysis of [small beta]-casein and [small beta]-lactoglobulin. Soft Matter 2009, 5(3):538-550.
    • (2009) Soft Matter , vol.5 , Issue.3 , pp. 538-550
    • Macierzanka, A.1    Sancho, A.I.2    Mills, E.N.C.3    Rigby, N.M.4    Mackie, A.R.5
  • 31
    • 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 2006, 64(2):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
  • 32
    • 77956910989 scopus 로고    scopus 로고
    • In vitro gastric digestion of interfacial protein structures: visualisation by AFM
    • Maldonado-Valderrama J., Gunning A.P., Wilde P.J., Morris V.J. In vitro gastric digestion of interfacial protein structures: visualisation by AFM. Soft Matter 2010, 6(19):4908-4915.
    • (2010) Soft Matter , vol.6 , Issue.19 , pp. 4908-4915
    • Maldonado-Valderrama, J.1    Gunning, A.P.2    Wilde, P.J.3    Morris, V.J.4
  • 33
    • 70350622059 scopus 로고    scopus 로고
    • In vitro digestibility of [beta]-casein and [beta]-lactoglobulin under simulated human gastric and duodenal conditions: a multi-laboratory evaluation
    • Mandalari G., Adel-Patient K., Barkholt V., Baro C., Bennett L., Bublin M., et al. In vitro digestibility of [beta]-casein and [beta]-lactoglobulin under simulated human gastric and duodenal conditions: a multi-laboratory evaluation. Regulatory Toxicology and Pharmacology 2009, 55(3):372-381.
    • (2009) Regulatory Toxicology and Pharmacology , vol.55 , Issue.3 , pp. 372-381
    • Mandalari, G.1    Adel-Patient, K.2    Barkholt, V.3    Baro, C.4    Bennett, L.5    Bublin, M.6
  • 34
    • 79960722781 scopus 로고    scopus 로고
    • Understanding the broad-spectrum neuroprotective action profile of green tea polyphenols in aging and neurodegenerative diseases
    • Mandel S.A., Amit T., Weinreb O., Youdim M.B. Understanding the broad-spectrum neuroprotective action profile of green tea polyphenols in aging and neurodegenerative diseases. Journal of Alzheimer's Disease: JAD 2011, 25(2):187-208.
    • (2011) Journal of Alzheimer's Disease: JAD , vol.25 , Issue.2 , pp. 187-208
    • Mandel, S.A.1    Amit, T.2    Weinreb, O.3    Youdim, M.B.4
  • 36
    • 29744451337 scopus 로고    scopus 로고
    • Phospholipid interactions protect the milk allergen α-lactalbumin from proteolysis during in vitro digestion
    • Moreno F.J., Mackie A.R., Mills E.N.C. Phospholipid interactions protect the milk allergen α-lactalbumin from proteolysis during in vitro digestion. Journal of Agricultural and Food Chemistry 2005, 53(25):9810-9816.
    • (2005) Journal of Agricultural and Food Chemistry , vol.53 , Issue.25 , pp. 9810-9816
    • Moreno, F.J.1    Mackie, A.R.2    Mills, E.N.C.3
  • 37
    • 78650667117 scopus 로고    scopus 로고
    • Covalent binding of tea catechins to protein thiols: the relationship between stability and electrophilic reactivity
    • Mori T., Ishii T., Akagawa M., Nakamura Y., Nakayama T. Covalent binding of tea catechins to protein thiols: the relationship between stability and electrophilic reactivity. Bioscience, Biotechnology, and Biochemistry 2010, 74(12):2451-2456.
    • (2010) Bioscience, Biotechnology, and Biochemistry , vol.74 , Issue.12 , pp. 2451-2456
    • Mori, T.1    Ishii, T.2    Akagawa, M.3    Nakamura, Y.4    Nakayama, T.5
  • 39
    • 79951959143 scopus 로고    scopus 로고
    • Evaluation of the bitterness of green tea catechins by a cell-based assay with the human bitter taste receptor hTAS2R39
    • Narukawa M., Noga C., Ueno Y., Sato T., Misaka T., Watanabe T. Evaluation of the bitterness of green tea catechins by a cell-based assay with the human bitter taste receptor hTAS2R39. Biochemical and Biophysical Research Communications 2011, 405(4):620-625.
    • (2011) Biochemical and Biophysical Research Communications , vol.405 , Issue.4 , pp. 620-625
    • Narukawa, M.1    Noga, C.2    Ueno, Y.3    Sato, T.4    Misaka, T.5    Watanabe, T.6
  • 40
  • 41
    • 77954713265 scopus 로고    scopus 로고
    • Optimized sample preparation of endoscopic collected pancreatic fluid for SDS-PAGE analysis
    • Paulo J.A., Lee L.S., Wu B., Repas K., Banks P.A., Conwell D.L., et al. Optimized sample preparation of endoscopic collected pancreatic fluid for SDS-PAGE analysis. Electrophoresis 2010, 31(14):2377-2387.
    • (2010) Electrophoresis , vol.31 , Issue.14 , pp. 2377-2387
    • Paulo, J.A.1    Lee, L.S.2    Wu, B.3    Repas, K.4    Banks, P.A.5    Conwell, D.L.6
  • 44
    • 0013806544 scopus 로고
    • PH stability and activity curves of pepsin with special reference to their clinical importance
    • Piper D.W., Fenton B.H. pH stability and activity curves of pepsin with special reference to their clinical importance. Gut 1965, 6(5).
    • (1965) Gut , vol.6 , Issue.5
    • Piper, D.W.1    Fenton, B.H.2
  • 45
    • 0030993642 scopus 로고    scopus 로고
    • Effect of temperature on the secondary structure of beta-lactoglobulin at pH 6.7, as determined by CD and IR spectroscopy: a test of the molten globule hypothesis
    • Qi X.L., Holt C., McNulty D., Clarke D.T., Brownlow S., Jones G.R. Effect of temperature on the secondary structure of beta-lactoglobulin at pH 6.7, as determined by CD and IR spectroscopy: a test of the molten globule hypothesis. Biochemical Journal 1997, 324(Pt 1):341-346.
    • (1997) Biochemical Journal , vol.324 , Issue.PART 1 , pp. 341-346
    • Qi, X.L.1    Holt, C.2    McNulty, D.3    Clarke, D.T.4    Brownlow, S.5    Jones, G.R.6
  • 46
    • 0000443256 scopus 로고
    • Structural and conformational basis of the resistance of beta-lactoglobulin to peptic and chymotryptic digestion
    • Reddy I.M., Kella N.K.D., Kinsella J.E. Structural and conformational basis of the resistance of beta-lactoglobulin to peptic and chymotryptic digestion. Journal of Agricultural and Food Chemistry 1988, 36(4):737-741.
    • (1988) Journal of Agricultural and Food Chemistry , vol.36 , Issue.4 , pp. 737-741
    • Reddy, I.M.1    Kella, N.K.D.2    Kinsella, J.E.3
  • 47
    • 77955511339 scopus 로고    scopus 로고
    • Beta-lactoglobulin-polysaccharide complexes as nanovehicles for hydrophobic nutraceuticals in non-fat foods and clear beverages
    • Ron N., Zimet P., Bargarum J., Livney Y.D. Beta-lactoglobulin-polysaccharide complexes as nanovehicles for hydrophobic nutraceuticals in non-fat foods and clear beverages. International Dairy Journal 2010, 20(10):686-693.
    • (2010) International Dairy Journal , vol.20 , Issue.10 , pp. 686-693
    • Ron, N.1    Zimet, P.2    Bargarum, J.3    Livney, Y.D.4
  • 49
    • 0023472472 scopus 로고
    • Tricine sodium dodecyl-sulfate polyacrylamide-gel electrophoresis for the separation of proteins in the range from 1-Kda to 100-Kda
    • Schagger H., Vonjagow G. Tricine sodium dodecyl-sulfate polyacrylamide-gel electrophoresis for the separation of proteins in the range from 1-Kda to 100-Kda. Analytical Biochemistry 1987, 166(2):368-379.
    • (1987) Analytical Biochemistry , vol.166 , Issue.2 , pp. 368-379
    • Schagger, H.1    Vonjagow, G.2
  • 51
    • 33750631721 scopus 로고    scopus 로고
    • Bioavailability and stability issues in understanding the cancer preventive effects of tea polyphenols
    • Shengmin Sang J.D.L., Yang C.S. Bioavailability and stability issues in understanding the cancer preventive effects of tea polyphenols. Journal of the Science of Food and Agriculture 2006, 86(14):2256-2265.
    • (2006) Journal of the Science of Food and Agriculture , vol.86 , Issue.14 , pp. 2256-2265
    • Shengmin Sang, J.D.L.1    Yang, C.S.2
  • 52
    • 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 2010, 24(8):735-743.
    • (2010) Food Hydrocolloids , vol.24 , Issue.8 , pp. 735-743
    • Shpigelman, A.1    Israeli, G.2    Livney, Y.D.3
  • 53
    • 80555123045 scopus 로고    scopus 로고
    • Green tea catechin, epigallocatechin-3-gallate (EGCG): Mechanisms, perspectives and clinical applications
    • Singh B.N., Shankar S., Srivastava R.K. Green tea catechin, epigallocatechin-3-gallate (EGCG): Mechanisms, perspectives and clinical applications. Biochemical Pharmacology 2011, 82(12):1807-1821.
    • (2011) Biochemical Pharmacology , vol.82 , Issue.12 , pp. 1807-1821
    • Singh, B.N.1    Shankar, S.2    Srivastava, R.K.3
  • 54
    • 84874347269 scopus 로고    scopus 로고
    • Application of FT-IR and Raman spectroscopy for the study of biopolymers in breads fortified with fibre and polyphenols. Food Research International, in press, Corrected Proof.
    • Sivam, A. S., Sun-Waterhouse, D., Perera, C. O., & Waterhouse, G. I. N. Application of FT-IR and Raman spectroscopy for the study of biopolymers in breads fortified with fibre and polyphenols. Food Research International, in press, Corrected Proof. http://dx.doi.org/10.1016/j.foodres.2011.03.039.
    • Sivam, A.S.1    Sun-Waterhouse, D.2    Perera, C.O.3    Waterhouse, G.I.N.4
  • 55
    • 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 Chemistry 2003, 83(2):189-195.
    • (2003) Food Chemistry , vol.83 , Issue.2 , pp. 189-195
    • Su, Y.L.1    Leung, L.K.2    Huang, Y.3    Chen, Z.Y.4
  • 56
    • 69449089722 scopus 로고    scopus 로고
    • Green tea consumption and mortality among Japanese elderly people: the prospective Shizuoka elderly cohort
    • Suzuki E., Yorifuji T., Takao S., Komatsu H., Sugiyama M., Ohta T., et al. Green tea consumption and mortality among Japanese elderly people: the prospective Shizuoka elderly cohort. Annals of Epidemiology 2009, 19(10):732-739.
    • (2009) Annals of Epidemiology , vol.19 , Issue.10 , pp. 732-739
    • Suzuki, E.1    Yorifuji, T.2    Takao, S.3    Komatsu, H.4    Sugiyama, M.5    Ohta, T.6
  • 57
    • 27744603235 scopus 로고    scopus 로고
    • Effect of some phenolic compounds and beverages on pepsin activity during simulated gastric digestion
    • 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 2005, 53(22):8706-8713.
    • (2005) Journal of Agricultural and Food Chemistry , vol.53 , Issue.22 , pp. 8706-8713
    • Tagliazucchi, D.1    Verzelloni, E.2    Conte, A.3
  • 58
    • 1542497819 scopus 로고    scopus 로고
    • Comparative study of in vitro digestibility of food proteins and effect of preheating on the digestion
    • Teshima R., Takagi K., Okunuki H., Sawada J. Comparative study of in vitro digestibility of food proteins and effect of preheating on the digestion. Biological & Pharmaceutical Bulletin 2003, 26(7):969-973.
    • (2003) Biological & Pharmaceutical Bulletin , vol.26 , Issue.7 , pp. 969-973
    • Teshima, R.1    Takagi, K.2    Okunuki, H.3    Sawada, J.4
  • 59
    • 0031160714 scopus 로고    scopus 로고
    • Binding of vitamin D and cholesterol to beta-lactoglobulin
    • Wang Q.W., Allen J.C., Swaisgood H.E. Binding of vitamin D and cholesterol to beta-lactoglobulin. Journal of Dairy Science 1997, 80(6):1054-1059.
    • (1997) Journal of Dairy Science , vol.80 , Issue.6 , pp. 1054-1059
    • Wang, Q.W.1    Allen, J.C.2    Swaisgood, H.E.3
  • 61
    • 43649093408 scopus 로고    scopus 로고
    • Reaction kinetics of degradation and epimerization of epigallocatechin gallate (EGCG) in aqueous system over a wide temperature range
    • Wang R., Zhou W.B., Jiang X.H. Reaction kinetics of degradation and epimerization of epigallocatechin gallate (EGCG) in aqueous system over a wide temperature range. Journal of Agricultural and Food Chemistry 2008, 56(8):2694-2701.
    • (2008) Journal of Agricultural and Food Chemistry , vol.56 , Issue.8 , pp. 2694-2701
    • Wang, R.1    Zhou, W.B.2    Jiang, X.H.3
  • 62
    • 80052793160 scopus 로고    scopus 로고
    • Analysis of binding interaction between (-)-epigallocatechin (EGC) and β-lactoglobulin by multi-spectroscopic method
    • 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 2011, 82(1):164-168.
    • (2011) Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy , vol.82 , Issue.1 , pp. 164-168
    • Wu, X.1    Wu, H.2    Liu, M.3    Liu, Z.4    Xu, H.5    Lai, F.6
  • 64
    • 79960983106 scopus 로고    scopus 로고
    • Molecular property-affinity relationship of the interaction between dietary polyphenols and bovine milk proteins
    • Xu C.J., Chen X.Q. Molecular property-affinity relationship of the interaction between dietary polyphenols and bovine milk proteins. Food & Function 2011, 2(7):368-372.
    • (2011) Food & Function , vol.2 , Issue.7 , pp. 368-372
    • Xu, C.J.1    Chen, X.Q.2
  • 66
    • 79959560121 scopus 로고    scopus 로고
    • Tea and cancer prevention: epidemiological studies
    • Yuan J.-M., Sun C., Butler L.M. Tea and cancer prevention: epidemiological studies. Pharmacological Research 2011, 64(2):123-135.
    • (2011) Pharmacological Research , vol.64 , Issue.2 , pp. 123-135
    • Yuan, J.-M.1    Sun, C.2    Butler, L.M.3
  • 67
    • 0032700342 scopus 로고    scopus 로고
    • Degradation kinetics of (-)-epigallocatechin gallate as a function of pH and dissolved oxygen in a liquid model system
    • Zimeri J., Tong C.H. Degradation kinetics of (-)-epigallocatechin gallate as a function of pH and dissolved oxygen in a liquid model system. Journal of Food Science 1999, 64(5):753-758.
    • (1999) Journal of Food Science , vol.64 , Issue.5 , pp. 753-758
    • Zimeri, J.1    Tong, C.H.2
  • 68
    • 57749091590 scopus 로고    scopus 로고
    • Beta-lactoglobulin and its nanocomplexes with pectin as vehicles for omega-3 polyunsaturated fatty acids
    • Zimet P., Livney Y.D. Beta-lactoglobulin and its nanocomplexes with pectin as vehicles for omega-3 polyunsaturated fatty acids. Food Hydrocolloids 2009, 23(4):1120-1126.
    • (2009) Food Hydrocolloids , vol.23 , Issue.4 , pp. 1120-1126
    • Zimet, P.1    Livney, Y.D.2


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