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Volumn 238, Issue 1, 2014, Pages 129-138

Effect of ultrasound treatment on the wet heating Maillard reaction between β-conglycinin and maltodextrin and on the emulsifying properties of conjugates

Author keywords

Conglycinin; Emulsifying properties; Maillard reaction; Maltodextrin; Ultrasound treatment

Indexed keywords

CONGLYCININ; EMULSIFYING PROPERTY; MAILLARD REACTION; MALTODEXTRINS; ULTRASOUND TREATMENTS;

EID: 84891843385     PISSN: 14382377     EISSN: 14382385     Source Type: Journal    
DOI: 10.1007/s00217-013-2082-y     Document Type: Article
Times cited : (60)

References (43)
  • 1
    • 40849118382 scopus 로고    scopus 로고
    • Physicochemical and rheological properties of soybean protein emulsions processed with a combined temperature/high-pressure treatment
    • Puppo MC, Beaumal V, Chapleau N, Speroni F, de Lamballerie M, Añón MC, Anton M (2008) Physicochemical and rheological properties of soybean protein emulsions processed with a combined temperature/high-pressure treatment. Food Hydrocolloids 22: 1079-1089.
    • (2008) Food Hydrocolloids , vol.22 , pp. 1079-1089
    • Puppo, M.C.1    Beaumal, V.2    Chapleau, N.3    Speroni, F.4    de Lamballerie, M.5    Añón, M.C.6    Anton, M.7
  • 2
    • 33747769311 scopus 로고    scopus 로고
    • Interactions between soy protein isolate and xanthan in heat-induced gels: the effect of salt addition
    • Braga ALM, Azevedo A, Marques MJ, Menossi M, Cunha RL (2006) Interactions between soy protein isolate and xanthan in heat-induced gels: the effect of salt addition. Food Hydrocolloids 20: 1178-1189.
    • (2006) Food Hydrocolloids , vol.20 , pp. 1178-1189
    • Braga, A.L.M.1    Azevedo, A.2    Marques, M.J.3    Menossi, M.4    Cunha, R.L.5
  • 3
    • 34347252586 scopus 로고    scopus 로고
    • The effect of heating on β-lactoglobulin-chitosan mixtures as influenced by pH and ionic strength
    • Mounsey JS, O'Kennedy BT, Fenelon MA, Brodkorb A (2008) The effect of heating on β-lactoglobulin-chitosan mixtures as influenced by pH and ionic strength. Food Hydrocolloids 22: 65-73.
    • (2008) Food Hydrocolloids , vol.22 , pp. 65-73
    • Mounsey, J.S.1    O'Kennedy, B.T.2    Fenelon, M.A.3    Brodkorb, A.4
  • 4
    • 0031858644 scopus 로고    scopus 로고
    • Induction of new physicochemical and functional properties by the glycosylation of whey proteins
    • Nacka F, Chobert JM, Burova T, Léonil J, Haertlé T (1998) Induction of new physicochemical and functional properties by the glycosylation of whey proteins. J Protein Chem 17: 495-503.
    • (1998) J Protein Chem , vol.17 , pp. 495-503
    • Nacka, F.1    Chobert, J.M.2    Burova, T.3    Léonil, J.4    Haertlé, T.5
  • 5
    • 33646377677 scopus 로고    scopus 로고
    • Creating proteins with novel functionality via the Maillard reaction: a review
    • Oliver CM, Melton LD, Stanley RA (2006) Creating proteins with novel functionality via the Maillard reaction: a review. Crit Rev Food Sci Nutr 46: 337-350.
    • (2006) Crit Rev Food Sci Nutr , vol.46 , pp. 337-350
    • Oliver, C.M.1    Melton, L.D.2    Stanley, R.A.3
  • 6
    • 0000409683 scopus 로고
    • Preparation and characterization of ovalbumin-dextran conjugate having excellent emulsifying properties
    • Kato A, Murata K, Kobayashi K (1988) Preparation and characterization of ovalbumin-dextran conjugate having excellent emulsifying properties. J Agric Food Chem 36: 421-425.
    • (1988) J Agric Food Chem , vol.36 , pp. 421-425
    • Kato, A.1    Murata, K.2    Kobayashi, K.3
  • 7
    • 0024986845 scopus 로고
    • Functional protein-polysaccharide conjugate prepared by controlled dry-heating of ovalbumin-dextran mixtures
    • Kato A, Sasaki Y, Furuta R (1990) Functional protein-polysaccharide conjugate prepared by controlled dry-heating of ovalbumin-dextran mixtures. J Agric Biol Chem 54: 107-112.
    • (1990) J Agric Biol Chem , vol.54 , pp. 107-112
    • Kato, A.1    Sasaki, Y.2    Furuta, R.3
  • 8
    • 0001212535 scopus 로고
    • Improvement of the functional properties of insoluble gluten by pronase digestion followed by dextran conjugate
    • Kato A, Shimokawa K, Kobayashi K (1991) Improvement of the functional properties of insoluble gluten by pronase digestion followed by dextran conjugate. J Agric Food Chem 39: 1053-1056.
    • (1991) J Agric Food Chem , vol.39 , pp. 1053-1056
    • Kato, A.1    Shimokawa, K.2    Kobayashi, K.3
  • 9
    • 33751391825 scopus 로고
    • Bifunctional lysozyme-galactomannan conjugate having excellent emulsifying properties and bactericidal effect
    • Nakamura S, Kato A, Kobayashi K (1992) Bifunctional lysozyme-galactomannan conjugate having excellent emulsifying properties and bactericidal effect. J Agric Food Chem 40: 735-739.
    • (1992) J Agric Food Chem , vol.40 , pp. 735-739
    • Nakamura, S.1    Kato, A.2    Kobayashi, K.3
  • 10
    • 0000668338 scopus 로고
    • Enhanced antioxidative effect of ovalbumin due to covalent binding of polysaccharides
    • Nakamura S, Kato A, Kobayashi K (1992) Enhanced antioxidative effect of ovalbumin due to covalent binding of polysaccharides. J Agric Food Chem 40: 2033-2037.
    • (1992) J Agric Food Chem , vol.40 , pp. 2033-2037
    • Nakamura, S.1    Kato, A.2    Kobayashi, K.3
  • 11
    • 0032822981 scopus 로고    scopus 로고
    • Functional improvements in dried egg white through the Maillard reaction
    • Handa A, Kuroda N (1999) Functional improvements in dried egg white through the Maillard reaction. J Agric Food Chem 47: 1845-1850.
    • (1999) J Agric Food Chem , vol.47 , pp. 1845-1850
    • Handa, A.1    Kuroda, N.2
  • 12
    • 31844444482 scopus 로고    scopus 로고
    • Microwave improvement of soy protein isolate-saccharide graft reactions
    • Guan JJ, Qiu AY, Liu XY, Hua YF, Ma YH (2006) Microwave improvement of soy protein isolate-saccharide graft reactions. Food Chem 97: 577-585.
    • (2006) Food Chem , vol.97 , pp. 577-585
    • Guan, J.J.1    Qiu, A.Y.2    Liu, X.Y.3    Hua, Y.F.4    Ma, Y.H.5
  • 13
    • 77950657041 scopus 로고    scopus 로고
    • Effect of ultrasonic treatment on the graft reaction between Soy Protein Isolate and Gum Acacia and on the physicochemical properties of conjugates
    • Mu LX, Zhao MM, Yang B (2010) Effect of ultrasonic treatment on the graft reaction between Soy Protein Isolate and Gum Acacia and on the physicochemical properties of conjugates. J Agric Food Chem 58: 4494-4499.
    • (2010) J Agric Food Chem , vol.58 , pp. 4494-4499
    • Mu, L.X.1    Zhao, M.M.2    Yang, B.3
  • 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
    • Lin C, Chen JS, Ren JY, Zhao MM (2011) 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) J Agric Food Chem , vol.59 , pp. 2600-2609
    • Lin, C.1    Chen, J.S.2    Ren, J.Y.3    Zhao, M.M.4
  • 15
    • 0019496142 scopus 로고
    • Soybean protein agglomeration: promotion by ultrasonic treatment
    • Wang LC (1981) Soybean protein agglomeration: promotion by ultrasonic treatment. J Agric Food Chem 29: 177-180.
    • (1981) J Agric Food Chem , vol.29 , pp. 177-180
    • Wang, L.C.1
  • 16
    • 79955638399 scopus 로고    scopus 로고
    • Properties of whey protein isolate-dextran conjugate prepared using pulsed electric field
    • Sun WW, Yu SJ, Zeng XA, Yang XQ, Jia X (2011) Properties of whey protein isolate-dextran conjugate prepared using pulsed electric field. Food Res Int 44: 1052-1058.
    • (2011) Food Res Int , vol.44 , pp. 1052-1058
    • Sun, W.W.1    Yu, S.J.2    Zeng, X.A.3    Yang, X.Q.4    Jia, X.5
  • 17
    • 0001984295 scopus 로고
    • Isolation and characterization of the multiple 7S globulins of soybean proteins
    • Thanh VH, Okubo K, Shibasaki K (1975) Isolation and characterization of the multiple 7S globulins of soybean proteins. Plant Physiol 56: 19-22.
    • (1975) Plant Physiol , vol.56 , pp. 19-22
    • Thanh, V.H.1    Okubo, K.2    Shibasaki, K.3
  • 19
    • 0038693085 scopus 로고    scopus 로고
    • Improvement of emulsifying properties of soybean protein isolate by conjugation with carboxymethyl cellulose
    • Diftis N, Kiosseoglou V (2003) Improvement of emulsifying properties of soybean protein isolate by conjugation with carboxymethyl cellulose. Food Chem 81: 1-6.
    • (2003) Food Chem , vol.81 , pp. 1-6
    • Diftis, N.1    Kiosseoglou, V.2
  • 20
    • 84891850337 scopus 로고    scopus 로고
    • Investigation of the Maillard reaction activities of soy protein components with maltodextrin and the emulsifying properties of the final conjugates
    • Hu K, Zeng L, Yu S (2007) Investigation of the Maillard reaction activities of soy protein components with maltodextrin and the emulsifying properties of the final conjugates. J Food Ferment Ind 33: 22-28.
    • (2007) J Food Ferment Ind , vol.33 , pp. 22-28
    • Hu, K.1    Zeng, L.2    Yu, S.3
  • 21
    • 0042667003 scopus 로고    scopus 로고
    • Kinetic modelling of reactions in heated disaccharide-casein systems
    • Brands J, van Boekel AJS (2003) Kinetic modelling of reactions in heated disaccharide-casein systems. Food Chem 83: 13-26.
    • (2003) Food Chem , vol.83 , pp. 13-26
    • Brands, J.1    van Boekel, A.J.S.2
  • 22
    • 0019331914 scopus 로고
    • Hydrophobicity determined by a fluorescence probe method and its correlation with surface properties of proteins
    • Kato A, Nakai S (1980) Hydrophobicity determined by a fluorescence probe method and its correlation with surface properties of proteins. Biochimica et Biophysica Acta (BBA)-Protein Struct 624: 13-20.
    • (1980) Biochimica Et Biophysica Acta (BBA)-Protein Struct , vol.624 , pp. 13-20
    • Kato, A.1    Nakai, S.2
  • 23
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding
    • Bradford M (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding. Anal Biochem 72: 248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.1
  • 24
    • 33947092713 scopus 로고
    • Emulsifying properties of proteins evaluation of a turbidimetric technique
    • 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
  • 25
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of head of bacteriophage T4
    • Laemmli UK (1970) Cleavage of structural proteins during the assembly of head of bacteriophage T4. Food Sci Nat 227: 680-685.
    • (1970) Food Sci Nat , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 26
    • 0006097146 scopus 로고
    • Lysine loss and polymerization of bovine β-lactoglobulin by amino carbonyl reaction with lactulose (4-O-β-d-galactopyranosyl-d-fructose)
    • Matsuda T, Kato Y, Nakamura R (1991) Lysine loss and polymerization of bovine β-lactoglobulin by amino carbonyl reaction with lactulose (4-O-β-d-galactopyranosyl-d-fructose). J Agric Food Chem 39: 1201-1204.
    • (1991) J Agric Food Chem , vol.39 , pp. 1201-1204
    • Matsuda, T.1    Kato, Y.2    Nakamura, R.3
  • 27
    • 0034672122 scopus 로고    scopus 로고
    • Estimation of protein secondary structure from circular dichroism spectra: inclusion of denatured proteins with native proteins in the analysis
    • Sreerama N, Venyaminov Y, Woody W (2000) Estimation of protein secondary structure from circular dichroism spectra: inclusion of denatured proteins with native proteins in the analysis. J Agric Food Chem 287: 243-251.
    • (2000) J Agric Food Chem , vol.287 , pp. 243-251
    • Sreerama, N.1    Venyaminov, Y.2    Woody, W.3
  • 28
    • 11144238233 scopus 로고    scopus 로고
    • Structural characteristics of purified β-conglycinin from soybeans stored under four conditions
    • Hou HJ, Chang KC (2004) Structural characteristics of purified β-conglycinin from soybeans stored under four conditions. J Agric Food Chem 52: 7931-7937.
    • (2004) J Agric Food Chem , vol.52 , pp. 7931-7937
    • Hou, H.J.1    Chang, K.C.2
  • 29
    • 27644536703 scopus 로고    scopus 로고
    • Physicochemical properties of dry-heated soy protein isolate-dextran mixtures
    • 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
  • 30
    • 33846207960 scopus 로고    scopus 로고
    • Whey protein-maltodextrin conjugates as emulsifying agents: an alternative to gum arabic
    • Akhtar M, Dickinson E (2007) Whey protein-maltodextrin conjugates as emulsifying agents: an alternative to gum arabic. Food Hydrocolloids 21: 607-616.
    • (2007) Food Hydrocolloids , vol.21 , pp. 607-616
    • Akhtar, M.1    Dickinson, E.2
  • 31
    • 0033825099 scopus 로고    scopus 로고
    • Dairy glycoconjugate emulsifiers: casein-maltodextrins
    • Shepherd R, Robertson A, Ofman D (2000) Dairy glycoconjugate emulsifiers: casein-maltodextrins. Food Hydrocolloids 14: 281-286.
    • (2000) Food Hydrocolloids , vol.14 , pp. 281-286
    • Shepherd, R.1    Robertson, A.2    Ofman, D.3
  • 32
    • 84863267579 scopus 로고    scopus 로고
    • Improvement of emulsifying properties of Maillard reaction products from β-conglycinin and dextran using controlled enzymatic hydrolysis
    • Zhang JB, Wu NN, Yang XQ, Tang XH, Wang LJ (2012) Improvement of emulsifying properties of Maillard reaction products from β-conglycinin and dextran using controlled enzymatic hydrolysis. Food Hydrocolloids 28: 301-312.
    • (2012) Food Hydrocolloids , vol.28 , pp. 301-312
    • Zhang, J.B.1    Wu, N.N.2    Yang, X.Q.3    Tang, X.H.4    Wang, L.J.5
  • 34
    • 3242816089 scopus 로고    scopus 로고
    • Brassica carinata protein isolates: chemical composition, protein characterization and improvement of functional properties by protein hydrolysis
    • Pedroche J, Yust MM, Lqari H, Girón-Calle J, Alaiz M, Vioque J, Millán F (2004) Brassica carinata protein isolates: chemical composition, protein characterization and improvement of functional properties by protein hydrolysis. Food Chem 88: 337-346.
    • (2004) Food Chem , vol.88 , pp. 337-346
    • Pedroche, J.1    Yust, M.M.2    Lqari, H.3    Girón-Calle, J.4    Alaiz, M.5    Vioque, J.6    Millán, F.7
  • 35
    • 0003849235 scopus 로고    scopus 로고
    • Interactions of ovalbumin with sulphated polysaccharides: effects of pH, ionic strength, heat and high pressure treatment
    • Galazka B, Smith D, Ledward A, Dickinson E (1999) Interactions of ovalbumin with sulphated polysaccharides: effects of pH, ionic strength, heat and high pressure treatment. Food Hydrocolloids 13: 81-88.
    • (1999) Food Hydrocolloids , vol.13 , pp. 81-88
    • Galazka, B.1    Smith, D.2    Ledward, A.3    Dickinson, E.4
  • 36
    • 84891871624 scopus 로고    scopus 로고
    • Effects of physicochemical factors on the hydrophobicity of soybean protein
    • Huang M, Bian K (2002) Effects of physicochemical factors on the hydrophobicity of soybean protein. J Zheng Zhou Inst Technol 23: 5-9.
    • (2002) J Zheng Zhou Inst Technol , vol.23 , pp. 5-9
    • Huang, M.1    Bian, K.2
  • 37
    • 35548957779 scopus 로고    scopus 로고
    • A circular dichroism and fluorescence spectrometric assessment of effects of selected chemical denaturants on soybean (Glycine max L.) storage proteins glycinin (11S) and β-conglycinin (7S)
    • Clare Sze KW, Kshirsagar H, Venkatachalam M, Sathe KS (2007) A circular dichroism and fluorescence spectrometric assessment of effects of selected chemical denaturants on soybean (Glycine max L.) storage proteins glycinin (11S) and β-conglycinin (7S). J Agric Food Chem 55: 8745-8753.
    • (2007) J Agric Food Chem , vol.55 , pp. 8745-8753
    • Clare Sze, K.W.1    Kshirsagar, H.2    Venkatachalam, M.3    Sathe, K.S.4
  • 38
    • 77957341764 scopus 로고    scopus 로고
    • The effect of glycosylation with dextran chains of differing lengths on the thermal aggregation of β-conglycinin and glycinin
    • Xu CH, Yang XQ, Yu SJ, Qi JR, Guo R, Sun WW, Yao YJ, Zhao MM (2010) The effect of glycosylation with dextran chains of differing lengths on the thermal aggregation of β-conglycinin and glycinin. Food Res Int 43: 2270-2276.
    • (2010) Food Res Int , vol.43 , pp. 2270-2276
    • Xu, C.H.1    Yang, X.Q.2    Yu, S.J.3    Qi, J.R.4    Guo, R.5    Sun, W.W.6    Yao, Y.J.7    Zhao, M.M.8
  • 39
    • 2342586625 scopus 로고    scopus 로고
    • Changes of glycinin conformation due to pH, heat and salt determined by differential scanning calorimetry and circular dichroism
    • Kim KS, Kim S, Yang HJ, Kwon DY (2004) Changes of glycinin conformation due to pH, heat and salt determined by differential scanning calorimetry and circular dichroism. J Food Sci Technol 39: 385-393.
    • (2004) J Food Sci Technol , vol.39 , pp. 385-393
    • Kim, K.S.1    Kim, S.2    Yang, H.J.3    Kwon, D.Y.4
  • 40
    • 0013105888 scopus 로고    scopus 로고
    • Preparation and functional properties of protein-polysaccharide conjugates
    • Marcel Dekker, Inc., New York
    • Kato A (1996) Preparation and functional properties of protein-polysaccharide conjugates. In: Surface activity of proteins. Marcel Dekker, Inc., New York, pp 115-130.
    • (1996) Surface activity of proteins , pp. 115-130
    • Kato, A.1
  • 41
    • 0002710363 scopus 로고
    • Formation of emulsion
    • P. Becher (Ed.), New York: Marcel Dekker Inc
    • Walstra P (1983) Formation of emulsion. In: Becher P (ed) Encyclopedia of emulsion technology: basic theory, vol 1. Marcel Dekker Inc, New York, pp 57-127.
    • (1983) Encyclopedia of Emulsion Technology: Basic Theory , vol.1 , pp. 57-127
    • Walstra, P.1
  • 42
    • 0003476530 scopus 로고
    • Sonochemistry: theory, applications and uses of ultrasound in chemistry
    • Mason TL, Lorimer JP (1989) Sonochemistry: theory, applications and uses of ultrasound in chemistry. Ultrasonics 27: 252-253.
    • (1989) Ultrasonics , vol.27 , pp. 252-253
    • Mason, T.L.1    Lorimer, J.P.2
  • 43
    • 0032958393 scopus 로고    scopus 로고
    • Sonochemistry, science and engineering
    • Thompson LH, Doraisamy LK (1999) Sonochemistry, science and engineering. Ind Eng Chem Res 38: 1215-1249.
    • (1999) Ind Eng Chem Res , vol.38 , pp. 1215-1249
    • Thompson, L.H.1    Doraisamy, L.K.2


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