메뉴 건너뛰기




Volumn 65, Issue 38, 2017, Pages 8443-8450

Binding of Gallic Acid and Epigallocatechin Gallate to Heat-Unfolded Whey Proteins at Neutral pH Alters Radical Scavenging Activity of in Vitro Protein Digests

Author keywords

binding; heat unfolded whey protein isolate; in vitro digestion; phenolic derivative; synergistic radical scavenging activity

Indexed keywords

BINS; ELECTROPHORESIS;

EID: 85030123065     PISSN: 00218561     EISSN: 15205118     Source Type: Journal    
DOI: 10.1021/acs.jafc.7b03006     Document Type: Article
Times cited : (47)

References (44)
  • 1
    • 0040941720 scopus 로고
    • Uses of milk proteins in formulated foods
    • Hudson, B. J. F. Applied Science Publisers: London
    • Evans, E. W. Uses of milk proteins in formulated foods. In Developments in Food Proteins; Hudson, B. J. F., Ed.; Applied Science Publisers: London, 1982; pp 131.
    • (1982) Developments in Food Proteins , pp. 131
    • Evans, E.W.1
  • 2
    • 0024822645 scopus 로고
    • Proteins in whey: Chemical, physical, and functional properties
    • Kinsella, J. E.; Whitehead, D. M. Proteins in whey: chemical, physical, and functional properties Adv. Food Nutr. Res. 1989, 33, 343-438 10.1016/S1043-4526(08)60130-8
    • (1989) Adv. Food Nutr. Res. , vol.33 , pp. 343-438
    • Kinsella, J.E.1    Whitehead, D.M.2
  • 3
    • 35348981282 scopus 로고    scopus 로고
    • Bovine whey proteins - Overview on their main biological properties
    • Madureira, A. R.; Pereira, C. I.; Gomes, A. M.; Pintado, M. E.; Malcata, F. X. Bovine whey proteins-overview on their main biological properties Food Res. Int. 2007, 40, 1197-1211 10.1016/j.foodres.2007.07.005
    • (2007) Food Res. Int. , vol.40 , pp. 1197-1211
    • Madureira, A.R.1    Pereira, C.I.2    Gomes, A.M.3    Pintado, M.E.4    Malcata, F.X.5
  • 4
    • 3042686006 scopus 로고    scopus 로고
    • Therapeutic applications of whey protein
    • Keri Marshall, N. D. Therapeutic applications of whey protein Altern. Med. Rev. 2004, 9, 136-156
    • (2004) Altern. Med. Rev. , vol.9 , pp. 136-156
    • Keri Marshall, N.D.1
  • 6
    • 33644928754 scopus 로고    scopus 로고
    • Green tea and its polyphenolic catechins: Medicinal uses in cancer and noncancer applications
    • Zaveri, N. T. Green tea and its polyphenolic catechins: medicinal uses in cancer and noncancer applications Life Sci. 2006, 78, 2073-2080 10.1016/j.lfs.2005.12.006
    • (2006) Life Sci. , vol.78 , pp. 2073-2080
    • Zaveri, N.T.1
  • 7
    • 84857382394 scopus 로고    scopus 로고
    • Interactions between polyphenols and macromolecules: Quantification methods and mechanisms
    • Le Bourvellec, C.; Renard, C. Interactions between polyphenols and macromolecules: quantification methods and mechanisms Crit. Rev. Food Sci. Nutr. 2012, 52, 213-248 10.1080/10408398.2010.499808
    • (2012) Crit. Rev. Food Sci. Nutr. , vol.52 , pp. 213-248
    • Le Bourvellec, C.1    Renard, C.2
  • 8
    • 15444362256 scopus 로고    scopus 로고
    • Anthocyanin antioxidant activity and partition behavior in whey protein emulsion
    • Viljanen, K.; Kylli, P.; Hubbermann, E.-M.; Schwarz, K.; Heinonen, M. Anthocyanin antioxidant activity and partition behavior in whey protein emulsion J. Agric. Food Chem. 2005, 53, 2022-2027 10.1021/jf047975d
    • (2005) J. Agric. Food Chem. , vol.53 , pp. 2022-2027
    • Viljanen, K.1    Kylli, P.2    Hubbermann, E.-M.3    Schwarz, K.4    Heinonen, M.5
  • 9
    • 20844443677 scopus 로고    scopus 로고
    • Binding of selected phenolic compounds to proteins
    • Rawel, H. M.; Meidtner, K.; Kroll, J. Binding of selected phenolic compounds to proteins J. Agric. Food Chem. 2005, 53, 4228-4235 10.1021/jf0480290
    • (2005) J. Agric. Food Chem. , vol.53 , pp. 4228-4235
    • Rawel, H.M.1    Meidtner, K.2    Kroll, J.3
  • 10
    • 0042387727 scopus 로고    scopus 로고
    • Influence of a sugar moiety (rhamnosylglucoside) at 3-O position on the reactivity of quercetin with whey proteins
    • Rawel, H. M.; Rohn, S.; Kroll, J. Influence of a sugar moiety (rhamnosylglucoside) at 3-O position on the reactivity of quercetin with whey proteins Int. J. Biol. Macromol. 2003, 32, 109-120 10.1016/S0141-8130(03)00044-8
    • (2003) Int. J. Biol. Macromol. , vol.32 , pp. 109-120
    • Rawel, H.M.1    Rohn, S.2    Kroll, J.3
  • 11
    • 85010911748 scopus 로고    scopus 로고
    • Interaction of whey proteins with phenolic derivatives under neutral and acidic pH conditions
    • Cao, Y.; Xiong, Y. L. Interaction of whey proteins with phenolic derivatives under neutral and acidic pH conditions J. Food Sci. 2017, 82, 409-419 10.1111/1750-3841.13607
    • (2017) J. Food Sci. , vol.82 , pp. 409-419
    • Cao, Y.1    Xiong, Y.L.2
  • 12
    • 84890032864 scopus 로고    scopus 로고
    • The impact of whey protein preheating on the properties of emulsion gel bead
    • Ruffin, E.; Schmit, T.; Lafitte, G.; Dollat, J.-M.; Chambin, O. The impact of whey protein preheating on the properties of emulsion gel bead Food Chem. 2014, 151, 324-332 10.1016/j.foodchem.2013.11.071
    • (2014) Food Chem. , vol.151 , pp. 324-332
    • Ruffin, E.1    Schmit, T.2    Lafitte, G.3    Dollat, J.-M.4    Chambin, O.5
  • 13
    • 84864773121 scopus 로고    scopus 로고
    • Effects of thermal denaturation on binding between bixin and whey protein
    • Zhang, Y.; Zhong, Q. Effects of thermal denaturation on binding between bixin and whey protein J. Agric. Food Chem. 2012, 60, 7526-7531 10.1021/jf3021656
    • (2012) J. Agric. Food Chem. , vol.60 , pp. 7526-7531
    • Zhang, Y.1    Zhong, Q.2
  • 14
    • 84988038617 scopus 로고    scopus 로고
    • Stability improvement of natural food colors: Impact of amino acid and peptide addition on anthocyanin stability in model beverages
    • Chung, C.; Rojanasasithara, T.; Mutilangi, W.; McClements, D. J. Stability improvement of natural food colors: impact of amino acid and peptide addition on anthocyanin stability in model beverages Food Chem. 2017, 218, 277-284 10.1016/j.foodchem.2016.09.087
    • (2017) Food Chem. , vol.218 , pp. 277-284
    • Chung, C.1    Rojanasasithara, T.2    Mutilangi, W.3    McClements, D.J.4
  • 15
    • 84936802233 scopus 로고    scopus 로고
    • Enhanced stability of anthocyanin-based color in model beverage systems through whey protein isolate complexation
    • Chung, C.; Rojanasasithara, T.; Mutilangi, W.; McClements, D. J. Enhanced stability of anthocyanin-based color in model beverage systems through whey protein isolate complexation Food Res. Int. 2015, 76, 761-768 10.1016/j.foodres.2015.07.003
    • (2015) Food Res. Int. , vol.76 , pp. 761-768
    • Chung, C.1    Rojanasasithara, T.2    Mutilangi, W.3    McClements, D.J.4
  • 16
    • 84888440371 scopus 로고    scopus 로고
    • Green tea extract: Chemistry, antioxidant properties and food applications - A review
    • Senanayake, S. N. Green tea extract: chemistry, antioxidant properties and food applications-a review J. Funct. Foods 2013, 5, 1529-1541 10.1016/j.jff.2013.08.011
    • (2013) J. Funct. Foods , vol.5 , pp. 1529-1541
    • Senanayake, S.N.1
  • 18
    • 0001146740 scopus 로고    scopus 로고
    • Characterization of (+)-catechin- acetaldehyde polymers: A model for colloidal state of wine polyphenols
    • Saucier, C.; Bourgeois, G.; Vitry, C.; Roux, D.; Glories, Y. Characterization of (+)-catechin- acetaldehyde polymers: a model for colloidal state of wine polyphenols J. Agric. Food Chem. 1997, 45, 1045-1049 10.1021/jf960597v
    • (1997) J. Agric. Food Chem. , vol.45 , pp. 1045-1049
    • Saucier, C.1    Bourgeois, G.2    Vitry, C.3    Roux, D.4    Glories, Y.5
  • 19
    • 0015907980 scopus 로고
    • Quenching of fluorescence by oxygen. A probe for structural fluctuations in macromolecules
    • Lakowicz, J. R.; Weber, G. Quenching of fluorescence by oxygen. A probe for structural fluctuations in macromolecules Biochemistry 1973, 12, 4161-4170 10.1021/bi00745a020
    • (1973) Biochemistry , vol.12 , pp. 4161-4170
    • Lakowicz, J.R.1    Weber, G.2
  • 20
    • 84875240763 scopus 로고    scopus 로고
    • A review on protein-phenolic interactions and associated changes
    • Ozdal, T.; Capanoglu, E.; Altay, F. A review on protein-phenolic interactions and associated changes Food Res. Int. 2013, 51, 954-970 10.1016/j.foodres.2013.02.009
    • (2013) Food Res. Int. , vol.51 , pp. 954-970
    • Ozdal, T.1    Capanoglu, E.2    Altay, F.3
  • 21
    • 85032119438 scopus 로고
    • Determination of SH- and SS-groups in some food proteins using Ellman's reagent
    • Beveridge, T.; Toma, S.; Nakai, S. Determination of SH- and SS-groups in some food proteins using Ellman's reagent J. Food Sci. 1974, 39, 49-51 10.1111/j.1365-2621.1974.tb00984.x
    • (1974) J. Food Sci. , vol.39 , pp. 49-51
    • Beveridge, T.1    Toma, S.2    Nakai, S.3
  • 22
    • 34248679167 scopus 로고    scopus 로고
    • Tricine-SDS-PAGE
    • Schägger, H. Tricine-SDS-PAGE Nat. Protoc. 2006, 1, 16-22 10.1038/nprot.2006.4
    • (2006) Nat. Protoc. , vol.1 , pp. 16-22
    • Schägger, H.1
  • 23
    • 0032982508 scopus 로고    scopus 로고
    • Antioxidant activity applying an improved ABTS radical cation decolorization assay
    • Re, R.; Pellegrini, N.; Proteggente, A.; Pannala, A.; Yang, M.; Rice-Evans, C. Antioxidant activity applying an improved ABTS radical cation decolorization assay Free Radical Biol. Med. 1999, 26, 1231-1237 10.1016/S0891-5849(98)00315-3
    • (1999) Free Radical Biol. Med. , vol.26 , pp. 1231-1237
    • Re, R.1    Pellegrini, N.2    Proteggente, A.3    Pannala, A.4    Yang, M.5    Rice-Evans, C.6
  • 24
    • 0028307238 scopus 로고
    • Deoxyribose assay for detecting hydroxyl radicals
    • Aruoma, O. I. Deoxyribose assay for detecting hydroxyl radicals Methods Enzymol. 1994, 233, 57-66 10.1016/S0076-6879(94)33008-5
    • (1994) Methods Enzymol. , vol.233 , pp. 57-66
    • Aruoma, O.I.1
  • 25
    • 33644969880 scopus 로고    scopus 로고
    • Antioxidant activity of hot water extract from the fruit of the Doum palm
    • Hsu, B.; Coupar, I. M.; Ng, K. Antioxidant activity of hot water extract from the fruit of the Doum palm Food Chem. 2006, 98, 317-328 10.1016/j.foodchem.2005.05.077
    • (2006) Food Chem. , vol.98 , pp. 317-328
    • Hsu, B.1    Coupar, I.M.2    Ng, K.3
  • 26
    • 33751158541 scopus 로고
    • Heat-induced conformational changes in whey protein isolate and its relation to foaming properties
    • Zhu, H.; Damodaran, S. Heat-induced conformational changes in whey protein isolate and its relation to foaming properties J. Agric. Food Chem. 1994, 42, 846-855 10.1021/jf00040a002
    • (1994) J. Agric. Food Chem. , vol.42 , pp. 846-855
    • Zhu, H.1    Damodaran, S.2
  • 27
    • 84861429878 scopus 로고    scopus 로고
    • Effect of microbial transglutaminase treatment on thermal stability and pH-solubility of heat-shocked whey protein isolate
    • Damodaran, S.; Agyare, K. K. Effect of microbial transglutaminase treatment on thermal stability and pH-solubility of heat-shocked whey protein isolate Food Hydrocolloids 2013, 30, 12-18 10.1016/j.foodhyd.2012.04.012
    • (2013) Food Hydrocolloids , vol.30 , pp. 12-18
    • Damodaran, S.1    Agyare, K.K.2
  • 28
    • 65249156463 scopus 로고    scopus 로고
    • Functional properties of whey proteins affected by heat treatment and hydrodynamic high-pressure shearing
    • Dissanayake, M.; Vasiljevic, T. Functional properties of whey proteins affected by heat treatment and hydrodynamic high-pressure shearing J. Dairy Sci. 2009, 92, 1387-1397 10.3168/jds.2008-1791
    • (2009) J. Dairy Sci. , vol.92 , pp. 1387-1397
    • Dissanayake, M.1    Vasiljevic, T.2
  • 29
    • 0000008540 scopus 로고    scopus 로고
    • Thermal unfolding of β-lactoglobulin: Characterization of initial unfolding events responsible for heat-induced aggregation
    • Prabakaran, S.; Damodaran, S. Thermal unfolding of β-lactoglobulin: characterization of initial unfolding events responsible for heat-induced aggregation J. Agric. Food Chem. 1997, 45, 4303-4308 10.1021/jf970269a
    • (1997) J. Agric. Food Chem. , vol.45 , pp. 4303-4308
    • Prabakaran, S.1    Damodaran, S.2
  • 30
    • 84950139191 scopus 로고    scopus 로고
    • Binding of an oligomeric ellagitannin series to bovine serum albumin (BSA): Analysis by isothermal titration calorimetry (ITC)
    • Karonen, M.; Oraviita, M.; Mueller-Harvey, I.; Salminen, J.-P.; Green, R. J. Binding of an oligomeric ellagitannin series to bovine serum albumin (BSA): analysis by isothermal titration calorimetry (ITC) J. Agric. Food Chem. 2015, 63, 10647-10654 10.1021/acs.jafc.5b04843
    • (2015) J. Agric. Food Chem. , vol.63 , pp. 10647-10654
    • Karonen, M.1    Oraviita, M.2    Mueller-Harvey, I.3    Salminen, J.-P.4    Green, R.J.5
  • 31
    • 84924811310 scopus 로고    scopus 로고
    • Probing the binding of (+)-catechin to bovine serum albumin by isothermal titration calorimetry and spectroscopic techniques
    • Li, X.; Hao, Y. Probing the binding of (+)-catechin to bovine serum albumin by isothermal titration calorimetry and spectroscopic techniques J. Mol. Struct. 2015, 1091, 109-117 10.1016/j.molstruc.2015.02.082
    • (2015) J. Mol. Struct. , vol.1091 , pp. 109-117
    • Li, X.1    Hao, Y.2
  • 32
    • 84950143102 scopus 로고    scopus 로고
    • Effect of covalent modification by (-)-epigallocatechin-3-gallate on physicochemical and functional properties of whey protein isolate
    • Jia, Z.; Zheng, M.; Tao, F.; Chen, W.; Huang, G.; Jiang, J. Effect of covalent modification by (-)-epigallocatechin-3-gallate on physicochemical and functional properties of whey protein isolate LWT-Food Sci. Technol. 2016, 66, 305-310 10.1016/j.lwt.2015.10.054
    • (2016) LWT-Food Sci. Technol. , vol.66 , pp. 305-310
    • Jia, Z.1    Zheng, M.2    Tao, F.3    Chen, W.4    Huang, G.5    Jiang, J.6
  • 33
    • 84897932868 scopus 로고    scopus 로고
    • Effects of rutin incorporation on the physical and oxidative stability of soy protein-stabilized emulsions
    • Cui, Z.; Kong, X.; Chen, Y.; Zhang, C.; Hua, Y. Effects of rutin incorporation on the physical and oxidative stability of soy protein-stabilized emulsions Food Hydrocolloids 2014, 41, 1-9 10.1016/j.foodhyd.2014.03.006
    • (2014) Food Hydrocolloids , vol.41 , pp. 1-9
    • Cui, Z.1    Kong, X.2    Chen, Y.3    Zhang, C.4    Hua, Y.5
  • 35
    • 84976640044 scopus 로고    scopus 로고
    • Effect of the structure of gallic acid and its derivatives on their interaction with plant ferritin
    • Wang, Q.; Zhou, K.; Ning, Y.; Zhao, G. Effect of the structure of gallic acid and its derivatives on their interaction with plant ferritin Food Chem. 2016, 213, 260-267 10.1016/j.foodchem.2016.06.085
    • (2016) Food Chem. , vol.213 , pp. 260-267
    • Wang, Q.1    Zhou, K.2    Ning, Y.3    Zhao, G.4
  • 36
    • 79951954922 scopus 로고    scopus 로고
    • Green tea polyphenol epigallocatechin-3-gallate (EGCG) induced intermolecular cross-linking of membrane proteins
    • Chen, R.; Wang, J.-B.; Zhang, X.-Q.; Ren, J.; Zeng, C.-M. Green tea polyphenol epigallocatechin-3-gallate (EGCG) induced intermolecular cross-linking of membrane proteins Arch. Biochem. Biophys. 2011, 507, 343-349 10.1016/j.abb.2010.12.033
    • (2011) Arch. Biochem. Biophys. , vol.507 , pp. 343-349
    • Chen, R.1    Wang, J.-B.2    Zhang, X.-Q.3    Ren, J.4    Zeng, C.-M.5
  • 37
    • 0032483094 scopus 로고    scopus 로고
    • Retinol and retinoic acid bind to a surface cleft in bovine β-lactoglobulin: A method of binding site determination using fluorescence resonance energy transfer
    • Lange, D. C.; Kothari, R.; Patel, R. C.; Patel, S. C. Retinol and retinoic acid bind to a surface cleft in bovine β-lactoglobulin: a method of binding site determination using fluorescence resonance energy transfer Biophys. Chem. 1998, 74, 45-51 10.1016/S0301-4622(98)00164-1
    • (1998) Biophys. Chem. , vol.74 , pp. 45-51
    • Lange, D.C.1    Kothari, R.2    Patel, R.C.3    Patel, S.C.4
  • 38
    • 84966330726 scopus 로고    scopus 로고
    • Dual role (anti-and pro-oxidant) of gallic acid in mediating myofibrillar protein gelation and gel in vitro digestion
    • Cao, Y.; True, A. D.; Chen, J.; Xiong, Y. L. Dual role (anti-and pro-oxidant) of gallic acid in mediating myofibrillar protein gelation and gel in vitro digestion J. Agric. Food Chem. 2016, 64, 3054-3061 10.1021/acs.jafc.6b00314
    • (2016) J. Agric. Food Chem. , vol.64 , pp. 3054-3061
    • Cao, Y.1    True, A.D.2    Chen, J.3    Xiong, Y.L.4
  • 39
    • 0001406422 scopus 로고    scopus 로고
    • Interactions between α-lactalbumin and β-lactoglobulin in the early stages of heat denaturation
    • Dalgleish, D. G.; Senaratne, V.; Francois, S. Interactions between α-lactalbumin and β-lactoglobulin in the early stages of heat denaturation J. Agric. Food Chem. 1997, 45, 3459-3464 10.1021/jf970113a
    • (1997) J. Agric. Food Chem. , vol.45 , pp. 3459-3464
    • Dalgleish, D.G.1    Senaratne, V.2    Francois, S.3
  • 40
    • 0034768130 scopus 로고    scopus 로고
    • Characterization of heat-induced aggregates of β-lactoglobulin, α-lactalbumin and bovine serum albumin in a whey protein concentrate environment
    • Havea, P.; Singh, H.; Creamer, L. K. Characterization of heat-induced aggregates of β-lactoglobulin, α-lactalbumin and bovine serum albumin in a whey protein concentrate environment J. Dairy Res. 2001, 68, 483-497 10.1017/S0022029901004964
    • (2001) J. Dairy Res. , vol.68 , pp. 483-497
    • Havea, P.1    Singh, H.2    Creamer, L.K.3
  • 41
    • 36549031664 scopus 로고    scopus 로고
    • Identification of intra- and intermolecular disulphide bonding in the plant mitochondrial proteome by diagonal gel electrophoresis
    • Winger, A. M.; Taylor, N. L.; Heazlewood, J. L.; Day, D. A.; Millar, A. H. Identification of intra- and intermolecular disulphide bonding in the plant mitochondrial proteome by diagonal gel electrophoresis Proteomics 2007, 7, 4158-4170 10.1002/pmic.200700209
    • (2007) Proteomics , vol.7 , pp. 4158-4170
    • Winger, A.M.1    Taylor, N.L.2    Heazlewood, J.L.3    Day, D.A.4    Millar, A.H.5
  • 42
    • 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. Macromol. 2012, 51, 774-782 10.1016/j.ijbiomac.2012.07.010
    • (2012) Int. J. Biol. Macromol. , vol.51 , pp. 774-782
    • Prodpran, T.1    Benjakul, S.2    Phatcharat, S.3
  • 43
    • 74549113852 scopus 로고    scopus 로고
    • Addition of whole, semiskimmed, and skimmed bovine milk reduces the total antioxidant capacity of black tea
    • Ryan, L.; Petit, S. Addition of whole, semiskimmed, and skimmed bovine milk reduces the total antioxidant capacity of black tea Nutr. Res. (NY, U.S.A.) 2010, 30, 14-20 10.1016/j.nutres.2009.11.005
    • (2010) Nutr. Res. (NY, U.S.A.) , vol.30 , pp. 14-20
    • Ryan, L.1    Petit, S.2
  • 44
    • 84883692206 scopus 로고    scopus 로고
    • Synergistic inhibition of lipid oxidation by pea protein hydrolysate coupled with licorice extract in a liposomal model system
    • Zhang, X.; Xiong, Y. L.; Chen, J.; Zhou, L. Synergistic inhibition of lipid oxidation by pea protein hydrolysate coupled with licorice extract in a liposomal model system J. Agric. Food Chem. 2013, 61, 8452-8461 10.1021/jf402256k
    • (2013) J. Agric. Food Chem. , vol.61 , pp. 8452-8461
    • Zhang, X.1    Xiong, Y.L.2    Chen, J.3    Zhou, L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.