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Volumn 53, Issue 8, 2016, Pages 3215-3224

Oxidative polyaldehyde production: a novel approach to the conjugation of dextran with soy peptides for improved emulsifying properties

Author keywords

Maillard conjugation; Oil water emulsion; Peptide; Polyaldehyde; Polysaccharide

Indexed keywords

DEXTRAN; PARTICLE SIZE; PEPTIDES; POLYSACCHARIDES;

EID: 84979982401     PISSN: 00221155     EISSN: 09758402     Source Type: Journal    
DOI: 10.1007/s13197-016-2296-7     Document Type: Article
Times cited : (11)

References (38)
  • 1
    • 33750014292 scopus 로고    scopus 로고
    • Dextran and 5-aminosalicylic acid (5-ASA) conjugates: synthesis, characterisation and enzymic hydrolysis
    • COI: 1:CAS:528:DC%2BD28XhtFSrurfN
    • Ahmad S, Tester RF, Corbett A, Karkalas J (2006) Dextran and 5-aminosalicylic acid (5-ASA) conjugates: synthesis, characterisation and enzymic hydrolysis. Carbohydr Res 341:2694–2701
    • (2006) Carbohydr Res , vol.341 , pp. 2694-2701
    • Ahmad, S.1    Tester, R.F.2    Corbett, A.3    Karkalas, J.4
  • 2
    • 0042161834 scopus 로고    scopus 로고
    • Emulsifying properties of whey protein–dextran conjugates at low pH and different salt concentrations
    • COI: 1:CAS:528:DC%2BD3sXms12jtLk%3D
    • Akhtar M, Dickinson E (2003) Emulsifying properties of whey protein–dextran conjugates at low pH and different salt concentrations. Colloids Surf B 31:125–132
    • (2003) Colloids Surf B , vol.31 , pp. 125-132
    • Akhtar, M.1    Dickinson, E.2
  • 3
    • 0034255689 scopus 로고    scopus 로고
    • Effect of transglutaminase treatment on the functional properties of native and chymotrypsin-digested soy protein
    • COI: 1:CAS:528:DC%2BD3cXktF2qurc%3D
    • Babiker EE (2000) Effect of transglutaminase treatment on the functional properties of native and chymotrypsin-digested soy protein. Food Chem 70:139–145
    • (2000) Food Chem , vol.70 , pp. 139-145
    • Babiker, E.E.1
  • 4
    • 1342324005 scopus 로고    scopus 로고
    • cis/trans-Isochromanones. DMAP induced cycloaddition of homophthalic anhydride and aldehydes
    • COI: 1:CAS:528:DC%2BD2cXhsFeqs78%3D
    • Bogdanov MG, Palamareva MD (2004) cis/trans-Isochromanones. DMAP induced cycloaddition of homophthalic anhydride and aldehydes. Tetrahedron 60:2525–2530
    • (2004) Tetrahedron , vol.60 , pp. 2525-2530
    • Bogdanov, M.G.1    Palamareva, M.D.2
  • 5
    • 84892487557 scopus 로고    scopus 로고
    • Antioxidant activities and functional properties of soy protein isolate hydrolysates obtained using microbial proteases
    • de Castro RJS, Sato HH (2014) Antioxidant activities and functional properties of soy protein isolate hydrolysates obtained using microbial proteases. Int J Food Sci Technol 49:317–328
    • (2014) Int J Food Sci Technol , vol.49 , pp. 317-328
    • de Castro, R.J.S.1    Sato, H.H.2
  • 6
    • 0029006202 scopus 로고
    • Selective oxidation of primary alcohols mediated by nitroxyl radical in aqueous solution. Kinetics and mechanism
    • de Nooy AEJ, Besemer AC, van Bekkum H (1995) Selective oxidation of primary alcohols mediated by nitroxyl radical in aqueous solution. Kinetics and mechanism. Tetrahedron 51:8023–8032
    • (1995) Tetrahedron , vol.51 , pp. 8023-8032
    • de Nooy, A.E.J.1    Besemer, A.C.2    van Bekkum, H.3
  • 7
    • 27644536703 scopus 로고    scopus 로고
    • Physicochemical properties of dry-heated soy protein isolate–dextran mixtures
    • COI: 1:CAS:528:DC%2BD2MXhtFOgsL7J
    • Diftis N, Kiosseoglou V (2006) Physicochemical properties of dry-heated soy protein isolate–dextran mixtures. Food Chem 96:228–233
    • (2006) Food Chem , vol.96 , pp. 228-233
    • Diftis, N.1    Kiosseoglou, V.2
  • 8
    • 84855225619 scopus 로고    scopus 로고
    • Characteristics and antioxidant activity of hydrolyzed β-lactoglobulin–glucose Maillard reaction products
    • COI: 1:CAS:528:DC%2BC38XjsVWgtLg%3D
    • Dong S, Panya A, Zeng M, Chen B, McClements DJ, Decker EA (2012) Characteristics and antioxidant activity of hydrolyzed β-lactoglobulin–glucose Maillard reaction products. Food Res Int 46:55–61
    • (2012) Food Res Int , vol.46 , pp. 55-61
    • Dong, S.1    Panya, A.2    Zeng, M.3    Chen, B.4    McClements, D.J.5    Decker, E.A.6
  • 9
    • 0037391070 scopus 로고    scopus 로고
    • Interaction and functionality of mixed myofibrillar and enzyme-hydrolyzed soy proteins
    • COI: 1:CAS:528:DC%2BD3sXjt1Wht78%3D
    • Feng J, Xiong Y (2003) Interaction and functionality of mixed myofibrillar and enzyme-hydrolyzed soy proteins. J Food Sci 68:803–809
    • (2003) J Food Sci , vol.68 , pp. 803-809
    • Feng, J.1    Xiong, Y.2
  • 10
    • 79961031305 scopus 로고    scopus 로고
    • Food protein functionality: a comprehensive approach
    • COI: 1:CAS:528:DC%2BC3MXpvVKnsLw%3D
    • Foegeding EA, Davis JP (2011) Food protein functionality: a comprehensive approach. Food Hydrocoll 25:1853–1864
    • (2011) Food Hydrocoll , vol.25 , pp. 1853-1864
    • Foegeding, E.A.1    Davis, J.P.2
  • 11
    • 0041341327 scopus 로고
    • Functional properties of succinylated and acetylated soy protein
    • COI: 1:CAS:528:DyaE28XksVGju70%3D
    • Franzen KL, Kinsella JE (1976) Functional properties of succinylated and acetylated soy protein. J Agric Food Chem 24:788–795
    • (1976) J Agric Food Chem , vol.24 , pp. 788-795
    • Franzen, K.L.1    Kinsella, J.E.2
  • 12
    • 84872663853 scopus 로고    scopus 로고
    • Comparison of two methods for assaying reducing sugars in the determination of carbohydrase activities
    • Gusakov AV, Kondratyeva EG, Sinitsyn AP (2011) Comparison of two methods for assaying reducing sugars in the determination of carbohydrase activities. Int J Anal Chem 2011:1–4
    • (2011) Int J Anal Chem , vol.2011 , pp. 1-4
    • Gusakov, A.V.1    Kondratyeva, E.G.2    Sinitsyn, A.P.3
  • 13
    • 70349215199 scopus 로고    scopus 로고
    • Structural and emulsifying properties of soy protein isolate subjected to acid and alkaline ph-shifting processes
    • COI: 1:CAS:528:DC%2BD1MXosVOnsrc%3D
    • Jiang J, Chen J, Xiong YL (2009) Structural and emulsifying properties of soy protein isolate subjected to acid and alkaline ph-shifting processes. J Agric Food Chem 57:7576–7583
    • (2009) J Agric Food Chem , vol.57 , pp. 7576-7583
    • Jiang, J.1    Chen, J.2    Xiong, Y.L.3
  • 14
    • 85027952307 scopus 로고    scopus 로고
    • The physicochemical properties of legume protein isolates and their ability to stabilize oil-in-water emulsions with and without genipin
    • COI: 1:CAS:528:DC%2BC2cXhvFOhtLfJ
    • Johnston S, Nickerson M, Low N (2015) The physicochemical properties of legume protein isolates and their ability to stabilize oil-in-water emulsions with and without genipin. J Food Sci Technol 52:4135–4145
    • (2015) J Food Sci Technol , vol.52 , pp. 4135-4145
    • Johnston, S.1    Nickerson, M.2    Low, N.3
  • 15
    • 0348237026 scopus 로고    scopus 로고
    • Industrial applications of Maillard-type protein–polysaccharide conjugates
    • COI: 1:CAS:528:DC%2BD38XptlCmsr0%3D
    • Kato A (2002) Industrial applications of Maillard-type protein–polysaccharide conjugates. Food Sci Technol Res 8:193–199
    • (2002) Food Sci Technol Res , vol.8 , pp. 193-199
    • Kato, A.1
  • 16
    • 0000310789 scopus 로고
    • Functional casein–poly saccharide conjugates prepared by controlled dry heating
    • COI: 1:CAS:528:DyaK38XktVKgtLc%3D
    • Kato A, Mifuru R, Matsudomi N, Kobayashi K (1992) Functional casein–poly saccharide conjugates prepared by controlled dry heating. Biosci Biotechnol Biochem 56:567–571
    • (1992) Biosci Biotechnol Biochem , vol.56 , pp. 567-571
    • Kato, A.1    Mifuru, R.2    Matsudomi, N.3    Kobayashi, K.4
  • 17
    • 0035333574 scopus 로고    scopus 로고
    • Characterization of different starches oxidized by hypochlorite
    • COI: 1:CAS:528:DC%2BD3MXjvFansL8%3D
    • Kuakpetoon D, Wang Y-J (2001) Characterization of different starches oxidized by hypochlorite. Starch Stärke 53:211–218
    • (2001) Starch Stärke , vol.53 , pp. 211-218
    • Kuakpetoon, D.1    Wang, Y.-J.2
  • 18
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • COI: 1:CAS:528:DC%2BD3MXlsFags7s%3D
    • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680–685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 19
    • 34547699022 scopus 로고    scopus 로고
    • Functional properties of native and chemically modified protein concentrates from bambarra groundnut
    • COI: 1:CAS:528:DC%2BD2sXovFyiurc%3D
    • Lawal O, Adebowale K, Adebowale Y (2007) Functional properties of native and chemically modified protein concentrates from bambarra groundnut. Food Res Int 40:1003–1011
    • (2007) Food Res Int , vol.40 , pp. 1003-1011
    • Lawal, O.1    Adebowale, K.2    Adebowale, Y.3
  • 20
    • 84861667009 scopus 로고    scopus 로고
    • Functional properties of Maillard reaction products of rice protein hydrolysates with mono-, oligo-and poly-saccharides
    • Li Y, Zhong F, Ji W, Yokoyama W, Shoemaker CF, Zhu S, Xia W (2013) Functional properties of Maillard reaction products of rice protein hydrolysates with mono-, oligo-and poly-saccharides. Food Hydrocoll 30:53–60
    • (2013) Food Hydrocoll , vol.30 , pp. 53-60
    • Li, Y.1    Zhong, F.2    Ji, W.3    Yokoyama, W.4    Shoemaker, C.F.5    Zhu, S.6    Xia, W.7
  • 21
    • 80755125220 scopus 로고    scopus 로고
    • Improvement of functional properties of peanut protein isolate by conjugation with dextran through Maillard reaction
    • COI: 1:CAS:528:DC%2BC3MXhsVWktLvP
    • Liu Y, Zhao G, Zhao M, Ren J, Yang B (2012) Improvement of functional properties of peanut protein isolate by conjugation with dextran through Maillard reaction. Food Chem 131:901–906
    • (2012) Food Chem , vol.131 , pp. 901-906
    • Liu, Y.1    Zhao, G.2    Zhao, M.3    Ren, J.4    Yang, B.5
  • 22
    • 78651394423 scopus 로고    scopus 로고
    • Insight on the periodate oxidation of dextran and its structural vicissitudes
    • COI: 1:CAS:528:DC%2BC3MXmsl2itQ%3D%3D
    • Maia J, Carvalho RA, Coelho JFJ, Simões PN, Gil MH (2011) Insight on the periodate oxidation of dextran and its structural vicissitudes. Polymer 52:258–265
    • (2011) Polymer , vol.52 , pp. 258-265
    • Maia, J.1    Carvalho, R.A.2    Coelho, J.F.J.3    Simões, P.N.4    Gil, M.H.5
  • 23
    • 80053571280 scopus 로고    scopus 로고
    • Detection of glucose in synthetic tear fluid using dually functionalized gold nanoparticles
    • COI: 1:CAS:528:DC%2BC3MXht1KmsL7P
    • Manju S, Sreenivasan K (2011) Detection of glucose in synthetic tear fluid using dually functionalized gold nanoparticles. Talanta 85:2643–2649
    • (2011) Talanta , vol.85 , pp. 2643-2649
    • Manju, S.1    Sreenivasan, K.2
  • 24
    • 33747333106 scopus 로고
    • Use of dinitrosalicylic acid reagent for determination of reducing sugar
    • COI: 1:CAS:528:DyaG1MXmtFKiuw%3D%3D
    • Miller GL (1959) Use of dinitrosalicylic acid reagent for determination of reducing sugar. Anal Chem 31:426–428
    • (1959) Anal Chem , vol.31 , pp. 426-428
    • Miller, G.L.1
  • 25
    • 84939942662 scopus 로고    scopus 로고
    • Modification of foaming properties of soy protein isolate by high ultrasound intensity: particle size effect
    • COI: 1:CAS:528:DC%2BC2MXhtlOjtrs%3D
    • Morales R, Martínez KD, Pizones Ruiz-Henestrosa VM, Pilosof AMR (2015) Modification of foaming properties of soy protein isolate by high ultrasound intensity: particle size effect. Ultrason Sonochem 26:48–55
    • (2015) Ultrason Sonochem , vol.26 , pp. 48-55
    • Morales, R.1    Martínez, K.D.2    Pizones Ruiz-Henestrosa, V.M.3    Pilosof, A.M.R.4
  • 27
    • 33947092713 scopus 로고
    • Emulsifying properties of proteins: evaluation of a turbidimetric technique
    • COI: 1:CAS:528:DyaE1cXhvVyhtrk%3D
    • Pearce KN, Kinsella JE (1978) Emulsifying properties of proteins: evaluation of a turbidimetric technique. J Agric Food Chem 26:716–723
    • (1978) J Agric Food Chem , vol.26 , pp. 716-723
    • Pearce, K.N.1    Kinsella, J.E.2
  • 28
    • 36549096392 scopus 로고
    • Dispersed fluorescence of jet-cooled tryptophan: excited state conformers and intramolecular exciplex formation
    • COI: 1:CAS:528:DyaL2sXktVOksw%3D%3D
    • Rizzo TR, Park YD, Levy DH (1986) Dispersed fluorescence of jet-cooled tryptophan: excited state conformers and intramolecular exciplex formation. J Chem Phys 85:6945–6951
    • (1986) J Chem Phys , vol.85 , pp. 6945-6951
    • Rizzo, T.R.1    Park, Y.D.2    Levy, D.H.3
  • 29
    • 84905506218 scopus 로고    scopus 로고
    • Short chain polyethylene glycols unusually assist thermal unfolding of human serum albumin
    • COI: 1:CAS:528:DC%2BC2cXhtVemtL%2FO
    • Samanta N, Mahanta DD, Hazra S, Kumar GS, Mitra RK (2014) Short chain polyethylene glycols unusually assist thermal unfolding of human serum albumin. Biochimie 104:81–89
    • (2014) Biochimie , vol.104 , pp. 81-89
    • Samanta, N.1    Mahanta, D.D.2    Hazra, S.3    Kumar, G.S.4    Mitra, R.K.5
  • 30
    • 0343772334 scopus 로고
    • Determination of dextran structure by periodate oxidation techniques
    • COI: 1:CAS:528:DyaG2MXmsVGqsw%3D%3D
    • Sloan JW, Alexander B, Lohmar R, Wolff I, Rist C (1954) Determination of dextran structure by periodate oxidation techniques. J Am Chem Soc 76:4429–4434
    • (1954) J Am Chem Soc , vol.76 , pp. 4429-4434
    • Sloan, J.W.1    Alexander, B.2    Lohmar, R.3    Wolff, I.4    Rist, C.5
  • 31
    • 0016636179 scopus 로고
    • An improved 2,4,6-trinitrobenzenesulfonic acid method for the determination of amines
    • COI: 1:CAS:528:DyaE2MXhsFWlsbc%3D
    • Snyder SL, Sobocinski PZ (1975) An improved 2,4,6-trinitrobenzenesulfonic acid method for the determination of amines. Anal Biochem 64:284–288
    • (1975) Anal Biochem , vol.64 , pp. 284-288
    • Snyder, S.L.1    Sobocinski, P.Z.2
  • 32
    • 24944529693 scopus 로고    scopus 로고
    • Reactivity of polysaccharide aldehydes toward N-nucleophiles
    • COI: 1:CAS:528:DC%2BD38XjtVGhtg%3D%3D
    • Suvorova O, Iozep A, Passet B (2001) Reactivity of polysaccharide aldehydes toward N-nucleophiles. Russ J Appl Chem 74:1016–1020
    • (2001) Russ J Appl Chem , vol.74 , pp. 1016-1020
    • Suvorova, O.1    Iozep, A.2    Passet, B.3
  • 33
    • 12344333869 scopus 로고    scopus 로고
    • Functional properties of soy protein hydrolysates obtained by selective proteolysis
    • COI: 1:CAS:528:DC%2BD2MXhs1WnsL8%3D
    • Tsumura K, Saito T, Tsuge K, Ashida H, Kugimiya W, Inouye K (2005) Functional properties of soy protein hydrolysates obtained by selective proteolysis. LWT Food Sci Technol 38:255–261
    • (2005) LWT Food Sci Technol , vol.38 , pp. 255-261
    • Tsumura, K.1    Saito, T.2    Tsuge, K.3    Ashida, H.4    Kugimiya, W.5    Inouye, K.6
  • 34
    • 79955928732 scopus 로고    scopus 로고
    • Comparative study of the efficacies of nine assay methods for the dextransucrase synthesis of dextran
    • COI: 1:CAS:528:DC%2BC3MXmtFajtL0%3D
    • Vettori MHPB, Mukerjea R, Robyt JF (2011) Comparative study of the efficacies of nine assay methods for the dextransucrase synthesis of dextran. Carbohydr Res 346:1077–1082
    • (2011) Carbohydr Res , vol.346 , pp. 1077-1082
    • Vettori, M.H.P.B.1    Mukerjea, R.2    Robyt, J.F.3
  • 35
    • 0035028745 scopus 로고    scopus 로고
    • Mechanisms of tryptophan fluorescence shifts in proteins
    • COI: 1:CAS:528:DC%2BD3MXkvFWjtr4%3D
    • Vivian JT, Callis PR (2001) Mechanisms of tryptophan fluorescence shifts in proteins. Biophys J 80:2093–2109
    • (2001) Biophys J , vol.80 , pp. 2093-2109
    • Vivian, J.T.1    Callis, P.R.2
  • 36
    • 0037448121 scopus 로고    scopus 로고
    • Physicochemical properties of common and waxy corn starches oxidized by different levels of sodium hypochlorite
    • COI: 1:CAS:528:DC%2BD3sXht1yrsb4%3D
    • Wang Y-J, Wang L (2003) Physicochemical properties of common and waxy corn starches oxidized by different levels of sodium hypochlorite. Carbohydr Polym 52:207–217
    • (2003) Carbohydr Polym , vol.52 , pp. 207-217
    • Wang, Y.-J.1    Wang, L.2
  • 37
    • 51649086473 scopus 로고    scopus 로고
    • Formation of whey protein isolate (WPI)–dextran conjugates in aqueous solutions
    • COI: 1:CAS:528:DC%2BD1cXptVagt7k%3D
    • Zhu D, Damodaran S, Lucey JA (2008) Formation of whey protein isolate (WPI)–dextran conjugates in aqueous solutions. J Agric Food Chem 56:7113–7118
    • (2008) J Agric Food Chem , vol.56 , pp. 7113-7118
    • Zhu, D.1    Damodaran, S.2    Lucey, J.A.3
  • 38
    • 77949404014 scopus 로고    scopus 로고
    • Physicochemical and emulsifying properties of whey protein isolate (WPI)–dextran conjugates produced in aqueous solution
    • COI: 1:CAS:528:DC%2BC3cXhslSgtLc%3D
    • Zhu D, Damodaran S, Lucey JA (2010) Physicochemical and emulsifying properties of whey protein isolate (WPI)–dextran conjugates produced in aqueous solution. J Agric Food Chem 58:2988–2994
    • (2010) J Agric Food Chem , vol.58 , pp. 2988-2994
    • Zhu, D.1    Damodaran, S.2    Lucey, J.A.3


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