메뉴 건너뛰기




Volumn 34, Issue 7, 2018, Pages 665-697

Interactions between milk proteins and polyphenols: Binding mechanisms, related changes, and the future trends in the dairy industry

Author keywords

binding; dairy products; Milk proteins; polyphenols; protein phenol interactions

Indexed keywords

BIOACTIVITY; DAIRY PRODUCTS; PHENOLS; PROTEINS;

EID: 85052823935     PISSN: 87559129     EISSN: 15256103     Source Type: Journal    
DOI: 10.1080/87559129.2017.1377225     Document Type: Review
Times cited : (186)

References (147)
  • 1
    • 34249882770 scopus 로고    scopus 로고
    • Effects of Dietary Flavonoids on Apoptotic Pathways Related to Cancer Chemoprevention
    • Ramos, S., Effects of Dietary Flavonoids on Apoptotic Pathways Related to Cancer Chemoprevention. J. Nutr. Biochem. 2007, 18, 427–442. DOI: 10.1016/j.jnutbio.2006.11.004.
    • (2007) J. Nutr. Biochem , vol.18 , pp. 427-442
    • Ramos, S.1
  • 2
    • 84890940480 scopus 로고    scopus 로고
    • Nature and Consequences of Non-Covalent Interactions between Flavonoids and Macronutrients in Foods
    • Bordenave, N.,; Hamaker, B.R.,; Ferruzzi, M.G., Nature and Consequences of Non-Covalent Interactions between Flavonoids and Macronutrients in Foods. Food Funct. 2014, 5, 18–34. DOI: 10.1039/C3FO60263J.
    • (2014) Food Funct , vol.5 , pp. 18-34
    • Bordenave, N.1    Hamaker, B.R.2    Ferruzzi, M.G.3
  • 3
    • 84922831968 scopus 로고    scopus 로고
    • Flavonoids Protecting Food and Beverages against Light
    • Huvaere, K.,; Skibsted, L.H., Flavonoids Protecting Food and Beverages against Light. Sci. Food Agric. 2015, 95, 20–35. DOI: 10.1002/jsfa.6796.
    • (2015) Sci. Food Agric , vol.95 , pp. 20-35
    • Huvaere, K.1    Skibsted, L.H.2
  • 4
    • 84896281851 scopus 로고    scopus 로고
    • Chemistry and Biological Activities of Flavonoids: An Overview
    • 2013
    • Kumar, S.,; Pandey, A.K., Chemistry and Biological Activities of Flavonoids: An Overview. Sci. World J. 2013, 2013, 1–16.
    • (2013) Sci. World J , pp. 1-16
    • Kumar, S.1    Pandey, A.K.2
  • 5
    • 33845620279 scopus 로고    scopus 로고
    • Moderate Consumption of Cabarnet Sauvignon Attenuates Β-Amyloid Neuropathology in a Mouse Model of Alzheimer’s Disease
    • Wang, J.,; Ho, L.,; Zhao, Z.,; Seror, I.,; Humala, N.,; Dickstein, D.L.,; Thiyagarajan, M.,; Percival, S.S.,; Talcott, S.T.,; Pasinetti, G.M., Moderate Consumption of Cabarnet Sauvignon Attenuates Β-Amyloid Neuropathology in a Mouse Model of Alzheimer’s Disease. Faseb J. 2006, 20, 2313–2320. DOI: 10.1096/fj.06-6281com.
    • (2006) Faseb J , vol.20 , pp. 2313-2320
    • Wang, J.1    Ho, L.2    Zhao, Z.3    Seror, I.4    Humala, N.5    Dickstein, D.L.6    Thiyagarajan, M.7    Percival, S.S.8    Talcott, S.T.9    Pasinetti, G.M.10
  • 7
    • 0000112275 scopus 로고    scopus 로고
    • Formation of Protein−Polyphenol Haze in Beverages
    • Siebert, K.J.,; Carrasco, A.,; Lynn, P.Y., Formation of Protein−Polyphenol Haze in Beverages. J. Agric. Food Chem. 1996, 44, 1997–2005. DOI: 10.1021/jf950716r.
    • (1996) J. Agric. Food Chem , vol.44 , pp. 1997-2005
    • Siebert, K.J.1    Carrasco, A.2    Lynn, P.Y.3
  • 8
    • 84867773358 scopus 로고    scopus 로고
    • Roles of Proteins, Polysaccharides, and Phenolics in Haze Formation in White Wine via Reconstitution Experiments
    • Gazzola, D.,; Van Sluyter, S.C.,; Curioni, A.,; Waters, E.J.,; Marangon, M., Roles of Proteins, Polysaccharides, and Phenolics in Haze Formation in White Wine via Reconstitution Experiments. J. Agric. Food Chem. 2012, 60, 10666–10673. DOI: 10.1021/jf302916n.
    • (2012) J. Agric. Food Chem , vol.60 , pp. 10666-10673
    • Gazzola, D.1    Van Sluyter, S.C.2    Curioni, A.3    Waters, E.J.4    Marangon, M.5
  • 9
    • 0345313659 scopus 로고    scopus 로고
    • Β-Lactoglobulin Binds Palmitate within Its Central Cavity
    • Wu, S.Y.,; Perez, M.D.,; Puyol, P.,; Sawyer, L., Β-Lactoglobulin Binds Palmitate within Its Central Cavity. J. Biol. Chem. 1999, 274, 170–174. DOI: 10.1074/jbc.274.1.170.
    • (1999) J. Biol. Chem , vol.274 , pp. 170-174
    • Wu, S.Y.1    Perez, M.D.2    Puyol, P.3    Sawyer, L.4
  • 11
    • 27144471876 scopus 로고    scopus 로고
    • Interactions of Vitamin D3 with Bovine Β-Lactoglobulin A and Β-Casein
    • Forrest, S.A.,; Yada, R.Y.,; Rousseau, D., Interactions of Vitamin D3 with Bovine Β-Lactoglobulin A and Β-Casein. J. Agric. Food Chem. 2005, 53, 8003–8009. DOI: 10.1021/jf050661l.
    • (2005) J. Agric. Food Chem , vol.53 , pp. 8003-8009
    • Forrest, S.A.1    Yada, R.Y.2    Rousseau, D.3
  • 12
    • 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 Hydrocoll. 2009, 23, 1120–1126. DOI: 10.1016/j.foodhyd.2008.10.008.
    • (2009) Food Hydrocoll , vol.23 , pp. 1120-1126
    • Zimet, P.1    Livney, Y.D.2
  • 13
    • 38849129380 scopus 로고    scopus 로고
    • Interaction of Β-Lactoglobulin with Resveratrol and Its Biological Implications
    • Liang, L.,; Tajmir-Riahi, H.A.,; Subirade, M., Interaction of Β-Lactoglobulin with Resveratrol and Its Biological Implications. Biomacromolecules. 2008, 9, 50–56. DOI: 10.1021/bm700728k.
    • (2008) Biomacromolecules , vol.9 , pp. 50-56
    • Liang, L.1    Tajmir-Riahi, H.A.2    Subirade, M.3
  • 14
    • 75849156917 scopus 로고    scopus 로고
    • Milk Proteins as Vehicles for Bioactives
    • Livney, Y.D.,;. Milk Proteins as Vehicles for Bioactives. Curr. Opin. Colloid Interface Sci. 2010, 15, 73–83. DOI: 10.1016/j.cocis.2009.11.002.
    • (2010) Curr. Opin. Colloid Interface Sci , vol.15 , pp. 73-83
    • Livney, Y.D.1
  • 16
    • 84957963394 scopus 로고    scopus 로고
    • Mechanism Evaluation of the Interactions between Flavonoids and Bovine Serum Albumin Based on Multi- Spectroscopy, Molecular Docking and Q-TOF HR-MS Analysis
    • Fu, L.,; Sun, Y.,; Ding, L.,; Wang, Y.,; Gao, Z.,; Wu, Z.,; Wang, Z.,; Li, W.,; Bi, Y., Mechanism Evaluation of the Interactions between Flavonoids and Bovine Serum Albumin Based on Multi- Spectroscopy, Molecular Docking and Q-TOF HR-MS Analysis. Food Chem. 2016, 203, 150–157. DOI: 10.1016/j.foodchem.2016.01.105.
    • (2016) Food Chem , vol.203 , pp. 150-157
    • Fu, L.1    Sun, Y.2    Ding, L.3    Wang, Y.4    Gao, Z.5    Wu, Z.6    Wang, Z.7    Li, W.8    Bi, Y.9
  • 17
    • 84897010387 scopus 로고    scopus 로고
    • Interaction of Flavan-3-Ol Derivatives and Different Caseins Is Determined by More than Proline Content and Number of Proline Repeats
    • Bohin, M.C.,; Vincken, J.P.,; Westphal, A.H.,; Tripp, A.M.,; Dekker, P.,; Van Der Hijden, H.T.M.W.,; Gruppen, H., Interaction of Flavan-3-Ol Derivatives and Different Caseins Is Determined by More than Proline Content and Number of Proline Repeats. Food Chem. 2014, 158, 408–416. DOI: 10.1016/j.foodchem.2014.02.145.
    • (2014) Food Chem , vol.158 , pp. 408-416
    • Bohin, M.C.1    Vincken, J.P.2    Westphal, A.H.3    Tripp, A.M.4    Dekker, P.5    Van Der Hijden, H.T.M.W.6    Gruppen, H.7
  • 18
    • 0000251552 scopus 로고
    • The Evaluation of Positive and Negative Contributions to the Second Virial Coefficient of Some Milk Proteins
    • Schmidt, D.G.,; Payens, T.A.J., The Evaluation of Positive and Negative Contributions to the Second Virial Coefficient of Some Milk Proteins. J. Colloid Interface Sci. 1972, 39, 655–662. DOI: 10.1016/0021-9797(72)90073-2.
    • (1972) J. Colloid Interface Sci , vol.39 , pp. 655-662
    • Schmidt, D.G.1    Payens, T.A.J.2
  • 19
    • 33746967183 scopus 로고    scopus 로고
    • Micellization of Bovine Beta Casein Studied by Isothermal Titration Microcalorimetry and Cryogenic Transmission Electron Microscopy
    • Portnaya, I.,; Cogan, U.,; Livney, Y.D.,; Ramon, O.,; Shimoni, K.,; Rosenberg, M., Micellization of Bovine Beta Casein Studied by Isothermal Titration Microcalorimetry and Cryogenic Transmission Electron Microscopy. J Agric. Food Chem. 2006, 54, 5555–5561. DOI: 10.1021/jf060119c.
    • (2006) J Agric. Food Chem , vol.54 , pp. 5555-5561
    • Portnaya, I.1    Cogan, U.2    Livney, Y.D.3    Ramon, O.4    Shimoni, K.5    Rosenberg, M.6
  • 20
    • 84930210665 scopus 로고    scopus 로고
    • Exploring the Interaction of Naringenin with Bovine Beta-Casein Nanoparticles Using Spectroscopy
    • Moeiniafshari, -A.-A.,; Zarrabi, A.,; Bordbar, A.-K., Exploring the Interaction of Naringenin with Bovine Beta-Casein Nanoparticles Using Spectroscopy. Food Hydrocoll. 2015, 51, 1–6. DOI: 10.1016/j.foodhyd.2015.04.036.
    • (2015) Food Hydrocoll , vol.51 , pp. 1-6
    • Moeiniafshari, A.-A.1    Zarrabi, A.2    Bordbar, A.-K.3
  • 21
    • 33947182943 scopus 로고    scopus 로고
    • Casein Micelle as a Natural Nanocapsular Vehicle for Nutraceuticals
    • Semo, E.,; Kesselman, E.,; Danino, D.,; Livney, Y.D., Casein Micelle as a Natural Nanocapsular Vehicle for Nutraceuticals. Food Hydrocoll. 2007, 21, 936–942. DOI: 10.1016/j.foodhyd.2006.09.006.
    • (2007) Food Hydrocoll , vol.21 , pp. 936-942
    • Semo, E.1    Kesselman, E.2    Danino, D.3    Livney, Y.D.4
  • 22
    • 55049113077 scopus 로고    scopus 로고
    • Fluorescence Study of the Curcumin−Casein Micelle Complexation and Its Application as a Drug Nanocarrier to Cancer Cells
    • Sahu, A.,; Kasoju, N.,; Bora, U., Fluorescence Study of the Curcumin−Casein Micelle Complexation and Its Application as a Drug Nanocarrier to Cancer Cells. Biomacromolecules. 2008, 9, 2905–2912. DOI: 10.1021/bm800683f.
    • (2008) Biomacromolecules , vol.9 , pp. 2905-2912
    • Sahu, A.1    Kasoju, N.2    Bora, U.3
  • 23
    • 0037216384 scopus 로고    scopus 로고
    • Milk Intake during Childhood and Adolescence Adult Bone Density and Osteoporotic Features in US Woman
    • Kalkwarf, H.J.,; Khoury, J.C.,; Lanphear, B.P., Milk Intake during Childhood and Adolescence Adult Bone Density and Osteoporotic Features in US Woman. Am. J. Clin. Nutr. 2003, 77, 257–265.
    • (2003) Am. J. Clin. Nutr , vol.77 , pp. 257-265
    • Kalkwarf, H.J.1    Khoury, J.C.2    Lanphear, B.P.3
  • 24
    • 24944577877 scopus 로고    scopus 로고
    • Market Trends and Opportunities for Functional Dairy Beverages
    • Sharma, R.,;. Market Trends and Opportunities for Functional Dairy Beverages. Aust. J. Dairy Technol. 2005, 60, 195–198.
    • (2005) Aust. J. Dairy Technol , vol.60 , pp. 195-198
    • Sharma, R.1
  • 25
    • 79958277238 scopus 로고    scopus 로고
    • The Impact of Tea Supplementation on Microflora, pH and Antioxidant Capacity of Yoghurt
    • Najgebauer-Lejko, D.,; Sady, M.,; Grega, T.,; Walczycka, M., The Impact of Tea Supplementation on Microflora, pH and Antioxidant Capacity of Yoghurt. Int. Dairy J. 2011, 21, 568–574. DOI: 10.1016/j.idairyj.2011.03.003.
    • (2011) Int. Dairy J , vol.21 , pp. 568-574
    • Najgebauer-Lejko, D.1    Sady, M.2    Grega, T.3    Walczycka, M.4
  • 26
    • 84882944459 scopus 로고    scopus 로고
    • Optimization of Green Tea Processed Cheese Processing Conditions
    • Chen, Y.,; Zeng, Q.,; Ren, F.-Z.,; Chen, S.-W., Optimization of Green Tea Processed Cheese Processing Conditions. Food Sci. Technol. 2009, 10, 89–92.
    • (2009) Food Sci. Technol , vol.10 , pp. 89-92
    • Chen, Y.1    Zeng, Q.2    Ren, F.-Z.3    Chen, S.-W.4
  • 27
    • 77954352018 scopus 로고    scopus 로고
    • The Antioxidant Properties of Skim Milk Supplemented with Rosemary and Green Tea Extracts in Response to Pasteurisation, Homogenisation and the Addition of Salts
    • Gad, A.S.,; Abd-El-Salam, M.H., The Antioxidant Properties of Skim Milk Supplemented with Rosemary and Green Tea Extracts in Response to Pasteurisation, Homogenisation and the Addition of Salts. Int. J. Dairy Technol. 2010, 63, 349–355. DOI: 10.1111/j.1471-0307.2010.00585.x.
    • (2010) Int. J. Dairy Technol , vol.63 , pp. 349-355
    • Gad, A.S.1    Abd-El-Salam, M.H.2
  • 28
    • 84886299994 scopus 로고    scopus 로고
    • Effects of Catechin on the Phenolic Content and Antioxidant Properties of Low-Fat Cheese
    • Rashidinejad, A.,; Birch, E.J.,; Sun-Waterhouse, D.,; Everett, D.W., Effects of Catechin on the Phenolic Content and Antioxidant Properties of Low-Fat Cheese. Int. J. Food Sci. Tech. 2013, 48, 2448–2455. DOI: 10.1111/ijfs.12234.
    • (2013) Int. J. Food Sci. Tech , vol.48 , pp. 2448-2455
    • Rashidinejad, A.1    Birch, E.J.2    Sun-Waterhouse, D.3    Everett, D.W.4
  • 29
    • 84873645273 scopus 로고    scopus 로고
    • Drinking Yoghurts with Berry Polyphenols Added before and after Fermentation
    • Sun-Waterhouse, D.,; Zhou, J.,; Wadhwa, S.S., Drinking Yoghurts with Berry Polyphenols Added before and after Fermentation. Food Control. 2013, 32, 450–460.
    • (2013) Food Control , vol.32 , pp. 450-460
    • Sun-Waterhouse, D.1    Zhou, J.2    Wadhwa, S.S.3
  • 30
    • 27144501029 scopus 로고    scopus 로고
    • Milk Proteins: General and Historical Aspects
    • Kluwer Academic/Plenum Publishers, New York:; McSweeney, P.L.H
    • Fox, P.F.,; McSweeney, P.L.H. Milk Proteins: General and Historical Aspects. In Advanced Dairy Chemistry Volume 1: Proteins (Part A); Kluwer Academic/Plenum Publishers: New York, 2003; pp 1–41.
    • (2003) Advanced Dairy Chemistry Volume 1: Proteins (Part A) , pp. 1-41
    • Fox, P.F.1
  • 32
    • 76749084741 scopus 로고    scopus 로고
    • Characterization of Binding Interactions Be- Tween Green Tea Flavanoids and Milk Proteins
    • Yuksel, Z.,; Avci, E.,; Erdem, Y.K., Characterization of Binding Interactions Be- Tween Green Tea Flavanoids and Milk Proteins. Food Chem. 2010, 121, 450–456. DOI: 10.1016/j.foodchem.2009.12.064.
    • (2010) Food Chem , vol.121 , pp. 450-456
    • Yuksel, Z.1    Avci, E.2    Erdem, Y.K.3
  • 33
    • 36148935581 scopus 로고    scopus 로고
    • Phenolics from Walnut (Juglans Regia L.) Kernels: Antioxidant Activity and Interactions with Proteins
    • Labuckas, D.O.,; Maestri, D.M.,; Perelló, M.,; Martínez, M.L.,; Lamarque, A.L., Phenolics from Walnut (Juglans Regia L.) Kernels: Antioxidant Activity and Interactions with Proteins. Food Chem. 2008, 107, 607–612. DOI: 10.1016/j.foodchem.2007.08.051.
    • (2008) Food Chem , vol.107 , pp. 607-612
    • Labuckas, D.O.1    Maestri, D.M.2    Perelló, M.3    Martínez, M.L.4    Lamarque, A.L.5
  • 34
    • 84866545928 scopus 로고    scopus 로고
    • Effect of Phenolic Compounds on Protein Cross-Linking and Properties of Film from Fish Myofibrillar Protein
    • Prodpran, T.,; Benjakul, S.,; Phatcharat, S., Effect of Phenolic Compounds on Protein Cross-Linking and Properties of Film from Fish Myofibrillar Protein. Int. J. Biol. Macromolec. 2012, 51, 774–782. DOI: 10.1016/j.ijbiomac.2012.07.010.
    • (2012) Int. J. Biol. Macromolec , vol.51 , pp. 774-782
    • Prodpran, T.1    Benjakul, S.2    Phatcharat, S.3
  • 35
    • 77957857745 scopus 로고    scopus 로고
    • Digestibility and Allergenicity of Β-Lactoglobulin following Laccase-Mediated Cross-Linking in the Presence of Sour Cherry Phenolics
    • Tantoush, Z.,; Stanic, D.,; Stojadinovic, M.,; Ognjenovic, J.,; Mihajlovic, L.,; Atanaskovic- Markavic, M.,; Velickovic, T.C., Digestibility and Allergenicity of Β-Lactoglobulin following Laccase-Mediated Cross-Linking in the Presence of Sour Cherry Phenolics. Food Chem. 2011, 125, 84–91. DOI: 10.1016/j.foodchem.2010.08.040.
    • (2011) Food Chem , vol.125 , pp. 84-91
    • Tantoush, Z.1    Stanic, D.2    Stojadinovic, M.3    Ognjenovic, J.4    Mihajlovic, L.5    Atanaskovic- Markavic, M.6    Velickovic, T.C.7
  • 36
    • 0034926162 scopus 로고    scopus 로고
    • Significance and Applications of Phenolic Compounds in the Production and Quality of Milk and Dairy Products: A Review
    • O’connell, J.E.,; Fox, P.F., Significance and Applications of Phenolic Compounds in the Production and Quality of Milk and Dairy Products: A Review. Int. Dairy J. 2001, 11, 103–120. DOI: 10.1016/S0958-6946(01)00033-4.
    • (2001) Int. Dairy J , vol.11 , pp. 103-120
    • O’connell, J.E.1    Fox, P.F.2
  • 37
    • 0029302371 scopus 로고
    • Interaction of Β-Lactoglobulin with Retinol and Fatty Acids and Its Role as A Possible Biological Function for This Protein: A Review
    • Perez, M.D.,; Calvo, M., Interaction of Β-Lactoglobulin with Retinol and Fatty Acids and Its Role as A Possible Biological Function for This Protein: A Review. J. Dairy Sci. 1995, 78, 978–988. DOI: 10.3168/jds.S0022-0302(95)76713-3.
    • (1995) J. Dairy Sci , vol.78 , pp. 978-988
    • Perez, M.D.1    Calvo, M.2
  • 38
    • 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. Spectrochim. Acta A. 2011, 82, 164–168. DOI: 10.1016/j.saa.2011.07.028.
    • (2011) Spectrochim. Acta A , vol.82 , pp. 164-168
    • Wu, X.1    Wu, H.2    Liu, M.3    Liu, Z.4    Xu, H.5    Lai, F.6
  • 39
    • 84950242616 scopus 로고    scopus 로고
    • Astringency Reduction in Red Wine by Whey Proteins
    • Jauregi, P.,; Olatujoye, J.B.,; Cabezudo, I.,; Frazier, R.A.,; Gordon, M.H., Astringency Reduction in Red Wine by Whey Proteins. Food Chem. 2016, 199, 547–555. DOI: 10.1016/j.foodchem.2015.12.052.
    • (2016) Food Chem , vol.199 , pp. 547-555
    • Jauregi, P.1    Olatujoye, J.B.2    Cabezudo, I.3    Frazier, R.A.4    Gordon, M.H.5
  • 40
    • 84881225726 scopus 로고    scopus 로고
    • The Interaction of Cocoa Polyphenols with Milk Proteins Studied by Proteomic Techniques
    • Gallo, M.,; Vinci, G.,; Graziani, G.,; De Simone, C.,; Ferranti, P., The Interaction of Cocoa Polyphenols with Milk Proteins Studied by Proteomic Techniques. Food Res. Int. 2013, 54, 406–415. DOI: 10.1016/j.foodres.2013.07.011.
    • (2013) Food Res. Int , vol.54 , pp. 406-415
    • Gallo, M.1    Vinci, G.2    Graziani, G.3    De Simone, C.4    Ferranti, P.5
  • 41
    • 0000943593 scopus 로고
    • Interaction of Synthetic Proanthocyanidin Dimer and Trimer with Bovine Serum Albumin and Purified Bean Globulin Fraction G-1
    • Artz, W.E.,; Bishop, P.D.,; Dunker, A.K.,; Schanus, E.G.,; Swanson, B.G., Interaction of Synthetic Proanthocyanidin Dimer and Trimer with Bovine Serum Albumin and Purified Bean Globulin Fraction G-1. J. Agric. Food Chem. 1987, 35, 417–421. DOI: 10.1021/jf00075a033.
    • (1987) J. Agric. Food Chem , vol.35 , pp. 417-421
    • Artz, W.E.1    Bishop, P.D.2    Dunker, A.K.3    Schanus, E.G.4    Swanson, B.G.5
  • 42
    • 11244303574 scopus 로고    scopus 로고
    • Interaction of Flavonoids with Bovine Serum Albumin: A Fluorescence Quenching Study
    • Papadopoulou, A.,; Green, R.J.,; Frazier, R.A., Interaction of Flavonoids with Bovine Serum Albumin: A Fluorescence Quenching Study. J. Agric. Food Chem. 2005, 53, 158–163. DOI: 10.1021/jf048693g.
    • (2005) J. Agric. Food Chem , vol.53 , pp. 158-163
    • Papadopoulou, A.1    Green, R.J.2    Frazier, R.A.3
  • 43
    • 9244243170 scopus 로고    scopus 로고
    • Spectrophotometric and Kinetic Studies on the Binding of the Bioflavonoid Quercetin to Bovine Serum Albumin
    • Kitson, T.M.,;. Spectrophotometric and Kinetic Studies on the Binding of the Bioflavonoid Quercetin to Bovine Serum Albumin. Biosci. Biotechnol. Biochem. 2004, 68, 2165–2170. DOI: 10.1271/bbb.68.2165.
    • (2004) Biosci. Biotechnol. Biochem , vol.68 , pp. 2165-2170
    • Kitson, T.M.1
  • 44
    • 42449128003 scopus 로고    scopus 로고
    • Influence of B-Ring Hydroxylation on Interactions of Flavonols with Bovine Serum Albumin
    • Xiao, J.,; Suzuki, M.,; Jiang, X.,; Chen, X.,; Yamamoto, K.,; Ren, F.,; Xu, M., Influence of B-Ring Hydroxylation on Interactions of Flavonols with Bovine Serum Albumin. J. Agric. Food Chem. 2008, 56, 2350–2356. DOI: 10.1021/jf7037295.
    • (2008) J. Agric. Food Chem , vol.56 , pp. 2350-2356
    • Xiao, J.1    Suzuki, M.2    Jiang, X.3    Chen, X.4    Yamamoto, K.5    Ren, F.6    Xu, M.7
  • 45
    • 84920724824 scopus 로고    scopus 로고
    • Analysis of Binding Interaction of Genistein and Kaempferol with Bovine Α-Lactalbumin
    • Mohammadi, F.,; Moeeni, M., Analysis of Binding Interaction of Genistein and Kaempferol with Bovine Α-Lactalbumin. J. Funct. Foods. 2015, 12, 458–467. DOI: 10.1016/j.jff.2014.12.012.
    • (2015) J. Funct. Foods , vol.12 , pp. 458-467
    • Mohammadi, F.1    Moeeni, M.2
  • 46
    • 84923647904 scopus 로고    scopus 로고
    • Study on the Interactions of Trans-Resveratrol and Curcumin with Bovine Α-Lactalbumin by Spectroscopic Analysis and Molecular Docking
    • Mohammadi, F.,; Moeeni, M., Study on the Interactions of Trans-Resveratrol and Curcumin with Bovine Α-Lactalbumin by Spectroscopic Analysis and Molecular Docking. Mater. Sci. Eng. C. 2015, 50, 358–366. DOI: 10.1016/j.msec.2015.02.007.
    • (2015) Mater. Sci. Eng. C , vol.50 , pp. 358-366
    • Mohammadi, F.1    Moeeni, M.2
  • 47
    • 0028097921 scopus 로고
    • The Structure and Function of Proline-Rich Regions in Proteins
    • Williamson, M.P.,;. The Structure and Function of Proline-Rich Regions in Proteins. Biochem. J. 1994, 297(2), 249–260. DOI:10.1042/bj2970249.
    • (1994) Biochem. J , vol.297 , Issue.2 , pp. 249-260
    • Williamson, M.P.1
  • 49
    • 84882407570 scopus 로고    scopus 로고
    • A Combined Spectroscopic, Molecular Docking and Molecular Dynamic Simulation Study on the Interaction of Quercetin with Β-Casein Nanoparticles
    • Mehranfar, F.,; Bordbar, A.-K.,; Parastar, H., A Combined Spectroscopic, Molecular Docking and Molecular Dynamic Simulation Study on the Interaction of Quercetin with Β-Casein Nanoparticles. J. Photochem. Photobiol B. 2013, 127, 100–107. DOI: 10.1016/j.jphotobiol.2013.07.019.
    • (2013) J. Photochem. Photobiol B , vol.127 , pp. 100-107
    • Mehranfar, F.1    Bordbar, A.-K.2    Parastar, H.3
  • 50
    • 0042061110 scopus 로고    scopus 로고
    • Effects of Non-Covalent Interactions with 5-O-Caffeoylquinic Acid (Chlorogenic Acid) on the Heat Denaturation and Solubility of Globular Proteins
    • Prigent, S.V.,; Gruppen, H.,; Visser, A.J.,; Van Koningsveld, G.A.,; De Jong, G.A.,; Voragen, A.G., Effects of Non-Covalent Interactions with 5-O-Caffeoylquinic Acid (Chlorogenic Acid) on the Heat Denaturation and Solubility of Globular Proteins. J. Agric. Food Chem. 2003, 51, 5088–5095. DOI: 10.1021/jf021229w.
    • (2003) J. Agric. Food Chem , vol.51 , pp. 5088-5095
    • Prigent, S.V.1    Gruppen, H.2    Visser, A.J.3    Van Koningsveld, G.A.4    De Jong, G.A.5    Voragen, A.G.6
  • 51
    • 20844443677 scopus 로고    scopus 로고
    • Binding of Selected Phenolic Compounds to Proteins J
    • Rawel, H.M.,; Meidtner, K.,; Kroll, J., Binding of Selected Phenolic Compounds to Proteins J. Agric. Food Chem. 2005, 53, 4228−4235. DOI: 10.1021/jf0480290.
    • (2005) Agric. Food Chem , vol.53 , pp. 4228-4235
    • Rawel, H.M.1    Meidtner, K.2    Kroll, J.3
  • 52
    • 84857059676 scopus 로고    scopus 로고
    • Study of the Acid and Thermal Stability of Β-Lactoglobulin–Ligand Complexes Using Fluorescence Quenching
    • Liang, L.,; Subirade, M., Study of the Acid and Thermal Stability of Β-Lactoglobulin–Ligand Complexes Using Fluorescence Quenching. Food Chem. 2012, 132, 2023–2029. DOI: 10.1016/j.foodchem.2011.12.043.
    • (2012) Food Chem , vol.132 , pp. 2023-2029
    • Liang, L.1    Subirade, M.2
  • 53
    • 0032475891 scopus 로고    scopus 로고
    • Monomeric Bovine Β-Lactoglobulin Adopts A-Barrel Fold at pH 2
    • Fogolari, F.,; Ragona, L.,; Zetta, L.,; Romagnoli, S.,; De Kruif, K.G.,; Molinari, H., Monomeric Bovine Β-Lactoglobulin Adopts A-Barrel Fold at pH 2. FEBS Lett. 1998, 436, 149–154. DOI: 10.1016/S0014-5793(98)00936-3.
    • (1998) FEBS Lett , vol.436 , pp. 149-154
    • Fogolari, F.1    Ragona, L.2    Zetta, L.3    Romagnoli, S.4    De Kruif, K.G.5    Molinari, H.6
  • 54
    • 33747592575 scopus 로고    scopus 로고
    • Isothermal Titration Calorimetry Study of Epicatechin Binding to Serum Albumin
    • Frazier, R.A.,; Papadopoulou, A.,; Green, R.J., Isothermal Titration Calorimetry Study of Epicatechin Binding to Serum Albumin. J. Pharm. Biomed. Anal. 2006, 41, 1602–1605. DOI: 10.1016/j.jpba.2006.02.004.
    • (2006) J. Pharm. Biomed. Anal , vol.41 , pp. 1602-1605
    • Frazier, R.A.1    Papadopoulou, A.2    Green, R.J.3
  • 55
    • 28444498926 scopus 로고    scopus 로고
    • Protein Precipitating Capacity of Phenolics of Wild Blueberry Leaves and Fruits
    • Naczk, M.,; Grant, S.,; Zadernowski, R.,; Barre, E., Protein Precipitating Capacity of Phenolics of Wild Blueberry Leaves and Fruits. Food Chem. 2006, 96, 640–647. DOI: 10.1016/j.foodchem.2005.03.017.
    • (2006) Food Chem , vol.96 , pp. 640-647
    • Naczk, M.1    Grant, S.2    Zadernowski, R.3    Barre, E.4
  • 56
    • 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.Y.,; Ho, C.T.,; Huang, Q.R., 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. DOI: 10.1021/jf070590l.
    • (2007) J. Agric. Food Chem , vol.55 , pp. 4987-4992
    • Wang, X.Y.1    Ho, C.T.2    Huang, Q.R.3
  • 57
    • 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 Hydrocoll. 2010, 24, 735–743. DOI: 10.1016/j.foodhyd.2010.03.015.
    • (2010) Food Hydrocoll , vol.24 , pp. 735-743
    • Shpigelman, A.1    Israeli, G.2    Livney, Y.D.3
  • 58
  • 59
    • 0035117563 scopus 로고    scopus 로고
    • Structural Features of Procyanidin Interactions with Salivary Proteins
    • De Freitas, V.,; Mateus, N., Structural Features of Procyanidin Interactions with Salivary Proteins. J. Agric. Food Chem. 2001, 49, 940–945. DOI: 10.1021/jf000981z.
    • (2001) J. Agric. Food Chem , vol.49 , pp. 940-945
    • De Freitas, V.1    Mateus, N.2
  • 60
    • 0032927142 scopus 로고    scopus 로고
    • Interactions of Grape Seed Tannins with Salivary Proteins
    • Sarni-Manchado, P.,; Cheynier, V.,; Moutounet, M., Interactions of Grape Seed Tannins with Salivary Proteins. J. Agric. Food Chem. 1999, 47, 42–47. DOI: 10.1021/jf9805146.
    • (1999) J. Agric. Food Chem , vol.47 , pp. 42-47
    • Sarni-Manchado, P.1    Cheynier, V.2    Moutounet, M.3
  • 61
    • 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. J. Agric. Food Chem. 2007, 55, 6726–6735. DOI: 10.1021/jf070905x.
    • (2007) J. Agric. Food Chem , vol.55 , pp. 6726-6735
    • Soares, S.1    Mateus, N.2    De Freitas, V.3
  • 62
    • 84865339163 scopus 로고    scopus 로고
    • Interactions of Different Polyphenols with Bovine Serum Albumin Using Fluorescence Quenching and Molecular Docking
    • Skrt, M.,; Benedik, E.,; Podlipnik, C.,; Ulrih, N.P., Interactions of Different Polyphenols with Bovine Serum Albumin Using Fluorescence Quenching and Molecular Docking. Food Chem. 2012, 135, 2418–2424. DOI: 10.1016/j.foodchem.2012.06.114.
    • (2012) Food Chem , vol.135 , pp. 2418-2424
    • Skrt, M.1    Benedik, E.2    Podlipnik, C.3    Ulrih, N.P.4
  • 63
    • 78650971978 scopus 로고    scopus 로고
    • Structure–Affinity Relationship of Flavones on Binding to Serum Albumins: Effect of Hydroxyl Groups on Ring A
    • Xiao, J.,; Cao, H.,; Wang, Y.,; Yamamoto, K.,; Wei, X., Structure–Affinity Relationship of Flavones on Binding to Serum Albumins: Effect of Hydroxyl Groups on Ring A. Mol. Nutr. Food Res. 2010, 54, 253–260. DOI: 10.1002/mnfr.200900454.
    • (2010) Mol. Nutr. Food Res , vol.54 , pp. 253-260
    • Xiao, J.1    Cao, H.2    Wang, Y.3    Yamamoto, K.4    Wei, X.5
  • 64
    • 84867474465 scopus 로고    scopus 로고
    • The Interaction of Polyphenol Flavonoids with Β-Lactoglobulin: Molecular Docking and Molecular Dynamics Simulation Studies
    • Sahihi, M.,; Heidari-Koholi, Z.,; Bordbar, A.-K., The Interaction of Polyphenol Flavonoids with Β-Lactoglobulin: Molecular Docking and Molecular Dynamics Simulation Studies. J. Macromol. Sci. B. 2012, 51, 2311–2323. DOI: 10.1080/00222348.2012.672854.
    • (2012) J. Macromol. Sci. B , vol.51 , pp. 2311-2323
    • Sahihi, M.1    Heidari-Koholi, Z.2    Bordbar, A.-K.3
  • 65
    • 80053557978 scopus 로고    scopus 로고
    • Investigation of Flavonoids Bearing Different Substituents on Ring C and Their Cu+2 Complex Binding with Bovine Serum Albumin: Structure Affinity Relationship Aspects
    • Shi, S.,; Zhang, Y.,; Chen, X.,; Peng, M., Investigation of Flavonoids Bearing Different Substituents on Ring C and Their Cu+2 Complex Binding with Bovine Serum Albumin: Structure Affinity Relationship Aspects. J. Agric. Food Chem. 2011, 59, 10761–10769. DOI: 10.1021/jf2027523.
    • (2011) J. Agric. Food Chem , vol.59 , pp. 10761-10769
    • Shi, S.1    Zhang, Y.2    Chen, X.3    Peng, M.4
  • 66
    • 80155155891 scopus 로고    scopus 로고
    • Interaction of Dietary Polyphenols with Bovine Milk Proteins: Molecular Structure–Affinity Relationship and Influencing Bioactivity Aspects
    • Xiao, J.,; Mao, F.,; Yang, F.,; Zhao, Y.,; Zhang, C.,; Yamamoto, K., Interaction of Dietary Polyphenols with Bovine Milk Proteins: Molecular Structure–Affinity Relationship and Influencing Bioactivity Aspects. Mol. Nutr. Food Res. 2011, 55, 1–9. DOI: 10.1002/mnfr.201100280.
    • (2011) Mol. Nutr. Food Res , vol.55 , pp. 1-9
    • Xiao, J.1    Mao, F.2    Yang, F.3    Zhao, Y.4    Zhang, C.5    Yamamoto, K.6
  • 67
    • 78650660610 scopus 로고    scopus 로고
    • Structural Relationship and Binding Mechanisms of Five Flavonoids with Bovine Serum Albumin
    • Liu, E.-H.,; Qi, L.-W.,; Li, P., Structural Relationship and Binding Mechanisms of Five Flavonoids with Bovine Serum Albumin. Molecules. 2010, 15, 9092–9103. DOI: 10.3390/molecules15129092.
    • (2010) Molecules , vol.15 , pp. 9092-9103
    • Liu, E.-H.1    Qi, L.-W.2    Li, P.3
  • 68
    • 34250683877 scopus 로고    scopus 로고
    • Hydrolyzable Tannin Structures Influence Relative Globular and Random Coil Protein Binding Strengths
    • Deaville, E.R.,; Green, R.J.,; Mueller-Harvey, I.,; Willoughby, I.,; Frazier, R.A., Hydrolyzable Tannin Structures Influence Relative Globular and Random Coil Protein Binding Strengths. J. Agric. Food Chem. 2007, 55, 4554–4561. DOI: 10.1021/jf063770o.
    • (2007) J. Agric. Food Chem , vol.55 , pp. 4554-4561
    • Deaville, E.R.1    Green, R.J.2    Mueller-Harvey, I.3    Willoughby, I.4    Frazier, R.A.5
  • 70
    • 27944473247 scopus 로고    scopus 로고
    • Role of Peptide Primary Sequence in Polyphenol-Protein Recognition: An Example with Neurotensin
    • Richard, T.,; Vitrac, X.,; Merillon, J.M.,; Monti, J.P., Role of Peptide Primary Sequence in Polyphenol-Protein Recognition: An Example with Neurotensin. Biochim. Biophys. Acta. 2005, 1726, 238− 243.
    • (2005) Biochim. Biophys. Acta , vol.1726 , pp. 238-243
    • Richard, T.1    Vitrac, X.2    Merillon, J.M.3    Monti, J.P.4
  • 71
    • 84866661019 scopus 로고    scopus 로고
    • Structures of Bovine, Equine and Leporine Serum Albumin
    • Bujacz, A.,;. Structures of Bovine, Equine and Leporine Serum Albumin. Acta Crystallogr., Sect. D: Biol. Crystallogr. 2012, 68, 1278–1289. DOI: 10.1107/S0907444912027047.
    • (2012) Acta Crystallogr., Sect. D: Biol. Crystallogr , vol.68 , pp. 1278-1289
    • Bujacz, A.1
  • 72
    • 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.,; Roy, A.S.,; Ghosh, K.S.,; Dasgupta, S., Spectroscopic and Docking Studies of the Binding of Two Stereoisomeric Antioxidant Catechins to Serum Albumins. J. Lumin. 2012, 132, 1364–1375. DOI: 10.1016/j.jlumin.2011.12.063.
    • (2012) J. Lumin , vol.132 , pp. 1364-1375
    • Roy, D.1    Dutta, S.2    Maity, S.S.3    Ghosh, S.4    Roy, A.S.5    Ghosh, K.S.6    Dasgupta, S.7
  • 73
    • 52649138940 scopus 로고    scopus 로고
    • Binding of Phenolic Compounds and Their Derivatives to Bovine and Reindeer 
Β-Lactoglobulin
    • Riihimäki, L.H.,; Vainio, M.J.,; Heikura, J.M.,; Valkonen, K.H.,; Virtanen, V.T.,; Vuorela, P.M., Binding of Phenolic Compounds and Their Derivatives to Bovine and Reindeer 
Β-Lactoglobulin. J. Agric. Food Chem. 2008, 56, 7721–7729. DOI: 10.1021/jf801120a.
    • (2008) J. Agric. Food Chem , vol.56 , pp. 7721-7729
    • Riihimäki, L.H.1    Vainio, M.J.2    Heikura, J.M.3    Valkonen, K.H.4    Virtanen, V.T.5    Vuorela, P.M.6
  • 74
    • 33644596182 scopus 로고    scopus 로고
    • Thermodynamics of Binding Interactions between Bovine Β-Lactoglobulin A and the Antihypertensive Peptide Β-Lg F142-148
    • Roufik, S.,; Gauthier, S.F.,; Leng, X.J.,; Turgeon, S.L., Thermodynamics of Binding Interactions between Bovine Β-Lactoglobulin A and the Antihypertensive Peptide Β-Lg F142-148. Biomacromolecules. 2006, 7, 419–426. DOI: 10.1021/bm050229c.
    • (2006) Biomacromolecules , vol.7 , pp. 419-426
    • Roufik, S.1    Gauthier, S.F.2    Leng, X.J.3    Turgeon, S.L.4
  • 75
    • 80052807887 scopus 로고    scopus 로고
    • Investigation into the Interaction between Resveratrol and Whey Proteins Using Fluorescence Spectroscopy
    • Hemar, Y.,; Gerbeaud, M.,; Oliver, C.M.,; Augustin, M.A., Investigation into the Interaction between Resveratrol and Whey Proteins Using Fluorescence Spectroscopy. Int. J. Food Sci. Tech. 2011, 46, 2137–2144. DOI: 10.1111/j.1365-2621.2011.02728.x.
    • (2011) Int. J. Food Sci. Tech , vol.46 , pp. 2137-2144
    • Hemar, Y.1    Gerbeaud, M.2    Oliver, C.M.3    Augustin, M.A.4
  • 76
    • 84893687795 scopus 로고    scopus 로고
    • Exploring Binding Properties of Naringenin with Bovine Β-Lactoglobulin: A Fluorescence, Molecular Docking and Molecular Dynamics
Simulation Study
    • Gholami, S.,; Bordbar, A.K., Exploring Binding Properties of Naringenin with Bovine Β-Lactoglobulin: A Fluorescence, Molecular Docking and Molecular Dynamics
Simulation Study. Biophys. Chem. 2014, 187, 33–42. DOI: 10.1016/j.bpc.2014.01.003.
    • (2014) Biophys. Chem , vol.187 , pp. 33-42
    • Gholami, S.1    Bordbar, A.K.2
  • 79
    • 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.A., Binding Sites of Resveratrol, Genistein, and Curcumin with Milk Α- and Β‐Caseins. J. Phys. Chem. B. 2013, 117, 1287–1295. DOI: 10.1021/jp3114557.
    • (2013) J. Phys. Chem. B , vol.117 , pp. 1287-1295
    • Bourassa, P.1    Bariyanga, J.2    Tajmir-Riahi, H.A.3
  • 80
    • 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. DOI: 10.1021/jf0704108.
    • (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
  • 81
    • 84946761496 scopus 로고    scopus 로고
    • Interaction of Chlorogenic Acid with Milk Proteins Analyzed by Spectroscopic and Modeling Methods
    • Liu, J.,; Wang, Q.,; Zhang, H.,; Yu, D.,; Jin, S.,; Ren, F., Interaction of Chlorogenic Acid with Milk Proteins Analyzed by Spectroscopic and Modeling Methods. Spectrosc. Lett. 2016, 49, 44–50. DOI: 10.1080/00387010.2015.1066826.
    • (2016) Spectrosc. Lett , vol.49 , pp. 44-50
    • Liu, J.1    Wang, Q.2    Zhang, H.3    Yu, D.4    Jin, S.5    Ren, F.6
  • 82
    • 84878314960 scopus 로고    scopus 로고
    • Binding of Resveratrol with Sodium Caseinate in Aqueous Solutions
    • Acharya, D.P.,; Sanguansri, L.,; Augustin, M.A., Binding of Resveratrol with Sodium Caseinate in Aqueous Solutions. Food Chem. 2013, 141, 1050–1054. DOI: 10.1016/j.foodchem.2013.03.037.
    • (2013) Food Chem , vol.141 , pp. 1050-1054
    • Acharya, D.P.1    Sanguansri, L.2    Augustin, M.A.3
  • 83
    • 84867896149 scopus 로고    scopus 로고
    • Binding Affinity between Dietary Polyphenols and Β-Lactoglobulin Negatively Correlates with the Protein Susceptibility to Digestion and Total Antioxidant Activity of Complexes Formed
    • Stojadinovic, M.,; Radosavljevic, J.,; Ognjenovic, J.,; Vesic, J.,; Prodic, I.,; Stanic-Vucinic, D.,; Cirkovic- Velickovic, T., Binding Affinity between Dietary Polyphenols and Β-Lactoglobulin Negatively Correlates with the Protein Susceptibility to Digestion and Total Antioxidant Activity of Complexes Formed. Food Chem. 2013, 136, 1263–1271. DOI: 10.1016/j.foodchem.2012.09.040.
    • (2013) Food Chem , vol.136 , pp. 1263-1271
    • Stojadinovic, M.1    Radosavljevic, J.2    Ognjenovic, J.3    Vesic, J.4    Prodic, I.5    Stanic-Vucinic, D.6    Cirkovic- Velickovic, T.7
  • 84
    • 84866493882 scopus 로고    scopus 로고
    • Spectroscopic and Isothermal Titration Calorimetry Studies of Binding Interaction of Ferulic Acid with Bovine Serum Albumin
    • Ojha, H.,; Mishra, K.,; Hassan, M.I.,; Chaudhury, N.K., Spectroscopic and Isothermal Titration Calorimetry Studies of Binding Interaction of Ferulic Acid with Bovine Serum Albumin. Thermochim. Acta. 2012, 548, 56–64. DOI: 10.1016/j.tca.2012.08.016.
    • (2012) Thermochim. Acta , vol.548 , pp. 56-64
    • Ojha, H.1    Mishra, K.2    Hassan, M.I.3    Chaudhury, N.K.4
  • 85
    • 84986456066 scopus 로고
    • Ultrafiltration Method of Studying Binding of Ligands to Macromolecules
    • Cheryan, M.,; Saeed, M., Ultrafiltration Method of Studying Binding of Ligands to Macromolecules. J. Food Biochem. 1989, 13, 289–316. DOI: 10.1111/j.1745-4514.1989.tb00400.x.
    • (1989) J. Food Biochem , vol.13 , pp. 289-316
    • Cheryan, M.1    Saeed, M.2
  • 86
    • 0032901515 scopus 로고    scopus 로고
    • Isothermal Titration Calorimetry and Differential Scanning Calorimetry as Complementary Tools to Investigate the Energetics of Biomolecular Recognition
    • Jelasarov, I.,; Bosshard, H.R., Isothermal Titration Calorimetry and Differential Scanning Calorimetry as Complementary Tools to Investigate the Energetics of Biomolecular Recognition. J. Mol. Recognit. 1999, 12, 3–8. DOI: 10.1002/(SICI)1099-1352(199901/02)12:1<3::AID-JMR441>3.0.CO;2-6.
    • (1999) J. Mol. Recognit , vol.12 , pp. 3-8
    • Jelasarov, I.1    Bosshard, H.R.2
  • 87
    • 0027956678 scopus 로고
    • Thermodynamics of Inhibitor Binding to the Catalytic Site of Glucoamylase from Aspergillus Niger Determined by Displacement Titration Calorimetry
    • Sigurskjold, B.W.,; Berland, C.R.,; Svensson, B., Thermodynamics of Inhibitor Binding to the Catalytic Site of Glucoamylase from Aspergillus Niger Determined by Displacement Titration Calorimetry. Biochemistry. 1994, 33, 10191–10199. DOI: 10.1021/bi00199a048.
    • (1994) Biochemistry , vol.33 , pp. 10191-10199
    • Sigurskjold, B.W.1    Berland, C.R.2    Svensson, B.3
  • 88
    • 0035442411 scopus 로고    scopus 로고
    • Direct Measurement of Protein Binding Energetics by Isothermal Titration Calorimetry
    • Leavitt, S.,; Freire, E., Direct Measurement of Protein Binding Energetics by Isothermal Titration Calorimetry. Curr. Opin. Struct. Biol. 2001, 11, 560–566. DOI: 10.1016/S0959-440X(00)00248-7.
    • (2001) Curr. Opin. Struct. Biol , vol.11 , pp. 560-566
    • Leavitt, S.1    Freire, E.2
  • 89
    • 3543005385 scopus 로고    scopus 로고
    • Thermodynamics of Protein–Ligand Interactions: History, Presence, and Future Aspects
    • Perozzo, R.,; Folkers, G.,; Scapozza, L., Thermodynamics of Protein–Ligand Interactions: History, Presence, and Future Aspects. J. Recept. Sig. Transd. 2004, 24, 1–52. DOI: 10.1081/RRS-120037896.
    • (2004) J. Recept. Sig. Transd , vol.24 , pp. 1-52
    • Perozzo, R.1    Folkers, G.2    Scapozza, L.3
  • 90
    • 84860390480 scopus 로고    scopus 로고
    • Extent of Enthalpy–Entropy Compensation in Protein–Ligand Interactions
    • Olsson, T.S.G.,; Ladbury, J.E.,; Pitt, W.R.,; Williams, M.A., Extent of Enthalpy–Entropy Compensation in Protein–Ligand Interactions. Protein Sci. 2011, 20, 1607–1618. DOI: 10.1002/pro.692.
    • (2011) Protein Sci , vol.20 , pp. 1607-1618
    • Olsson, T.S.G.1    Ladbury, J.E.2    Pitt, W.R.3    Williams, M.A.4
  • 91
    • 76449111379 scopus 로고    scopus 로고
    • Study on the Interaction of Matrine with Bovine Serum Albumin
    • Sun, X.,; Xu, X.,; Liu, M.,; Li, L.,; Sun, D., Study on the Interaction of Matrine with Bovine Serum Albumin. J. Sol. Chem. 2010, 39, 77–85. DOI: 10.1007/s10953-009-9487-z.
    • (2010) J. Sol. Chem , vol.39 , pp. 77-85
    • Sun, X.1    Xu, X.2    Liu, M.3    Li, L.4    Sun, D.5
  • 92
    • 79959690715 scopus 로고    scopus 로고
    • Fluorescence Quenching and Ligand Binding: A Critical Discussion of A Popular Methodology
    • Van De Weert, M.,; Stella, L., Fluorescence Quenching and Ligand Binding: A Critical Discussion of A Popular Methodology. J. Mol. Struct. 2011, 998, 144–150. DOI: 10.1016/j.molstruc.2011.05.023.
    • (2011) J. Mol. Struct , vol.998 , pp. 144-150
    • Van De Weert, M.1    Stella, L.2
  • 93
    • 33748413614 scopus 로고    scopus 로고
    • Determining the Binding Affinities of Phenolic Compounds to Proteins by Quenching of the Intrinsic Tryptophan Fluorescence
    • Rawel, H.M.,; Frey, S.K.,; Meidtner, K.,; Kroll, J.,; Schweigert, F.J., Determining the Binding Affinities of Phenolic Compounds to Proteins by Quenching of the Intrinsic Tryptophan Fluorescence. Mol. Nutr. Food Res. 2006, 50, 705–713. DOI: 10.1002/(ISSN)1613-4133.
    • (2006) Mol. Nutr. Food Res , vol.50 , pp. 705-713
    • Rawel, H.M.1    Frey, S.K.2    Meidtner, K.3    Kroll, J.4    Schweigert, F.J.5
  • 95
    • 33748276474 scopus 로고    scopus 로고
    • Protein–Ligand Docking: Current Status and Future Challenges
    • Sousa, S.F.,; Fernandes, P.A.,; Ramos, M.J., Protein–Ligand Docking: Current Status and Future Challenges. Proteins: Struct., Funct., Bioinf. 2006, 65, 15–26. DOI: 10.1002/prot.21082.
    • (2006) Proteins: Struct., Funct., Bioinf , vol.65 , pp. 15-26
    • Sousa, S.F.1    Fernandes, P.A.2    Ramos, M.J.3
  • 96
    • 79959224583 scopus 로고    scopus 로고
    • Molecular Docking: A Powerful Approach for Structure-Based Drug Discovery
    • Meng, X.Y.,; Zhang, H.X.,; Mezei, M.,; Cui, M., Molecular Docking: A Powerful Approach for Structure-Based Drug Discovery. Curr. Comput. Aided Drug Des. 2011, 7, 146–157. DOI: 10.2174/157340911795677602.
    • (2011) Curr. Comput. Aided Drug Des , vol.7 , pp. 146-157
    • Meng, X.Y.1    Zhang, H.X.2    Mezei, M.3    Cui, M.4
  • 97
    • 84872275671 scopus 로고    scopus 로고
    • Studies on the Interaction Of‐Epigallocatechin‐3‐Gallate from Green Tea with Bovine Β‐Lactoglobulin by Spectroscopic Methods and Docking
    • Wu, X.,; Dey, R.,; Wu, H.U.I.,; Liu, Z.,; He, Q.,; Zeng, X., Studies on the Interaction Of‐Epigallocatechin‐3‐Gallate from Green Tea with Bovine Β‐Lactoglobulin by Spectroscopic Methods and Docking. Int. J. Dairy Technol. 2013, 66, 7–13. DOI: 10.1111/idt.2013.66.issue-1.
    • (2013) Int. J. Dairy Technol , vol.66 , pp. 7-13
    • Wu, X.1    Dey, R.2    Wu, H.U.I.3    Liu, Z.4    He, Q.5    Zeng, X.6
  • 98
    • 80054991125 scopus 로고    scopus 로고
    • Interaction of Epigallocatechin-3-Gallate
With Β-Lactoglobulin: Molecular Characterization and Biological Implication
    • Zorilla, R.,; Liang, L.,; Remondetto, G.,; Subirade, M., Interaction of Epigallocatechin-3-Gallate
With Β-Lactoglobulin: Molecular Characterization and Biological Implication. Dairy Sci. Technol. 2011, 91, 629–644. DOI: 10.1007/s13594-011-0036-3.
    • (2011) Dairy Sci. Technol , vol.91 , pp. 629-644
    • Zorilla, R.1    Liang, L.2    Remondetto, G.3    Subirade, M.4
  • 99
    • 84887013732 scopus 로고    scopus 로고
    • Probing the Binding Sites of Resveratrol, Genistein, and Curcumin with Milk Β-Lactoglobulin
    • Kanakis, C.D.,; Tarantilis, P.A.,; Polissiou, M.G.,; Tajmir-Riahi, H.A., Probing the Binding Sites of Resveratrol, Genistein, and Curcumin with Milk Β-Lactoglobulin. J. Biomol. Struct. Dyn. 2013, 31, 1455–1466. DOI: 10.1080/07391102.2012.742461.
    • (2013) J. Biomol. Struct. Dyn , vol.31 , pp. 1455-1466
    • Kanakis, C.D.1    Tarantilis, P.A.2    Polissiou, M.G.3    Tajmir-Riahi, H.A.4
  • 100
    • 70749122929 scopus 로고    scopus 로고
    • Interactions between Globular Proteins and Procyanidins of Different Degrees of Polymerization
    • Prigent, S.V.E.,; Voragen, A.G.,; Van Koningsveld, G.A.,; Baron, A.,; Renard, C.M.G.C.,; Gruppen, H., Interactions between Globular Proteins and Procyanidins of Different Degrees of Polymerization. J. Dairy Sci. 2009, 92, 5843–5853. DOI: 10.3168/jds.2009-2261.
    • (2009) J. Dairy Sci , vol.92 , pp. 5843-5853
    • Prigent, S.V.E.1    Voragen, A.G.2    Van Koningsveld, G.A.3    Baron, A.4    Renard, C.M.G.C.5    Gruppen, H.6
  • 101
    • 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 Funct. 2012, 3, 592–605. DOI: 10.1039/c2fo00006g.
    • (2012) Food Funct , vol.3 , pp. 592-605
    • Bandyopadhyay, P.1    Ghosh, A.K.2    Ghosh, C.3
  • 102
    • 0000484404 scopus 로고
    • Control of Surfactant- Induced Destabilization of Foams through Polyphenol-Mediated Protein-Protein Interactions
    • Sarker, D.K.,; Wilde, P.J.,; Clark, D.C., Control of Surfactant- Induced Destabilization of Foams through Polyphenol-Mediated Protein-Protein Interactions. J. Agric. Food Chem. 1995, 43, 295–300. DOI: 10.1021/jf00050a006.
    • (1995) J. Agric. Food Chem , vol.43 , pp. 295-300
    • Sarker, D.K.1    Wilde, P.J.2    Clark, D.C.3
  • 103
    • 84881520618 scopus 로고    scopus 로고
    • Interactions between Tea Catechins and Casein Micelles and Their Impact on Renneting Functionality
    • Haratifar, S.,; Corredig, M., Interactions between Tea Catechins and Casein Micelles and Their Impact on Renneting Functionality. Food Chem. 2014, 143, 27–32. DOI: 10.1016/j.foodchem.2013.07.092.
    • (2014) Food Chem , vol.143 , pp. 27-32
    • Haratifar, S.1    Corredig, M.2
  • 104
    • 1642308134 scopus 로고    scopus 로고
    • Neurodegenerative Diseases and Oxidative Stress
    • Barnham, K.J.,; Masters, C.L.,; Bush, A.I., Neurodegenerative Diseases and Oxidative Stress. Nat. Rev. Drug Discov. 2004, 3, 205–214. DOI: 10.1038/nrd1330.
    • (2004) Nat. Rev. Drug Discov , vol.3 , pp. 205-214
    • Barnham, K.J.1    Masters, C.L.2    Bush, A.I.3
  • 105
    • 84860520256 scopus 로고    scopus 로고
    • Target Molecules of Food Phytochemicals: Food Science Bound for the Next Dimension
    • Murakami, A.,; Ohniski, K., Target Molecules of Food Phytochemicals: Food Science Bound for the Next Dimension. Food Funct. 2012, 3, 462–476. DOI: 10.1039/c2fo10274a.
    • (2012) Food Funct , vol.3 , pp. 462-476
    • Murakami, A.1    Ohniski, K.2
  • 106
    • 39149145824 scopus 로고    scopus 로고
    • Influence of Milk and Sugar on Antioxidant Potential of Black Tea
    • Sharma, V.,; Kumar, H.V.,; Rao, L.J.M., Influence of Milk and Sugar on Antioxidant Potential of Black Tea. Food Res. Int. 2008, 41, 124–129. DOI: 10.1016/j.foodres.2007.10.009.
    • (2008) Food Res. Int , vol.41 , pp. 124-129
    • Sharma, V.1    Kumar, H.V.2    Rao, L.J.M.3
  • 107
    • 33747097489 scopus 로고    scopus 로고
    • Changes in the Antioxidant Properties of Protein Solutions in the Presence of Epigallocatechin Gallate
    • Almajano, M.P.,; Delgado, M.E.,; Gordon, M.H., Changes in the Antioxidant Properties of Protein Solutions in the Presence of Epigallocatechin Gallate. Food Chem. 2007, 101, 126–130. DOI: 10.1016/j.foodchem.2006.01.009.
    • (2007) Food Chem , vol.101 , pp. 126-130
    • Almajano, M.P.1    Delgado, M.E.2    Gordon, M.H.3
  • 109
    • 74549113852 scopus 로고    scopus 로고
    • Addition of Whole, Semi Skimmed, and Skimmed Bovine Milk Reduces the Total Antioxidant Capacity of Black Tea
    • Ryan, L.,; Petit, S., Addition of Whole, Semi Skimmed, and Skimmed Bovine Milk Reduces the Total Antioxidant Capacity of Black Tea. Nut. Res. 2010, 30, 14–20. DOI: 10.1016/j.nutres.2009.11.005.
    • (2010) Nut. Res , vol.30 , pp. 14-20
    • Ryan, L.1    Petit, S.2
  • 110
    • 77957859387 scopus 로고    scopus 로고
    • Antioxidant and Antimicro Bial Performance of Different Argentinean Green Tea Varieties as Affected by Whey Proteins
    • Von Staszewski, M.V.,; Pilosof, A.M.R.,; Jagus, R.J., Antioxidant and Antimicro Bial Performance of Different Argentinean Green Tea Varieties as Affected by Whey Proteins. Food Chem. 2011, 125, 186–192. DOI: 10.1016/j.foodchem.2010.08.059.
    • (2011) Food Chem , vol.125 , pp. 186-192
    • Von Staszewski, M.V.1    Pilosof, A.M.R.2    Jagus, R.J.3
  • 111
    • 77951631566 scopus 로고    scopus 로고
    • Dual Effect of Milk on the Antioxidant Capacity of Green, Darjeeling, and English Breakfast Teas
    • Dubeau, S.,; Samson, G.,; Tajmir-Riahi, H.-A., Dual Effect of Milk on the Antioxidant Capacity of Green, Darjeeling, and English Breakfast Teas. Food Chem. 2010, 122, 539–545. DOI: 10.1016/j.foodchem.2010.03.005.
    • (2010) Food Chem , vol.122 , pp. 539-545
    • Dubeau, S.1    Samson, G.2    Tajmir-Riahi, H.-A.3
  • 113
    • 84861572761 scopus 로고    scopus 로고
    • Bioactive Composition and Antioxidant Potential of Different Commonly Consumed Coffee Brews Affected by Their Preparation Technique and Milk Addition
    • Niseteo, T.,; Komes, D.,; Belščak-Cvitanović, A.,; Horžić, D.,; Budeč, M., Bioactive Composition and Antioxidant Potential of Different Commonly Consumed Coffee Brews Affected by Their Preparation Technique and Milk Addition. Food Chem. 2012, 134, 1870–1877. DOI: 10.1016/j.foodchem.2012.03.095.
    • (2012) Food Chem , vol.134 , pp. 1870-1877
    • Niseteo, T.1    Komes, D.2    Belščak-Cvitanović, A.3    Horžić, D.4    Budeč, M.5
  • 114
    • 4644229132 scopus 로고    scopus 로고
    • In Vitro Antioxidant Activity of Coffees Brewed Using Different Procedures (Italian, Espresso and Filter)
    • Sanchez-Gonzalez, I.,; Jimenez-Escrig, A.,; Saura-Calixto, F., In Vitro Antioxidant Activity of Coffees Brewed Using Different Procedures (Italian, Espresso and Filter). Food Chem. 2005, 90, 133–139. DOI: 10.1016/j.foodchem.2004.03.037.
    • (2005) Food Chem , vol.90 , pp. 133-139
    • Sanchez-Gonzalez, I.1    Jimenez-Escrig, A.2    Saura-Calixto, F.3
  • 115
    • 33646342275 scopus 로고    scopus 로고
    • Coffee Antioxidant Properties: Effects of Milk Addition and Processing Conditions J
    • Dupas, C.J.,; Marsset-Baglieri, A.C.,; Ordonaud, C.S.,; Ducept, F.M.G.,; Maillard, M.N., Coffee Antioxidant Properties: Effects of Milk Addition and Processing Conditions J. Food Sci. 2006, 71, 253–258. DOI: 10.1111/j.1365-2621.2006.tb15650.x.
    • (2006) Food Sci , vol.71 , pp. 253-258
    • Dupas, C.J.1    Marsset-Baglieri, A.C.2    Ordonaud, C.S.3    Ducept, F.M.G.4    Maillard, M.N.5
  • 116
    • 3242742757 scopus 로고    scopus 로고
    • Antioxidant Activity of Protein-Bound Quercetin
    • Rohn, S.,; Rawel, H.M.,; Kroll, J., Antioxidant Activity of Protein-Bound Quercetin. J. Agric. Food Chem. 2004, 52, 4725–4729. DOI: 10.1021/jf0496797.
    • (2004) J. Agric. Food Chem , vol.52 , pp. 4725-4729
    • Rohn, S.1    Rawel, H.M.2    Kroll, J.3
  • 117
    • 0030062436 scopus 로고    scopus 로고
    • In Vivo Antioxidant Effect of Green and Black Tea in Man
    • Serafini, M.,; Ghiselli, A.,; Ferro-Luzzi, A., In Vivo Antioxidant Effect of Green and Black Tea in Man. Eur. J. Clin. Nutr. 1996, 50, 28–32.
    • (1996) Eur. J. Clin. Nutr , vol.50 , pp. 28-32
    • Serafini, M.1    Ghiselli, A.2    Ferro-Luzzi, A.3
  • 119
    • 0033772557 scopus 로고    scopus 로고
    • Consumption of Black Tea Elicits an Increase in Plasma Antioxidant Potential in Humans
    • Langley-Evans, S.C.,;. Consumption of Black Tea Elicits an Increase in Plasma Antioxidant Potential in Humans. Int. J. Food Sci. Nut. 2000, 51, 309–315. DOI: 10.1080/096374800426902.
    • (2000) Int. J. Food Sci. Nut , vol.51 , pp. 309-315
    • Langley-Evans, S.C.1
  • 120
    • 70349212561 scopus 로고    scopus 로고
    • Studies on Radical Scavenging Activity of Tea Leaves and Effect of Additives on Activities of Black Tea Liquor
    • Muthuiah, M.J.,; Thomas, J.,; Kumar, R.R.,; Mandal, A.K.A., Studies on Radical Scavenging Activity of Tea Leaves and Effect of Additives on Activities of Black Tea Liquor. Int. J. Food Sci. Tech. 2009, 44, 2070–2074. DOI: 10.1111/j.1365-2621.2009.02033.x.
    • (2009) Int. J. Food Sci. Tech , vol.44 , pp. 2070-2074
    • Muthuiah, M.J.1    Thomas, J.2    Kumar, R.R.3    Mandal, A.K.A.4
  • 122
    • 0033975353 scopus 로고    scopus 로고
    • A Single Dose of Tea with or without Milk Increases Plasma Antioxidant Activity in Humans
    • Leenen, R.,; Roodenburg, A.J.C.,; Tijburg, L.B.M.,; Wiseman, S.A., A Single Dose of Tea with or without Milk Increases Plasma Antioxidant Activity in Humans. Eur. J. Clin. Nutr. 2000, 54, 87–92. DOI: 10.1038/sj.ejcn.1600900.
    • (2000) Eur. J. Clin. Nutr , vol.54 , pp. 87-92
    • Leenen, R.1    Roodenburg, A.J.C.2    Tijburg, L.B.M.3    Wiseman, S.A.4
  • 123
    • 23844481777 scopus 로고    scopus 로고
    • Addition of Milk Does Not Alter the Antioxidant Activity of Black Tea
    • Reddy, V.C.,; Vidya Sagar, G.V.,; Sreeramulu, D.,; Venu, L.,; Raghunath, M., Addition of Milk Does Not Alter the Antioxidant Activity of Black Tea. Ann. Nutr. Metab. 2005, 49, 189–195. DOI: 10.1159/000087071.
    • (2005) Ann. Nutr. Metab , vol.49 , pp. 189-195
    • Reddy, V.C.1    Vidya Sagar, G.V.2    Sreeramulu, D.3    Venu, L.4    Raghunath, M.5
  • 124
    • 70350279308 scopus 로고    scopus 로고
    • Influence of Chocolate Matrix Composition on Cocoa Flavan-3-Ol Bioaccessibility in Vitro and Bioavailability in Humans
    • Neilson, A.P.,; George, J.C.,; Janle, E.M.,; Mattes, R.D.,; Rudolph, R.,; Matusheski, N.V.,; Ferruzzi, M.G., Influence of Chocolate Matrix Composition on Cocoa Flavan-3-Ol Bioaccessibility in Vitro and Bioavailability in Humans. J. Agric. Food Chem. 2009, 57, 9418–9426. DOI: 10.1021/jf902919k.
    • (2009) J. Agric. Food Chem , vol.57 , pp. 9418-9426
    • Neilson, A.P.1    George, J.C.2    Janle, E.M.3    Mattes, R.D.4    Rudolph, R.5    Matusheski, N.V.6    Ferruzzi, M.G.7
  • 125
    • 34147126028 scopus 로고    scopus 로고
    • The Effect of Milk Protein on the Bioavailability of Cocoa Polyphenols
    • Keogh, J.B.,; McInerney, J.,; Clifton, P.M., The Effect of Milk Protein on the Bioavailability of Cocoa Polyphenols. J. Food Sci. 2007, 72, 230–233. DOI: 10.1111/j.1750-3841.2007.00314.x.
    • (2007) J. Food Sci , vol.72 , pp. 230-233
    • Keogh, J.B.1    McInerney, J.2    Clifton, P.M.3
  • 128
    • 34250732858 scopus 로고    scopus 로고
    • Effects of Infusion Time and Addition of Milk on Content and Absorption of Polyphenols from Black Tea
    • Kyle, J.A.M.,; Morrice, P.C.,; McNeill, G.,; Duthie, G.G., Effects of Infusion Time and Addition of Milk on Content and Absorption of Polyphenols from Black Tea. J. Agric. Food Chem. 2007, 55, 4889–4894. DOI: 10.1021/jf070351y.
    • (2007) J. Agric. Food Chem , vol.55 , pp. 4889-4894
    • Kyle, J.A.M.1    Morrice, P.C.2    McNeill, G.3    Duthie, G.G.4
  • 129
    • 79960566777 scopus 로고    scopus 로고
    • Effect of Simultaneous Consumption of Milk and Coffee on Chlorogenic Acids’ Bioavailability in Humans
    • Duarte, G.S.,; Farah, A., Effect of Simultaneous Consumption of Milk and Coffee on Chlorogenic Acids’ Bioavailability in Humans. J. Agric. Food Chem. 2011, 59, 7925–7931. DOI: 10.1021/jf201906p.
    • (2011) J. Agric. Food Chem , vol.59 , pp. 7925-7931
    • Duarte, G.S.1    Farah, A.2
  • 130
    • 34948860094 scopus 로고    scopus 로고
    • Common Tea Formulations Modulate in Vitro Digestive Recovery of Green Tea Catechins
    • Green, R.J.,; Murphy, A.S.,; Schulz, B.,; Watkins, B.A.,; Ferruzzi, M.G., Common Tea Formulations Modulate in Vitro Digestive Recovery of Green Tea Catechins. Mol. Nutr. Food Res. 2007, 51, 1152–1162. DOI: 10.1002/(ISSN)1613-4133.
    • (2007) Mol. Nutr. Food Res , vol.51 , pp. 1152-1162
    • Green, R.J.1    Murphy, A.S.2    Schulz, B.3    Watkins, B.A.4    Ferruzzi, M.G.5
  • 131
    • 79960608130 scopus 로고    scopus 로고
    • Effect of Milk and Brewing Method on Black Tea Catechin Bioaccessibility
    • Van Der Burg-Koorevaar, M.C.D.,; Miret, S.,; Duchateau, G.S.M.J.E., Effect of Milk and Brewing Method on Black Tea Catechin Bioaccessibility. J. Agric. Food Chem. 2011, 59, 7752–7758. DOI: 10.1021/jf2015232.
    • (2011) J. Agric. Food Chem , vol.59 , pp. 7752-7758
    • Van Der Burg-Koorevaar, M.C.D.1    Miret, S.2    Duchateau, G.S.M.J.E.3
  • 132
    • 84907821080 scopus 로고    scopus 로고
    • Interaction of Green Tea Polyphenols with Dairy Matrices in a Simulated Gastrointestinal Environment
    • Lamothe, S.,; Azimy, N.,; Bazinet, L.,; Couillard, C.,; Britten, M., Interaction of Green Tea Polyphenols with Dairy Matrices in a Simulated Gastrointestinal Environment. Food Funct. 2014, 5, 2621–2631. DOI: 10.1039/C4FO00203B.
    • (2014) Food Funct , vol.5 , pp. 2621-2631
    • Lamothe, S.1    Azimy, N.2    Bazinet, L.3    Couillard, C.4    Britten, M.5
  • 133
    • 0032803991 scopus 로고    scopus 로고
    • Effects of Phenolic Compounds on the Heat Stability of Milk and Concentrated Milk
    • O’Connell, J.E.,; Fox, P.F., Effects of Phenolic Compounds on the Heat Stability of Milk and Concentrated Milk. J. Dairy Res. 1999, 66, 399–407. DOI: 10.1017/S0022029999003593.
    • (1999) J. Dairy Res , vol.66 , pp. 399-407
    • O’Connell, J.E.1    Fox, P.F.2
  • 134
    • 0032147679 scopus 로고    scopus 로고
    • Effects of Tea, Coffee and Cocoa Extracts on the Colloidal Stability of Milk and Concentrated Milk
    • O’Connell, J.E.,; Fox, P.F.,; Tan-Kintia, R.,; Fox, P.F., Effects of Tea, Coffee and Cocoa Extracts on the Colloidal Stability of Milk and Concentrated Milk. Int. Dairy J. 1998, 8, 689–693. DOI: 10.1016/S0958-6946(98)00105-8.
    • (1998) Int. Dairy J , vol.8 , pp. 689-693
    • O’Connell, J.E.1    Fox, P.F.2    Tan-Kintia, R.3    Fox, P.F.4
  • 135
    • 12344270353 scopus 로고    scopus 로고
    • Inhibition of Key Aroma Compound Generated during Ultrahigh-Temperature Processing of Bovine Milk via Epicatechin Addition
    • Colahan-Sederstrom, P.M.,; Peterson, D.G., Inhibition of Key Aroma Compound Generated during Ultrahigh-Temperature Processing of Bovine Milk via Epicatechin Addition. J. Agric. Food Chem. 2005, 53, 398–402. DOI: 10.1021/jf0487248.
    • (2005) J. Agric. Food Chem , vol.53 , pp. 398-402
    • Colahan-Sederstrom, P.M.1    Peterson, D.G.2
  • 136
    • 84906239581 scopus 로고    scopus 로고
    • Control of Maillard-Type Off-Flavor Development in Ultrahigh-Temperature-Processed Bovine Milk by Phenolic Chemistry
    • Kokkinidou, S.,; Peterson, D.G., Control of Maillard-Type Off-Flavor Development in Ultrahigh-Temperature-Processed Bovine Milk by Phenolic Chemistry. J. Agric. Food Chem. 2014, 62, 8023–8033. DOI: 10.1021/jf501919y.
    • (2014) J. Agric. Food Chem , vol.62 , pp. 8023-8033
    • Kokkinidou, S.1    Peterson, D.G.2
  • 137
    • 78751703604 scopus 로고    scopus 로고
    • Phenolic Fortification of Yogurt Using Grape and Callus Extracts
    • Karaaslan, M.,; Ozden, M.,; Vardin, H.,; Turkoglu, H., Phenolic Fortification of Yogurt Using Grape and Callus Extracts. LWT Food Sci. Technol. 2011, 44, 1065–1072. DOI: 10.1016/j.lwt.2010.12.009.
    • (2011) LWT Food Sci. Technol , vol.44 , pp. 1065-1072
    • Karaaslan, M.1    Ozden, M.2    Vardin, H.3    Turkoglu, H.4
  • 138
    • 84903954374 scopus 로고    scopus 로고
    • Antioxidant Activity and Protein–Polyphenol Interactions in a Pomegranate (Punica Granatum L.) Yogurt
    • Trigueros, L.,; Wojdyło, A.,; Sendra, E., Antioxidant Activity and Protein–Polyphenol Interactions in a Pomegranate (Punica Granatum L.) Yogurt. J. Agric. Food Chem. 2014, 62, 6417–6425. DOI: 10.1021/jf501503h.
    • (2014) J. Agric. Food Chem , vol.62 , pp. 6417-6425
    • Trigueros, L.1    Wojdyło, A.2    Sendra, E.3
  • 139
    • 79959197166 scopus 로고    scopus 로고
    • Physicochemical Properties of Acidified Skim Milk Gels Containing Cocoa Flavanols
    • Vega, C.,; Grover, M.K., Physicochemical Properties of Acidified Skim Milk Gels Containing Cocoa Flavanols. J. Agric. Food Chem. 2011, 59, 6740–6747. DOI: 10.1021/jf200993f.
    • (2011) J. Agric. Food Chem , vol.59 , pp. 6740-6747
    • Vega, C.1    Grover, M.K.2
  • 140
    • 33749507179 scopus 로고    scopus 로고
    • Effect of Tea Phenolics and Their Aromatic Fecal Bacterial Metabolites on Intestinal
    • Lee, H.C.,; Jenner, A.M.,; Low, C.S.,; Lee, Y.K., Effect of Tea Phenolics and Their Aromatic Fecal Bacterial Metabolites on Intestinal. Res. Microbiol. 2006, 157, 876–884. DOI: 10.1016/j.resmic.2006.07.004.
    • (2006) Res. Microbiol , vol.157 , pp. 876-884
    • Lee, H.C.1    Jenner, A.M.2    Low, C.S.3    Lee, Y.K.4
  • 141
    • 70349131990 scopus 로고    scopus 로고
    • Influence of Addition of Raftiline HP® on the Growth, Proteolytic, ACEe and A-Glucosidase Inhibitory Activities of Selected Lactic Acidbacteria and Bifidobacterium
    • Ramchandran, L.,; Shah, N.P., Influence of Addition of Raftiline HP® on the Growth, Proteolytic, ACEe and A-Glucosidase Inhibitory Activities of Selected Lactic Acidbacteria and Bifidobacterium. LWT Food Sci. Technol. 2008, 43, 146–152. DOI: 10.1016/j.lwt.2009.06.022.
    • (2008) LWT Food Sci. Technol , vol.43 , pp. 146-152
    • Ramchandran, L.1    Shah, N.P.2
  • 142
    • 84855873721 scopus 로고    scopus 로고
    • Effect of Hawk Tea (Litsea Coreana L.) On the Numbers of Lactic Acid Bacteria and Flavour Compounds of Yoghurt
    • Ye, M.,; Liu, D.,; Zhang, R.,; Yang, L.,; Wang, J., Effect of Hawk Tea (Litsea Coreana L.) On the Numbers of Lactic Acid Bacteria and Flavour Compounds of Yoghurt. Int. Dairy J. 2012, 23, 68–71. DOI: 10.1016/j.idairyj.2011.09.014.
    • (2012) Int. Dairy J , vol.23 , pp. 68-71
    • Ye, M.1    Liu, D.2    Zhang, R.3    Yang, L.4    Wang, J.5
  • 143
    • 79953028060 scopus 로고    scopus 로고
    • Changes in Yogurt Fermentation Characteristics, and Antioxidant Potential and in Vitro Inhibition of Angiotensin-1 Converting Enzyme upon the Inclusion of Peppermint, Dill and Basil
    • Amirdivani, S.,; Baba, A.S., Changes in Yogurt Fermentation Characteristics, and Antioxidant Potential and in Vitro Inhibition of Angiotensin-1 Converting Enzyme upon the Inclusion of Peppermint, Dill and Basil. LWT Food Sci. Technol. 2011, 44, 1458–1464. DOI: 10.1016/j.lwt.2011.01.019.
    • (2011) LWT Food Sci. Technol , vol.44 , pp. 1458-1464
    • Amirdivani, S.1    Baba, A.S.2
  • 145
    • 84884740686 scopus 로고    scopus 로고
    • Manufacture of Low Fat UF-soft Cheese Supplemented with Rosemary Extract (As Natural Antioxidant)
    • Hala, M.F.,; Ebtisam, E.D.,; Sanaa, I.,; Badran, M.A.,; Marwa, A.S.,; Said, M.E., Manufacture of Low Fat UF-soft Cheese Supplemented with Rosemary Extract (As Natural Antioxidant). J. Am. Sci. 2010, 6, 570–579.
    • (2010) J. Am. Sci , vol.6 , pp. 570-579
    • Hala, M.F.1    Ebtisam, E.D.2    Sanaa, I.3    Badran, M.A.4    Marwa, A.S.5    Said, M.E.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.