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Volumn 98, Issue 15, 2018, Pages 5683-5689

Covalent modification of soy protein isolate by (−)-epigallocatechin-3-gallate: effects on structural and emulsifying properties

Author keywords

( ) Epigallocatechin 3 gallate; covalent modification; emulsifying property; soy protein isolate

Indexed keywords

CATECHIN; EPIGALLOCATECHIN GALLATE; SOYBEAN PROTEIN;

EID: 85056234047     PISSN: 00225142     EISSN: 10970010     Source Type: Journal    
DOI: 10.1002/jsfa.9114     Document Type: Article
Times cited : (53)

References (41)
  • 1
    • 69949133381 scopus 로고    scopus 로고
    • Stable oil-in-water emulsions prepared from soy protein-dextran conjugates
    • Xu K and Yao P, Stable oil-in-water emulsions prepared from soy protein-dextran conjugates. Langmuir 25:9714–9720 (2009).
    • (2009) Langmuir , vol.25 , pp. 9714-9720
    • Xu, K.1    Yao, P.2
  • 2
    • 84878310546 scopus 로고    scopus 로고
    • Food proteins: a review on their emulsifying properties using a structure-function approach
    • Lam RSH and Nickerson MT, Food proteins: a review on their emulsifying properties using a structure-function approach. Food Chem 141:975–984 (2013).
    • (2013) Food Chem , vol.141 , pp. 975-984
    • Lam, R.S.H.1    Nickerson, M.T.2
  • 3
    • 0030265397 scopus 로고    scopus 로고
    • Polymerization of soy protein digests by microbial transglutaminase for improvement of the functional properties
    • Babiker EFE, Khan MAS, Matsudomi N and Kato A, Polymerization of soy protein digests by microbial transglutaminase for improvement of the functional properties. Food Res Int 29:627–634 (1996).
    • (1996) Food Res Int , vol.29 , pp. 627-634
    • Babiker, E.F.E.1    Khan, M.A.S.2    Matsudomi, N.3    Kato, A.4
  • 4
    • 34447644031 scopus 로고    scopus 로고
    • Porphyran as a functional modifier of a soybean protein isolate through conjugation by the maillard reaction
    • Takano K, Hattori M, Yoshida T, Kanuma S and Takahashi K, Porphyran as a functional modifier of a soybean protein isolate through conjugation by the maillard reaction. J Agric Food Chem 55:5796–5802 (2007).
    • (2007) J Agric Food Chem , vol.55 , pp. 5796-5802
    • Takano, K.1    Hattori, M.2    Yoshida, T.3    Kanuma, S.4    Takahashi, K.5
  • 5
    • 84959883759 scopus 로고    scopus 로고
    • Improved emulsifying capabilities of hydrolysates of soy protein isolate pretreated with high pressure microfluidization
    • Chen L, Chen J, Yu L and Wu K, Improved emulsifying capabilities of hydrolysates of soy protein isolate pretreated with high pressure microfluidization. LWT-Food Sci Technol 69:1–8 (2016).
    • (2016) LWT-Food Sci Technol , vol.69 , pp. 1-8
    • Chen, L.1    Chen, J.2    Yu, L.3    Wu, K.4
  • 6
    • 0034807826 scopus 로고    scopus 로고
    • Dietary agents in cancer prevention: flavonoids and isoflavonoids
    • Birt DF, Hendrich S and Wang W, Dietary agents in cancer prevention: flavonoids and isoflavonoids. Pharmacol Therap 90:157–177 (2001).
    • (2001) Pharmacol Therap , vol.90 , pp. 157-177
    • Birt, D.F.1    Hendrich, S.2    Wang, W.3
  • 7
    • 77957896043 scopus 로고    scopus 로고
    • Encapsulation of polyphenols-a review
    • Fang Z and Bhandari B, Encapsulation of polyphenols-a review. Trends Food Sci Technol 21:510–523 (2010).
    • (2010) Trends Food Sci Technol , vol.21 , pp. 510-523
    • Fang, Z.1    Bhandari, B.2
  • 8
    • 85019985337 scopus 로고    scopus 로고
    • Black carrot (Daucus carota L.), dietary and health promoting perspectives of its polyphenols: a review
    • Akhtar S, Rauf A, Imran M, Qamar M, Riaz M and Mubarak MS, Black carrot (Daucus carota L.), dietary and health promoting perspectives of its polyphenols: a review. Trends Food Sci Technol 66:36–47 (2010).
    • (2010) Trends Food Sci Technol , vol.66 , pp. 36-47
    • Akhtar, S.1    Rauf, A.2    Imran, M.3    Qamar, M.4    Riaz, M.5    Mubarak, M.S.6
  • 9
    • 20844443677 scopus 로고    scopus 로고
    • Binding of selected phenolic compounds to proteins
    • Rawel HM, Meidtner K and Kroll J, Binding of selected phenolic compounds to proteins. J Agric Food Chem 53:4228–4235 (2005).
    • (2005) J Agric Food Chem , vol.53 , pp. 4228-4235
    • Rawel, H.M.1    Meidtner, K.2    Kroll, J.3
  • 10
    • 70350237026 scopus 로고    scopus 로고
    • Catechol type polyphenol is a potential modifier of protein Sulfhydryls: development and application of a new probe for understanding the dietary polyphenol actions
    • Ishii T, Ishikawa M, Miyoshi N, Yasunaga M, Akagawa M, Uchida K et al., Catechol type polyphenol is a potential modifier of protein Sulfhydryls: development and application of a new probe for understanding the dietary polyphenol actions. Chem Res Toxicol 22:1689–1698 (2005).
    • (2005) Chem Res Toxicol , vol.22 , pp. 1689-1698
    • Ishii, T.1    Ishikawa, M.2    Miyoshi, N.3    Yasunaga, M.4    Akagawa, M.5    Uchida, K.6
  • 11
    • 84888228349 scopus 로고    scopus 로고
    • Covalent complexation and functional evaluation of (−)-epigallocatechin gallate and α-lactalbumin
    • Wang X, Zhang J, Lei F, Liang C, Yuan F and Gao Y, Covalent complexation and functional evaluation of (−)-epigallocatechin gallate and α-lactalbumin. Food Chem 150:341–347 (2014).
    • (2014) Food Chem , vol.150 , pp. 341-347
    • Wang, X.1    Zhang, J.2    Lei, F.3    Liang, C.4    Yuan, F.5    Gao, Y.6
  • 12
    • 79955466143 scopus 로고    scopus 로고
    • (−)-Epigallocatechin-3-gallate suppresses growth of AZ521 human gastric cancer cells by targeting the DEAD-box RNA helicase p68
    • Tanaka T, Ishii T, Mizuno D, Mori T, Yamaji R, Nakamura Y et al., (−)-Epigallocatechin-3-gallate suppresses growth of AZ521 human gastric cancer cells by targeting the DEAD-box RNA helicase p68. Free Radical Biol Med 50:1324–1335 (2011).
    • (2011) Free Radical Biol Med , vol.50 , pp. 1324-1335
    • Tanaka, T.1    Ishii, T.2    Mizuno, D.3    Mori, T.4    Yamaji, R.5    Nakamura, Y.6
  • 13
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK, Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680–685 (1970).
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 14
    • 79952758423 scopus 로고    scopus 로고
    • Effects of ultrasound pretreatment on the enzymatic hydrolysis of soy protein isolates and on the emulsifying properties of hydrolysates
    • Chen L, Chen J, Ren J and Zhao M, Effects of ultrasound pretreatment on the enzymatic hydrolysis of soy protein isolates and on the emulsifying properties of hydrolysates. J Agric Food Chem 59:2600–2609 (2011).
    • (2011) J Agric Food Chem , vol.59 , pp. 2600-2609
    • Chen, L.1    Chen, J.2    Ren, J.3    Zhao, M.4
  • 15
    • 0019331914 scopus 로고
    • Hydrophobicity determined by a fluorescence probe method and its correlation with surface properties of proteins
    • Kato A and Nakai S, Hydrophobicity determined by a fluorescence probe method and its correlation with surface properties of proteins. BBA-Protein Struct 624:13–20 (1980).
    • (1980) BBA-Protein Struct , vol.624 , pp. 13-20
    • Kato, A.1    Nakai, S.2
  • 16
    • 84995390613 scopus 로고    scopus 로고
    • Multilevel structural responses of β-conglycinin and glycinin under acidic or alkaline heat treatment
    • Xiao J, Shi C, Zhang L, Li Y, Qi J, Wang Y et al., Multilevel structural responses of β-conglycinin and glycinin under acidic or alkaline heat treatment. Food Res Int 89:540–548 (2016).
    • (2016) Food Res Int , vol.89 , pp. 540-548
    • Xiao, J.1    Shi, C.2    Zhang, L.3    Li, Y.4    Qi, J.5    Wang, Y.6
  • 17
    • 11144219949 scopus 로고    scopus 로고
    • Structure-physicochemical functioan relationships of soybean glycinin at subunit levels assessed by using mutant lines
    • Maruyama M, Prak K, Kotoyama S, Choi S, Yagasagi K, Ishomoto M et al., Structure-physicochemical functioan relationships of soybean glycinin at subunit levels assessed by using mutant lines. J Agric Food Chem 52:8197–8201 (2004).
    • (2004) J Agric Food Chem , vol.52 , pp. 8197-8201
    • Maruyama, M.1    Prak, K.2    Kotoyama, S.3    Choi, S.4    Yagasagi, K.5    Ishomoto, M.6
  • 18
    • 54349099430 scopus 로고    scopus 로고
    • Covalent modification of proteins by green tea polyphenol (−)-epigallocatechin-3-gallate through autoxidation
    • Ishii T, Mori T, Tanaka T, Mizuno D, Yamaji R, Kumazawa S et al., Covalent modification of proteins by green tea polyphenol (−)-epigallocatechin-3-gallate through autoxidation. Free Radical Biol Med 45:1384–1394 (2008).
    • (2008) Free Radical Biol Med , vol.45 , pp. 1384-1394
    • Ishii, T.1    Mori, T.2    Tanaka, T.3    Mizuno, D.4    Yamaji, R.5    Kumazawa, S.6
  • 19
    • 84919799018 scopus 로고    scopus 로고
    • Evaluation of structural and functional properties of protein-EGCG complexes and their ability of stabilizing a model β-carotene emulsion
    • Wei Z, Yang W, Fan R, Yuan F and Gao Y, Evaluation of structural and functional properties of protein-EGCG complexes and their ability of stabilizing a model β-carotene emulsion. Food Hydrocolloid 45:337–350 (2015).
    • (2015) Food Hydrocolloid , vol.45 , pp. 337-350
    • Wei, Z.1    Yang, W.2    Fan, R.3    Yuan, F.4    Gao, Y.5
  • 20
    • 84888203053 scopus 로고    scopus 로고
    • Purification and characterization of a stable Kunitz trypsin inhibitor from Trigonella foenum-graecum (fenugreek) seeds
    • Oddepally R, Sriram G and Guruprasad L, Purification and characterization of a stable Kunitz trypsin inhibitor from Trigonella foenum-graecum (fenugreek) seeds. Phytochemistry 96:26–36 (2013).
    • (2013) Phytochemistry , vol.96 , pp. 26-36
    • Oddepally, R.1    Sriram, G.2    Guruprasad, L.3
  • 21
    • 79955086146 scopus 로고    scopus 로고
    • Physical properties, molecular structures, and protein quality of texturized whey protein isolate: effect of extrusion temperature
    • Qi PX and Onwulata CI, Physical properties, molecular structures, and protein quality of texturized whey protein isolate: effect of extrusion temperature. J Agric Food Chem 59:4668–4675 (2011).
    • (2011) J Agric Food Chem , vol.59 , pp. 4668-4675
    • Qi, P.X.1    Onwulata, C.I.2
  • 22
    • 84918816295 scopus 로고    scopus 로고
    • Concentration-dependent reversible self-Oligomerization of serum albumins through intermolecular β-sheet formation
    • Bhattacharya A, Prajapati R, Chatterjee S and Mukherjee TK, Concentration-dependent reversible self-Oligomerization of serum albumins through intermolecular β-sheet formation. Langmuir 30:14894–14904 (2014).
    • (2014) Langmuir , vol.30 , pp. 14894-14904
    • Bhattacharya, A.1    Prajapati, R.2    Chatterjee, S.3    Mukherjee, T.K.4
  • 23
    • 84871724197 scopus 로고    scopus 로고
    • The effects of limited enzymatic hydrolysis on the physicochemical and emulsifying properties of a lentil protein isolate
    • Avramenko NA, Low NH and Nickerson MT, The effects of limited enzymatic hydrolysis on the physicochemical and emulsifying properties of a lentil protein isolate. Food Res Int 51:162–169 (2013).
    • (2013) Food Res Int , vol.51 , pp. 162-169
    • Avramenko, N.A.1    Low, N.H.2    Nickerson, M.T.3
  • 24
    • 84862573582 scopus 로고    scopus 로고
    • Structural changes imposed on whey proteins by UV irradiation in a continuous UV light reactor
    • Kristo E, Hazizaj A and Corredig M, Structural changes imposed on whey proteins by UV irradiation in a continuous UV light reactor. J Agric Food Chem 60:6204–6209 (2012).
    • (2012) J Agric Food Chem , vol.60 , pp. 6204-6209
    • Kristo, E.1    Hazizaj, A.2    Corredig, M.3
  • 25
    • 70349096756 scopus 로고    scopus 로고
    • Structural modification of soy protein by the lipid peroxidation product acrolein
    • Wu W, Wu X and Hua Y, Structural modification of soy protein by the lipid peroxidation product acrolein. LWT-Food Sci Technol 43:133–140 (2010).
    • (2010) LWT-Food Sci Technol , vol.43 , pp. 133-140
    • Wu, W.1    Wu, X.2    Hua, Y.3
  • 26
    • 84862811886 scopus 로고    scopus 로고
    • Aggregation and structural changes of silver carp actomyosin as affected by mild acidification with D-gluconic acid δ-lactone
    • Xu Y, Xia W and Jiang Q, Aggregation and structural changes of silver carp actomyosin as affected by mild acidification with D-gluconic acid δ-lactone. Food Chem 134:1005–1010 (2012).
    • (2012) Food Chem , vol.134 , pp. 1005-1010
    • Xu, Y.1    Xia, W.2    Jiang, Q.3
  • 27
    • 33748413614 scopus 로고    scopus 로고
    • Determining the binding affinities of phenolic compounds to proteins by quenching of the intrinsic tryptophan fluorescence
    • Rawel HM, Frey SK, Meidtner K, Kroll J and Schweigert FJ, Determining the binding affinities of phenolic compounds to proteins by quenching of the intrinsic tryptophan fluorescence. Mol Nutr Food Res 50:705–713 (2006).
    • (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
  • 29
    • 84894088317 scopus 로고    scopus 로고
    • Soy proteins: a review on composition, aggregation and emulsification
    • Nishinari K, Fang Y, Guo S and Phillips GO, Soy proteins: a review on composition, aggregation and emulsification. Food Hydrocolloid 39:301–318 (2014).
    • (2014) Food Hydrocolloid , vol.39 , pp. 301-318
    • Nishinari, K.1    Fang, Y.2    Guo, S.3    Phillips, G.O.4
  • 30
    • 77955770459 scopus 로고    scopus 로고
    • Improved emulsifying properties of soy proteins by acylation with saturated fatty acids
    • Matemu AO, Kayahara H, Murasawa H, Katayama S and Nakamura S, Improved emulsifying properties of soy proteins by acylation with saturated fatty acids. Food Chem 124:596–602 (2011).
    • (2011) Food Chem , vol.124 , pp. 596-602
    • Matemu, A.O.1    Kayahara, H.2    Murasawa, H.3    Katayama, S.4    Nakamura, S.5
  • 31
    • 84924390285 scopus 로고    scopus 로고
    • Changes in protein conformation and surface hydrophobicity upon peroxidase-catalyzed cross-linking of apo-α-lactalbumin
    • Saricay Y, Wierenga PA and Vries R, Changes in protein conformation and surface hydrophobicity upon peroxidase-catalyzed cross-linking of apo-α-lactalbumin. J Agric Food Chem 62:9345–9352 (2014).
    • (2014) J Agric Food Chem , vol.62 , pp. 9345-9352
    • Saricay, Y.1    Wierenga, P.A.2    Vries, R.3
  • 32
    • 0037129793 scopus 로고    scopus 로고
    • Interactions of different phenolic acids and flavonoids with soy proteins
    • Rawel HM, Czajka D, Rohn S and Kroll J, Interactions of different phenolic acids and flavonoids with soy proteins. Int J Biol Macromol 30:137–150 (2002).
    • (2002) Int J Biol Macromol , vol.30 , pp. 137-150
    • Rawel, H.M.1    Czajka, D.2    Rohn, S.3    Kroll, J.4
  • 33
    • 84994029381 scopus 로고    scopus 로고
    • Ultra high-pressure homogenized emulsions stabilized by sodium caseinate: effects of protein concentration and pressure on emulsions structure and stability
    • Hebishy E, Buffa M, Juan B, Blasco-Moreno A and Trujillo AJ, Ultra high-pressure homogenized emulsions stabilized by sodium caseinate: effects of protein concentration and pressure on emulsions structure and stability. LWT-Food Sci Technol 76:57–66 (2017).
    • (2017) LWT-Food Sci Technol , vol.76 , pp. 57-66
    • Hebishy, E.1    Buffa, M.2    Juan, B.3    Blasco-Moreno, A.4    Trujillo, A.J.5
  • 34
    • 77956550859 scopus 로고    scopus 로고
    • Heat-induced changes occurring in oil/water emulsions stabilized by soy glycinin and β-conglycinin
    • Keerati-U-Rai M and Corredig M, Heat-induced changes occurring in oil/water emulsions stabilized by soy glycinin and β-conglycinin. J Agric Food Chem 58:9171–9180 (2010).
    • (2010) J Agric Food Chem , vol.58 , pp. 9171-9180
    • Keerati-U-Rai, M.1    Corredig, M.2
  • 35
    • 84880045974 scopus 로고    scopus 로고
    • Emulsifying and surface properties of citric acid deamidated wheat gliadin
    • Qiu C, Sun W, Zhao Q, Cui C and Zhao M, Emulsifying and surface properties of citric acid deamidated wheat gliadin. J Cereal Sci 58:68–75 (2013).
    • (2013) J Cereal Sci , vol.58 , pp. 68-75
    • Qiu, C.1    Sun, W.2    Zhao, Q.3    Cui, C.4    Zhao, M.5
  • 36
    • 11844284817 scopus 로고    scopus 로고
    • Influence of protein concentration and order of addition on the thermal stability of beta-lactoglobulin stabilized n-hexadecane oil-in-water emulsions at neutral pH
    • Kim HJ, Decker EA and McClements DJ, Influence of protein concentration and order of addition on the thermal stability of beta-lactoglobulin stabilized n-hexadecane oil-in-water emulsions at neutral pH. Langmuir 21:134–139 (2005).
    • (2005) Langmuir , vol.21 , pp. 134-139
    • Kim, H.J.1    Decker, E.A.2    McClements, D.J.3
  • 37
    • 84255176341 scopus 로고    scopus 로고
    • Charge modifications to improve the emulsifying properties of whey protein isolate
    • Ma H, Forssell P, Partanen R, Buchert J and Boer H, Charge modifications to improve the emulsifying properties of whey protein isolate. J Agric Food Chem 59:13246–13253 (2011a).
    • (2011) J Agric Food Chem , vol.59 , pp. 13246-13253
    • Ma, H.1    Forssell, P.2    Partanen, R.3    Buchert, J.4    Boer, H.5
  • 38
    • 79951737545 scopus 로고    scopus 로고
    • Improving laccase catalyzed cross-linking of whey protein isolate and their application as emulsifiers
    • Ma H, Forssell P, Partanen R, Buchert J and Boer H, Improving laccase catalyzed cross-linking of whey protein isolate and their application as emulsifiers. J Agric Food Chem 59:1406–1414 (2011b).
    • (2011) J Agric Food Chem , vol.59 , pp. 1406-1414
    • Ma, H.1    Forssell, P.2    Partanen, R.3    Buchert, J.4    Boer, H.5
  • 39
    • 79955013465 scopus 로고    scopus 로고
    • Emulsifying and foaming properties of ultraviolet-irradiated egg white protein and sodium caseinate
    • Kuan YH, Bhat R and Karim AA, Emulsifying and foaming properties of ultraviolet-irradiated egg white protein and sodium caseinate. J Agric Food Chem 59:4111–4118 (2011).
    • (2011) J Agric Food Chem , vol.59 , pp. 4111-4118
    • Kuan, Y.H.1    Bhat, R.2    Karim, A.A.3
  • 40
    • 84931268629 scopus 로고    scopus 로고
    • Cross-linking proteins by laccase: effects on the droplet size and rheology of emulsions stabilized by sodium caseinate
    • Sato ACK, Perrechil FA, Costa AAS, Santana RC and Cunha RL, Cross-linking proteins by laccase: effects on the droplet size and rheology of emulsions stabilized by sodium caseinate. Food Res Int 75:244–251 (2015).
    • (2015) Food Res Int , vol.75 , pp. 244-251
    • Sato, A.C.K.1    Perrechil, F.A.2    Costa, A.A.S.3    Santana, R.C.4    Cunha, R.L.5
  • 41
    • 80053183936 scopus 로고    scopus 로고
    • Emulsion properties of pork myofibrillar protein in combination with microbial transglutaminase and calcium alginate under various pH conditions
    • Hong GP, Min SG and Chin KB, Emulsion properties of pork myofibrillar protein in combination with microbial transglutaminase and calcium alginate under various pH conditions. Meat Sci 90:185–193 (2012).
    • (2012) Meat Sci , vol.90 , pp. 185-193
    • Hong, G.P.1    Min, S.G.2    Chin, K.B.3


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