메뉴 건너뛰기




Volumn 97, Issue 8, 2014, Pages 4695-4702

Antigenicity and conformational changes of β-lactoglobulin by dynamic high pressure microfluidization combining with glycation treatment

Author keywords

Antigenicity; Conformational change; Dynamic high pressure microfluidization combined with glycation; lactoglobulin

Indexed keywords

LACTOGLOBULIN; OLIGOSACCHARIDE;

EID: 84904420876     PISSN: 00220302     EISSN: 15253198     Source Type: Journal    
DOI: 10.3168/jds.2013-7829     Document Type: Article
Times cited : (49)

References (53)
  • 1
    • 84889990839 scopus 로고    scopus 로고
    • Food Materials Science: Principles and Practice. Springer Science & Business Media LLC, New York, NY.
    • Aguilera, J. M., and P. J. Lillford. 2008. Food Materials Science: Principles and Practice. Springer Science & Business Media LLC, New York, NY.
    • (2008)
    • Aguilera, J.M.1    Lillford, P.J.2
  • 2
    • 84987261103 scopus 로고
    • Lipophilization of β-lactoglobulin: Effect on hydrophobicity, conformation and surface functional properties
    • Akita E.M., Nakai S. Lipophilization of β-lactoglobulin: Effect on hydrophobicity, conformation and surface functional properties. J. Food Sci. 1990, 55:711-717.
    • (1990) J. Food Sci. , vol.55 , pp. 711-717
    • Akita, E.M.1    Nakai, S.2
  • 3
    • 52949123627 scopus 로고    scopus 로고
    • A heat-stable trypsin from the hepatopancreas of the cuttlefish (Sepia officinalis): Purification and characterisation
    • Balti R., Barkia A., Bougatef A., Ktari N., Nasri M. A heat-stable trypsin from the hepatopancreas of the cuttlefish (Sepia officinalis): Purification and characterisation. Food Chem. 2009, 113:146-154.
    • (2009) Food Chem. , vol.113 , pp. 146-154
    • Balti, R.1    Barkia, A.2    Bougatef, A.3    Ktari, N.4    Nasri, M.5
  • 4
    • 0034921222 scopus 로고    scopus 로고
    • Improvement of functional properties of β-lactoglobulin glycated through the Maillard reaction is related to the nature of the sugar
    • Chevalier F., Chobert J.M., Popineau Y., Nicolas M.G., Haertle T. Improvement of functional properties of β-lactoglobulin glycated through the Maillard reaction is related to the nature of the sugar. Int. Dairy J. 2001, 11:145-152.
    • (2001) Int. Dairy J. , vol.11 , pp. 145-152
    • Chevalier, F.1    Chobert, J.M.2    Popineau, Y.3    Nicolas, M.G.4    Haertle, T.5
  • 5
    • 33846596245 scopus 로고    scopus 로고
    • Influence of binding conjugated linoleic acid and myristic acid on the heat- and high-pressure-induced unfolding and aggregation of β-lactoglobulin B
    • Considine T., Patel H.A., Singh H., Creamer L.K. Influence of binding conjugated linoleic acid and myristic acid on the heat- and high-pressure-induced unfolding and aggregation of β-lactoglobulin B. Food Chem. 2007, 102:1270-1280.
    • (2007) Food Chem. , vol.102 , pp. 1270-1280
    • Considine, T.1    Patel, H.A.2    Singh, H.3    Creamer, L.K.4
  • 6
    • 47049093974 scopus 로고    scopus 로고
    • Structural characterization of bovine β-lactoglobulin galactose/tagatose Maillard complexes by electrophoretic, chromatographic and spectroscopic methods
    • Corzo-Martínez M., Moreno F.J., Olano A., Villamiel M. Structural characterization of bovine β-lactoglobulin galactose/tagatose Maillard complexes by electrophoretic, chromatographic and spectroscopic methods. J. Agric. Food Chem. 2008, 56:4244-4252.
    • (2008) J. Agric. Food Chem. , vol.56 , pp. 4244-4252
    • Corzo-Martínez, M.1    Moreno, F.J.2    Olano, A.3    Villamiel, M.4
  • 7
    • 1942441014 scopus 로고    scopus 로고
    • Spectroscopic characterization of heat-induced nonnative β-lactoglobulin monomers
    • Croguennec T., Molle D., Mehra R., Bouhallab S. Spectroscopic characterization of heat-induced nonnative β-lactoglobulin monomers. Protein Sci. 2004, 13:1340-1346.
    • (2004) Protein Sci. , vol.13 , pp. 1340-1346
    • Croguennec, T.1    Molle, D.2    Mehra, R.3    Bouhallab, S.4
  • 8
    • 50849141103 scopus 로고    scopus 로고
    • Structural modifications of beta-lactoglobulin subjected to gamma radiation
    • de la Hoz L., Netto F.M. Structural modifications of beta-lactoglobulin subjected to gamma radiation. Int. Dairy J. 2008, 18:1126-1132.
    • (2008) Int. Dairy J. , vol.18 , pp. 1126-1132
    • de la Hoz, L.1    Netto, F.M.2
  • 9
    • 76349110558 scopus 로고    scopus 로고
    • Effects of temperature and chromium (III) ion on the structure of bovine β-lactoglobulin A
    • Divsalar A., Saboury A.A., Ahmad F., Moosavi-Movahedi A.A. Effects of temperature and chromium (III) ion on the structure of bovine β-lactoglobulin A. J. Braz. Chem. Soc. 2009, 20:1782-1789.
    • (2009) J. Braz. Chem. Soc. , vol.20 , pp. 1782-1789
    • Divsalar, A.1    Saboury, A.A.2    Ahmad, F.3    Moosavi-Movahedi, A.A.4
  • 11
    • 68149142319 scopus 로고    scopus 로고
    • Glycation and phosphorylation of alpha-lactalbumin by dry-heating: Effect on protein structure and physiological functions
    • Enomoto H., Hayashi Y., Li C.P., Ohki S., Ohtomo H., Shiokawa M., Aoki T. Glycation and phosphorylation of alpha-lactalbumin by dry-heating: Effect on protein structure and physiological functions. J. Dairy Sci. 2009, 92:3057-3068.
    • (2009) J. Dairy Sci. , vol.92 , pp. 3057-3068
    • Enomoto, H.1    Hayashi, Y.2    Li, C.P.3    Ohki, S.4    Ohtomo, H.5    Shiokawa, M.6    Aoki, T.7
  • 12
    • 0034941083 scopus 로고    scopus 로고
    • Cow's milk protein allergy and possible means for its prevention
    • Exl B.M., Fritsche R. Cow's milk protein allergy and possible means for its prevention. Nutrition 2001, 17:642-651.
    • (2001) Nutrition , vol.17 , pp. 642-651
    • Exl, B.M.1    Fritsche, R.2
  • 14
    • 33847659962 scopus 로고    scopus 로고
    • ANS fluorescence: Potential to augment the identification of the external binding sites of proteins
    • Gasymov O.K., Glasgow B.J. ANS fluorescence: Potential to augment the identification of the external binding sites of proteins. Biochim. Biophys. Acta 2007, 1774:403-411.
    • (2007) Biochim. Biophys. Acta , vol.1774 , pp. 403-411
    • Gasymov, O.K.1    Glasgow, B.J.2
  • 16
    • 0346976253 scopus 로고    scopus 로고
    • Functional improvements in food proteins in multiple aspects by conjugation with saccharides: Case studies of β-lactoglobulin-acidic polysaccharides conjugates
    • Hattori M. Functional improvements in food proteins in multiple aspects by conjugation with saccharides: Case studies of β-lactoglobulin-acidic polysaccharides conjugates. Food Sci. Res. 2002, 8:291-299.
    • (2002) Food Sci. Res. , vol.8 , pp. 291-299
    • Hattori, M.1
  • 17
    • 0033919021 scopus 로고    scopus 로고
    • Functional changes in β-lactoglobulin by conjugation with cationic saccharides
    • Hattori M., Koichi N., Akio A., et al. Functional changes in β-lactoglobulin by conjugation with cationic saccharides. J. Agric. Food Chem. 2000, 48:2050-2056.
    • (2000) J. Agric. Food Chem. , vol.48 , pp. 2050-2056
    • Hattori, M.1    Koichi, N.2    Akio, A.3
  • 18
    • 3142581377 scopus 로고    scopus 로고
    • Reduced immunogenicity of β-lactoglobulin by conjugation with acidic oligosaccharides
    • Hattori M., Miyakawa S., Ohama Y. Reduced immunogenicity of β-lactoglobulin by conjugation with acidic oligosaccharides. J. Agric. Food Chem. 2004, 52:4546-4553.
    • (2004) J. Agric. Food Chem. , vol.52 , pp. 4546-4553
    • Hattori, M.1    Miyakawa, S.2    Ohama, Y.3
  • 19
    • 77953131707 scopus 로고    scopus 로고
    • Functional properties of milk proteins as affected by Maillard reaction induced oligomerisation
    • Hiller B., Lorenzen P.C. Functional properties of milk proteins as affected by Maillard reaction induced oligomerisation. Food Res. Int. 2010, 43:1155-1166.
    • (2010) Food Res. Int. , vol.43 , pp. 1155-1166
    • Hiller, B.1    Lorenzen, P.C.2
  • 21
    • 0036124772 scopus 로고    scopus 로고
    • Proteolysis of bovine β-lactoglobulin during thermal treatment on subdenaturing conditions highlights some structural features of the temperature-modified protein and yields fragments with low immunoreactivity
    • Iametti S., Rasmussen P., Frokiaer H., Ferranti P., Addeo F., Bonomi F. Proteolysis of bovine β-lactoglobulin during thermal treatment on subdenaturing conditions highlights some structural features of the temperature-modified protein and yields fragments with low immunoreactivity. Eur. J. Biochem. 2002, 269:1362-1372.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 1362-1372
    • Iametti, S.1    Rasmussen, P.2    Frokiaer, H.3    Ferranti, P.4    Addeo, F.5    Bonomi, F.6
  • 22
    • 34848859979 scopus 로고    scopus 로고
    • Peptic and tryptic hydrolysis of native and heated whey protein to reduce its antigenicity
    • Kim S.B., Ki K.S., Khan M.A. Peptic and tryptic hydrolysis of native and heated whey protein to reduce its antigenicity. J. Dairy Sci. 2007, 90:4043-4050.
    • (2007) J. Dairy Sci. , vol.90 , pp. 4043-4050
    • Kim, S.B.1    Ki, K.S.2    Khan, M.A.3
  • 23
    • 21044455900 scopus 로고    scopus 로고
    • The antigenic response of beta-lactoglobulin is modulated by thermally induced aggregation
    • Kleber N., Krause I., Illgner S., Hinrichs J. The antigenic response of beta-lactoglobulin is modulated by thermally induced aggregation. Eur. Food Res. Technol. 2004, 219:105-110.
    • (2004) Eur. Food Res. Technol. , vol.219 , pp. 105-110
    • Kleber, N.1    Krause, I.2    Illgner, S.3    Hinrichs, J.4
  • 24
    • 0035117504 scopus 로고    scopus 로고
    • Reduced immunogenicity of β-lactoglobulin by conjugation with carboxymethyl dextran differing in molecular weight
    • Kobayashi K. Reduced immunogenicity of β-lactoglobulin by conjugation with carboxymethyl dextran differing in molecular weight. J. Agric. Food Chem. 2001, 49:823-831.
    • (2001) J. Agric. Food Chem. , vol.49 , pp. 823-831
    • Kobayashi, K.1
  • 25
    • 0034999046 scopus 로고    scopus 로고
    • Effects of high pressure and low temperature on β-lactoglobulin unfolding and aggregation
    • Kolakowski P., Dumay E., Cheftel J.C. Effects of high pressure and low temperature on β-lactoglobulin unfolding and aggregation. Food Hydrocoll. 2001, 15:215-232.
    • (2001) Food Hydrocoll. , vol.15 , pp. 215-232
    • Kolakowski, P.1    Dumay, E.2    Cheftel, J.C.3
  • 26
    • 0031253029 scopus 로고    scopus 로고
    • Characterization by ionization mass spectrometry of lactosyl β-lactoglobulin conjugates formed during heat treatment of milk and whey and identification of one lactose-binding site
    • Leonil J., Molle D., Fauquant J., Maubois L., Pearce R.J., Bouhallab S. Characterization by ionization mass spectrometry of lactosyl β-lactoglobulin conjugates formed during heat treatment of milk and whey and identification of one lactose-binding site. J. Dairy Sci. 1997, 80:2270-2281.
    • (1997) J. Dairy Sci. , vol.80 , pp. 2270-2281
    • Leonil, J.1    Molle, D.2    Fauquant, J.3    Maubois, L.4    Pearce, R.J.5    Bouhallab, S.6
  • 27
    • 84860395576 scopus 로고    scopus 로고
    • Effects of Maillard reaction conditions on the antigenicity of α-lactalbumin and β-lactoglobulin in whey protein conjugated with maltose
    • Li Z., Luo Y., Feng L. Effects of Maillard reaction conditions on the antigenicity of α-lactalbumin and β-lactoglobulin in whey protein conjugated with maltose. Eur. Food Res. Technol. 2011, 233:387-394.
    • (2011) Eur. Food Res. Technol. , vol.233 , pp. 387-394
    • Li, Z.1    Luo, Y.2    Feng, L.3
  • 28
    • 84866028087 scopus 로고    scopus 로고
    • Glycation a promising method for food protein modification: Physicochemical properties and structure, a review
    • Liu J.H., Ru Q., Ding Y. Glycation a promising method for food protein modification: Physicochemical properties and structure, a review. Food Res. Int. 2012, 49:170-183.
    • (2012) Food Res. Int. , vol.49 , pp. 170-183
    • Liu, J.H.1    Ru, Q.2    Ding, Y.3
  • 29
    • 77954620043 scopus 로고    scopus 로고
    • The effect of dynamic high-pressure microfluidization on the activity, stability and conformation of trypsin
    • Liu W., Zhang Z.Q., Liu C.M., Xie M.Y., Tu Z.C., Liu J.H., Liang R.H. The effect of dynamic high-pressure microfluidization on the activity, stability and conformation of trypsin. Food Chem. 2010, 123:616-621.
    • (2010) Food Chem. , vol.123 , pp. 616-621
    • Liu, W.1    Zhang, Z.Q.2    Liu, C.M.3    Xie, M.Y.4    Tu, Z.C.5    Liu, J.H.6    Liang, R.H.7
  • 30
    • 84856150284 scopus 로고    scopus 로고
    • In vivo methods for testing allergenicity show that high hydrostatic pressure hydrolysates of β-lactoglobulin are immunologically inert
    • López-Expósito I., Chicón R., Belloque J., et al. In vivo methods for testing allergenicity show that high hydrostatic pressure hydrolysates of β-lactoglobulin are immunologically inert. J. Dairy Sci. 2012, 95:541-548.
    • (2012) J. Dairy Sci. , vol.95 , pp. 541-548
    • López-Expósito, I.1    Chicón, R.2    Belloque, J.3
  • 31
    • 0032839589 scopus 로고    scopus 로고
    • Effect of heat treatment on bovine β-lactoglobulin A, B and C explored using thiol availability and fluorescence
    • Manderson G.A., Hardman M.J., Creamer L.K. Effect of heat treatment on bovine β-lactoglobulin A, B and C explored using thiol availability and fluorescence. J. Agric. Food Chem. 1999, 47:3617-3627.
    • (1999) J. Agric. Food Chem. , vol.47 , pp. 3617-3627
    • Manderson, G.A.1    Hardman, M.J.2    Creamer, L.K.3
  • 32
    • 52949111347 scopus 로고    scopus 로고
    • The effect of glycation on foam and structural properties of β-lactoglobulin
    • Medrano A., Abirached C., Panizzolo L., Moyna P., Anon M.C. The effect of glycation on foam and structural properties of β-lactoglobulin. Food Chem. 2009, 113:127-133.
    • (2009) Food Chem. , vol.113 , pp. 127-133
    • Medrano, A.1    Abirached, C.2    Panizzolo, L.3    Moyna, P.4    Anon, M.C.5
  • 33
    • 34547753123 scopus 로고    scopus 로고
    • Site-specific formation of Maillard, oxidation, and condensation products from whey proteins during reaction with lactose
    • Meltretter J., Seeber S., Humeny A. Site-specific formation of Maillard, oxidation, and condensation products from whey proteins during reaction with lactose. J. Agric. Food Chem. 2007, 55:6096-6103.
    • (2007) J. Agric. Food Chem. , vol.55 , pp. 6096-6103
    • Meltretter, J.1    Seeber, S.2    Humeny, A.3
  • 34
    • 0002915720 scopus 로고
    • Effect of pH and temperature on protein unfolding and thiol-disulfide interchange reactions during heat-induced gelation of whey proteins
    • Monahan F.J., German J.B., Kinsella J.E. Effect of pH and temperature on protein unfolding and thiol-disulfide interchange reactions during heat-induced gelation of whey proteins. J. Agric. Food Chem. 1995, 43:46-52.
    • (1995) J. Agric. Food Chem. , vol.43 , pp. 46-52
    • Monahan, F.J.1    German, J.B.2    Kinsella, J.E.3
  • 35
    • 26244468729 scopus 로고    scopus 로고
    • Effect of Maillard reaction on allergenicity of scallop tropomyosin
    • Nakamura A., Watanabe K., Ojima T., et al. Effect of Maillard reaction on allergenicity of scallop tropomyosin. J. Agric. Food Chem. 2005, 53:7559-7564.
    • (2005) J. Agric. Food Chem. , vol.53 , pp. 7559-7564
    • Nakamura, A.1    Watanabe, K.2    Ojima, T.3
  • 37
    • 70350214654 scopus 로고    scopus 로고
    • Improvement of functional properties of acid-precipitated soy protein by the attachment of dextran through Maillard reaction
    • Qi J.R., Yang X.Q., Liao J.S. Improvement of functional properties of acid-precipitated soy protein by the attachment of dextran through Maillard reaction. Int. J. Food Sci. Technol. 2009, 44:2296-2302.
    • (2009) Int. J. Food Sci. Technol. , vol.44 , pp. 2296-2302
    • Qi, J.R.1    Yang, X.Q.2    Liao, J.S.3
  • 38
    • 0030993642 scopus 로고    scopus 로고
    • Effect of temperature on the secondary structure of β-lactoglobulin at pH 6.7, as determined by CD and IR spectroscopy: A test of the molten globule hypothesis
    • Qi X.L., Holt C., McNulty D., Clarke D.T., Brownlow S., Jones G.R. Effect of temperature on the secondary structure of β-lactoglobulin at pH 6.7, as determined by CD and IR spectroscopy: A test of the molten globule hypothesis. Biochem. J. 1997, 324:341-346.
    • (1997) Biochem. J. , vol.324 , pp. 341-346
    • Qi, X.L.1    Holt, C.2    McNulty, D.3    Clarke, D.T.4    Brownlow, S.5    Jones, G.R.6
  • 39
    • 20844461856 scopus 로고    scopus 로고
    • The kinetics of heat-induced structural changes of beta-lactoglobulin
    • Sava N., Van der Plancken I., Claeys W., Hendrickx M. The kinetics of heat-induced structural changes of beta-lactoglobulin. J. Dairy Sci. 2005, 88:1646-1653.
    • (2005) J. Dairy Sci. , vol.88 , pp. 1646-1653
    • Sava, N.1    Van der Plancken, I.2    Claeys, W.3    Hendrickx, M.4
  • 40
    • 0032795517 scopus 로고    scopus 로고
    • Allergy to bovine β-lactoglobulin: Specificity of human IgE to tryptic peptides
    • Sélo I., Clement G., Bernard H., et al. Allergy to bovine β-lactoglobulin: Specificity of human IgE to tryptic peptides. Clin. Exp. Allergy 1999, 29:1055-1063.
    • (1999) Clin. Exp. Allergy , vol.29 , pp. 1055-1063
    • Sélo, I.1    Clement, G.2    Bernard, H.3
  • 41
    • 84859152164 scopus 로고    scopus 로고
    • Microfluidization as a potential technique to modify surface properties of soy protein isolate
    • Shen L., Tang C.-H. Microfluidization as a potential technique to modify surface properties of soy protein isolate. Food Res. Int. 2012, 48:108-118.
    • (2012) Food Res. Int. , vol.48 , pp. 108-118
    • Shen, L.1    Tang, C.-H.2
  • 42
    • 46749121703 scopus 로고    scopus 로고
    • Circular dichroism study on the early folding events of beta-lactoglobulin entrapped in wet silica gels
    • Shibayama N. Circular dichroism study on the early folding events of beta-lactoglobulin entrapped in wet silica gels. FEBS Lett. 2008, 582:2668-2672.
    • (2008) FEBS Lett. , vol.582 , pp. 2668-2672
    • Shibayama, N.1
  • 43
    • 1542376970 scopus 로고    scopus 로고
    • Modification of ovalbumin with a rare ketohexose through the Maillard reaction: Effect on protein structure and gel properties
    • Sun Y., Hayakawa S., Izumori K. Modification of ovalbumin with a rare ketohexose through the Maillard reaction: Effect on protein structure and gel properties. J. Agric. Food Chem. 2004, 52:1293-1299.
    • (2004) J. Agric. Food Chem. , vol.52 , pp. 1293-1299
    • Sun, Y.1    Hayakawa, S.2    Izumori, K.3
  • 44
    • 0029936006 scopus 로고    scopus 로고
    • Modification of the single unpaired sulfhydryl group of β-1actoglobulin under high pressure and the role of intermolecular S-S exchange in the pressure denaturation
    • Tanaka N., Tsurui Y., Kobayashi I. Modification of the single unpaired sulfhydryl group of β-1actoglobulin under high pressure and the role of intermolecular S-S exchange in the pressure denaturation. Int. J. Biol. Macromol. 1996, 19:63-68.
    • (1996) Int. J. Biol. Macromol. , vol.19 , pp. 63-68
    • Tanaka, N.1    Tsurui, Y.2    Kobayashi, I.3
  • 45
    • 23644445987 scopus 로고    scopus 로고
    • Glycosylation of β-lactoglobulin lowers the heat capacity change of unfolding; a unique way to affect protein thermodynamics
    • van Teeffelen A.M.M., Broersen K., de Jongh H.H.J. Glycosylation of β-lactoglobulin lowers the heat capacity change of unfolding; a unique way to affect protein thermodynamics. Protein Sci. 2005, 14:2187-2194.
    • (2005) Protein Sci. , vol.14 , pp. 2187-2194
    • van Teeffelen, A.M.M.1    Broersen, K.2    de Jongh, H.H.J.3
  • 46
    • 0034974942 scopus 로고    scopus 로고
    • Structure and function of milk allergens
    • Wal J.M. Structure and function of milk allergens. Allergy 2001, 56:35-38.
    • (2001) Allergy , vol.56 , pp. 35-38
    • Wal, J.M.1
  • 47
    • 79955020359 scopus 로고    scopus 로고
    • Deamidated wheat protein-dextran Maillard conjugates: Effect of size and location of polysaccharide conjugated on steric stabilization of emulsions at acidic pH
    • Wong B.T., Day L., Augustin M.A. Deamidated wheat protein-dextran Maillard conjugates: Effect of size and location of polysaccharide conjugated on steric stabilization of emulsions at acidic pH. Food Hydrocoll. 2011, 25:1424-1432.
    • (2011) Food Hydrocoll. , vol.25 , pp. 1424-1432
    • Wong, B.T.1    Day, L.2    Augustin, M.A.3
  • 48
    • 34047104073 scopus 로고    scopus 로고
    • Rheology of whey protein-dextran conjugate films at the air/water interface
    • Wooster T.J., Augustin M.A. Rheology of whey protein-dextran conjugate films at the air/water interface. Food Hydrocoll. 2007, 21:1072-1080.
    • (2007) Food Hydrocoll. , vol.21 , pp. 1072-1080
    • Wooster, T.J.1    Augustin, M.A.2
  • 50
    • 79959302375 scopus 로고    scopus 로고
    • Effect of dynamic high-pressure microfluidization at different temperatures on the antigenic response of bovine β-lactoglobulin
    • Zhong J.Z., Liu C.M., Liu W., et al. Effect of dynamic high-pressure microfluidization at different temperatures on the antigenic response of bovine β-lactoglobulin. Eur. Food Res. Technol. 2011, 233:95-102.
    • (2011) Eur. Food Res. Technol. , vol.233 , pp. 95-102
    • Zhong, J.Z.1    Liu, C.M.2    Liu, W.3
  • 51
    • 84864053225 scopus 로고    scopus 로고
    • Aggregation and conformational changes of bovine β-lactoglobulin subjected to dynamic high-pressure microfluidization in relation to antigenicity
    • Zhong J.Z., Liu W., Liu C.M., et al. Aggregation and conformational changes of bovine β-lactoglobulin subjected to dynamic high-pressure microfluidization in relation to antigenicity. J. Dairy Sci. 2012, 95:4237-4245.
    • (2012) J. Dairy Sci. , vol.95 , pp. 4237-4245
    • Zhong, J.Z.1    Liu, W.2    Liu, C.M.3
  • 52
    • 84876734132 scopus 로고    scopus 로고
    • Antigenicity and functional properties of β-lactoglobulin conjugated with fructo-oligosaccharides in relation to conformational changes
    • Zhong J.Z., Xu Y.J., Liu W., et al. Antigenicity and functional properties of β-lactoglobulin conjugated with fructo-oligosaccharides in relation to conformational changes. J. Dairy Sci. 2013, 96:2808-2815.
    • (2013) J. Dairy Sci. , vol.96 , pp. 2808-2815
    • Zhong, J.Z.1    Xu, Y.J.2    Liu, W.3
  • 53
    • 77949404014 scopus 로고    scopus 로고
    • Physicochemical and emulsifying properties of whey protein isolate (WPI)-dextran conjugates produced in aqueous solution
    • Zhu D., Damodaran S., Lucey J.A. Physicochemical and emulsifying properties of whey protein isolate (WPI)-dextran conjugates produced in aqueous solution. J. Agric. Food Chem. 2010, 58:2988-2994.
    • (2010) J. Agric. Food Chem. , vol.58 , pp. 2988-2994
    • Zhu, D.1    Damodaran, S.2    Lucey, J.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.