메뉴 건너뛰기




Volumn 25, Issue 8, 2011, Pages 1945-1962

β-Lactoglobulin and WPI aggregates: Formation, structure and applications

Author keywords

Cold gelation; Emulsion; Encapsulation; Film; Foam; Lactoglobulin; Protein aggregate; Whey

Indexed keywords

AGGREGATES; EMULSIFICATION; GELATION;

EID: 79961023076     PISSN: 0268005X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.foodhyd.2011.02.006     Document Type: Article
Times cited : (478)

References (230)
  • 2
    • 44449138916 scopus 로고    scopus 로고
    • Peptides are building blocks of heat-induced fibrillar protein aggregates of beta-lactoglobulin formed at pH 2
    • Akkermans C., Venema P., van der Goot A.J., Gruppen H., Bakx E.J., Boom R.M., et al. Peptides are building blocks of heat-induced fibrillar protein aggregates of beta-lactoglobulin formed at pH 2. Biomacromolecules 2008, 9:1474-1479.
    • (2008) Biomacromolecules , vol.9 , pp. 1474-1479
    • Akkermans, C.1    Venema, P.2    van der Goot, A.J.3    Gruppen, H.4    Bakx, E.J.5    Boom, R.M.6
  • 3
    • 57849103415 scopus 로고    scopus 로고
    • Quantitative analysis of confocal laser scanning microscopy images of heat-set globular protein gels
    • Ako K., Durand D., Nicolai T., Becu L. Quantitative analysis of confocal laser scanning microscopy images of heat-set globular protein gels. Food Hydrocolloids 2009, 23:1111-1119.
    • (2009) Food Hydrocolloids , vol.23 , pp. 1111-1119
    • Ako, K.1    Durand, D.2    Nicolai, T.3    Becu, L.4
  • 4
    • 77950793931 scopus 로고    scopus 로고
    • Salt-induced gelation of globular protein aggregates: structure and kinetics
    • Ako K., Nicolai T., Durand D. Salt-induced gelation of globular protein aggregates: structure and kinetics. Biomacromolecules 2010, 11:864-871.
    • (2010) Biomacromolecules , vol.11 , pp. 864-871
    • Ako, K.1    Nicolai, T.2    Durand, D.3
  • 5
    • 77956102828 scopus 로고    scopus 로고
    • Micro-phase separation explains the abrupt structural change of denatured globular protein gels on varying the ionic strength or the pH
    • Ako K., Nicolai T., Durand D., Brotons G. Micro-phase separation explains the abrupt structural change of denatured globular protein gels on varying the ionic strength or the pH. Soft Matter 2009, 5:4033-4041.
    • (2009) Soft Matter , vol.5 , pp. 4033-4041
    • Ako, K.1    Nicolai, T.2    Durand, D.3    Brotons, G.4
  • 6
    • 0036226122 scopus 로고    scopus 로고
    • Comparative evaluation of edible coatings to reduce fat uptake in a deep-fried cereal product
    • Albert S., Mittal G.S. Comparative evaluation of edible coatings to reduce fat uptake in a deep-fried cereal product. Food Research International 2002, 35:445-458.
    • (2002) Food Research International , vol.35 , pp. 445-458
    • Albert, S.1    Mittal, G.S.2
  • 7
    • 0038362143 scopus 로고    scopus 로고
    • Number of thiol groups rather than the size of the aggregates determines the hardness of cold set whey protein gels
    • Alting A.C., Hamer R.J., De Kruif C.G., Paques M., Visschers R.W. Number of thiol groups rather than the size of the aggregates determines the hardness of cold set whey protein gels. Food Hydrocolloids 2003, 17:469-479.
    • (2003) Food Hydrocolloids , vol.17 , pp. 469-479
    • Alting, A.C.1    Hamer, R.J.2    De Kruif, C.G.3    Paques, M.4    Visschers, R.W.5
  • 9
    • 0038746782 scopus 로고    scopus 로고
    • Cold-set globular protein gels: interactions, structure and rheology as a function of protein concentration
    • Alting A.C., Hamer R.J., De Kruif C.G., Visschers R.W. Cold-set globular protein gels: interactions, structure and rheology as a function of protein concentration. Journal of Agricultural and Food Chemistry 2003, 51:3150-3156.
    • (2003) Journal of Agricultural and Food Chemistry , vol.51 , pp. 3150-3156
    • Alting, A.C.1    Hamer, R.J.2    De Kruif, C.G.3    Visschers, R.W.4
  • 13
    • 0000475224 scopus 로고    scopus 로고
    • Mechanical properties, water vapor permeability, and moisture contents of β-lactoglobulin and whey protein films using multivariate analysis
    • Anker M., Stading M., Hermansson A.M. Mechanical properties, water vapor permeability, and moisture contents of β-lactoglobulin and whey protein films using multivariate analysis. Journal of Agricultural and Food Chemistry 1998, 46:1820-1829.
    • (1998) Journal of Agricultural and Food Chemistry , vol.46 , pp. 1820-1829
    • Anker, M.1    Stading, M.2    Hermansson, A.M.3
  • 14
    • 0033795116 scopus 로고    scopus 로고
    • Relationship between the microstructure and the mechanical and barrier properties of whey protein films
    • Anker M., Stading M., Hermansson A.M. Relationship between the microstructure and the mechanical and barrier properties of whey protein films. Journal of Agricultural and Food Chemistry 2000, 48:3806-3816.
    • (2000) Journal of Agricultural and Food Chemistry , vol.48 , pp. 3806-3816
    • Anker, M.1    Stading, M.2    Hermansson, A.M.3
  • 15
    • 0034726483 scopus 로고    scopus 로고
    • Thermodynamic parameters for beta-lactoglobulin dissociation over a broad temperature range at pH 2.6 and 7.0
    • Apenten R.K.O., Galani D. Thermodynamic parameters for beta-lactoglobulin dissociation over a broad temperature range at pH 2.6 and 7.0. Thermochimica Acta 2000, 359:181-188.
    • (2000) Thermochimica Acta , vol.359 , pp. 181-188
    • Apenten, R.K.O.1    Galani, D.2
  • 16
    • 33846274983 scopus 로고    scopus 로고
    • Strong impact of ionic strength on the kinetics of fibrilar aggregation of bovine β-lactoglobulin
    • Arnaudov L.N., De Vries R. Strong impact of ionic strength on the kinetics of fibrilar aggregation of bovine β-lactoglobulin. Biomacromolecules 2006, 7:3490-3498.
    • (2006) Biomacromolecules , vol.7 , pp. 3490-3498
    • Arnaudov, L.N.1    De Vries, R.2
  • 19
    • 2242461391 scopus 로고    scopus 로고
    • Experimental evidence for a two-step process in the aggregation of β-lactoglobulin at pH7
    • Aymard P., Gimel J.C., Nicolai T., Durand D. Experimental evidence for a two-step process in the aggregation of β-lactoglobulin at pH7. Journal de Chimie Physique 1996, 93:987-997.
    • (1996) Journal de Chimie Physique , vol.93 , pp. 987-997
    • Aymard, P.1    Gimel, J.C.2    Nicolai, T.3    Durand, D.4
  • 20
    • 0001417865 scopus 로고    scopus 로고
    • Static and dynamic scattering of β-lactoglobulin aggregates formed after heat-induced denaturation at pH2
    • Aymard P., Nicolai T., Durand D. Static and dynamic scattering of β-lactoglobulin aggregates formed after heat-induced denaturation at pH2. Macromolecules 1999, 35:2542-2552.
    • (1999) Macromolecules , vol.35 , pp. 2542-2552
    • Aymard, P.1    Nicolai, T.2    Durand, D.3
  • 21
    • 33748752323 scopus 로고    scopus 로고
    • Influence of cosolvent systems on the gelation mechanism of globular protein: thermodynamic, kinetic, and structural aspects of globular protein gelation
    • Baier S.K., McClements D.J. Influence of cosolvent systems on the gelation mechanism of globular protein: thermodynamic, kinetic, and structural aspects of globular protein gelation. Comprehensive Reviews in Food Science and Food Safety 2005, 4:43-54.
    • (2005) Comprehensive Reviews in Food Science and Food Safety , vol.4 , pp. 43-54
    • Baier, S.K.1    McClements, D.J.2
  • 22
    • 0142229534 scopus 로고    scopus 로고
    • Effect of pre-heating on the foaming properties of whey protein isolate using a membrane foaming apparatus
    • Bals A., Kulozik U. Effect of pre-heating on the foaming properties of whey protein isolate using a membrane foaming apparatus. International Dairy Journal 2003, 13:903-908.
    • (2003) International Dairy Journal , vol.13 , pp. 903-908
    • Bals, A.1    Kulozik, U.2
  • 24
    • 0000521049 scopus 로고
    • Effects of calcium level on the structure of pre-heated whey protein isolate gels
    • Barbut S. Effects of calcium level on the structure of pre-heated whey protein isolate gels. LWT - Food Science and Technology 1995, 28:598-603.
    • (1995) LWT - Food Science and Technology , vol.28 , pp. 598-603
    • Barbut, S.1
  • 25
    • 0031231835 scopus 로고    scopus 로고
    • Relationships between optical and textural properties of cold-set whey protein gels
    • Barbut S. Relationships between optical and textural properties of cold-set whey protein gels. LWT - Food Science and Technology 1997, 30:590-593.
    • (1997) LWT - Food Science and Technology , vol.30 , pp. 590-593
    • Barbut, S.1
  • 26
    • 0030690259 scopus 로고    scopus 로고
    • Effect of reheating on sodium-induced cold gelation of whey proteins
    • Barbut S., Drake D. Effect of reheating on sodium-induced cold gelation of whey proteins. Food Research International 1997, 30:153-157.
    • (1997) Food Research International , vol.30 , pp. 153-157
    • Barbut, S.1    Drake, D.2
  • 27
    • 84893617475 scopus 로고
    • Ca 2+ induced gelation of pre-heated whey protein isolate
    • Barbut S., Foegeding E.A. Ca 2+ induced gelation of pre-heated whey protein isolate. Journal of Food Science 1993, 58:867-871.
    • (1993) Journal of Food Science , vol.58 , pp. 867-871
    • Barbut, S.1    Foegeding, E.A.2
  • 28
    • 0032001691 scopus 로고    scopus 로고
    • Detection of intermediate oligomers, important for the formation of heat aggregates of β-lactoglobulin
    • Bauer R., Hansen S., Ogendal L. Detection of intermediate oligomers, important for the formation of heat aggregates of β-lactoglobulin. International Dairy Journal 1998, 8:105-112.
    • (1998) International Dairy Journal , vol.8 , pp. 105-112
    • Bauer, R.1    Hansen, S.2    Ogendal, L.3
  • 30
    • 0036196485 scopus 로고    scopus 로고
    • Elaboration and characterization of whey protein beads by an emulsification/cold gelation process: application for the protection of retinol
    • Beaulieu L., Savoie L., Paquin P., Subirade M. Elaboration and characterization of whey protein beads by an emulsification/cold gelation process: application for the protection of retinol. Biomacromolecules 2002, 3:239-248.
    • (2002) Biomacromolecules , vol.3 , pp. 239-248
    • Beaulieu, L.1    Savoie, L.2    Paquin, P.3    Subirade, M.4
  • 31
    • 79851514744 scopus 로고    scopus 로고
    • Enhancement of emulsifying properties of whey proteins by controlling spray-drying parameters
    • Bernard C., Regnault S., Gendreau S., Charbonneau S., Relkin P. Enhancement of emulsifying properties of whey proteins by controlling spray-drying parameters. Food Hydrocolloids 2011, 25:758-763.
    • (2011) Food Hydrocolloids , vol.25 , pp. 758-763
    • Bernard, C.1    Regnault, S.2    Gendreau, S.3    Charbonneau, S.4    Relkin, P.5
  • 32
    • 33947120642 scopus 로고    scopus 로고
    • Structural effects on the permeability of whey protein films in an aqueous environment
    • Bodnár I., Alting A.C., Verschueren M. Structural effects on the permeability of whey protein films in an aqueous environment. Food Hydrocolloids 2007, 21:889-895.
    • (2007) Food Hydrocolloids , vol.21 , pp. 889-895
    • Bodnár, I.1    Alting, A.C.2    Verschueren, M.3
  • 35
    • 33947694371 scopus 로고    scopus 로고
    • Heat-induced whey protein isolate fibrils: conversion, hydrolysis, and disulphide bond formation
    • Bolder S.G., Vasbinder A.J., Sagis L.M.C., van der Linden E. Heat-induced whey protein isolate fibrils: conversion, hydrolysis, and disulphide bond formation. International Dairy Journal 2007, 17:846-853.
    • (2007) International Dairy Journal , vol.17 , pp. 846-853
    • Bolder, S.G.1    Vasbinder, A.J.2    Sagis, L.M.C.3    van der Linden, E.4
  • 36
    • 33847074506 scopus 로고    scopus 로고
    • Characterization and acid-induced gelation of butter oil emulsions produced from heated whey protein dispersions
    • Boutin C., Giroux H.J., Paquin P., Britten M. Characterization and acid-induced gelation of butter oil emulsions produced from heated whey protein dispersions. International Dairy Journal 2007, 17:696-703.
    • (2007) International Dairy Journal , vol.17 , pp. 696-703
    • Boutin, C.1    Giroux, H.J.2    Paquin, P.3    Britten, M.4
  • 37
    • 33847034438 scopus 로고    scopus 로고
    • Heat treatments to improve functional properties of whey proteins
    • International Dairy Federation, Brussels, Belgium
    • Britten M. Heat treatments to improve functional properties of whey proteins. Whey 1998, 189-196. International Dairy Federation, Brussels, Belgium.
    • (1998) Whey , pp. 189-196
    • Britten, M.1
  • 38
    • 0035183519 scopus 로고    scopus 로고
    • Acid-induced gelation of whey protein polymers: effects of pH and calcium concentration during polymerization
    • Britten M., Giroux H.J. Acid-induced gelation of whey protein polymers: effects of pH and calcium concentration during polymerization. Food Hydrocolloids 2001, 15:609-617.
    • (2001) Food Hydrocolloids , vol.15 , pp. 609-617
    • Britten, M.1    Giroux, H.J.2
  • 39
    • 33845611464 scopus 로고    scopus 로고
    • Mechanisms of structure formation in particulate gels of beta-lactoglobulin formed near the isoelectric point
    • Bromley E.H.C., Krebs M.R.H., Donald A.M. Mechanisms of structure formation in particulate gels of beta-lactoglobulin formed near the isoelectric point. European Physical Journal E 2006, 21:145-152.
    • (2006) European Physical Journal E , vol.21 , pp. 145-152
    • Bromley, E.H.C.1    Krebs, M.R.H.2    Donald, A.M.3
  • 40
    • 0032053268 scopus 로고    scopus 로고
    • Molecular basis of protein functionality with special consideration of cold-set gels derived from heat-denatured whey
    • Bryant C.M., McClements D.J. Molecular basis of protein functionality with special consideration of cold-set gels derived from heat-denatured whey. Trends in Food Science and Technology 1998, 9:143-151.
    • (1998) Trends in Food Science and Technology , vol.9 , pp. 143-151
    • Bryant, C.M.1    McClements, D.J.2
  • 41
    • 0033827807 scopus 로고    scopus 로고
    • Influence of NaCl and CaCl2 on cold-set gelation of heat-denatured whey protein
    • Bryant C.M., McClements D.J. Influence of NaCl and CaCl2 on cold-set gelation of heat-denatured whey protein. Journal of Food Science 2000, 65:802-804.
    • (2000) Journal of Food Science , vol.65 , pp. 802-804
    • Bryant, C.M.1    McClements, D.J.2
  • 42
    • 0033862015 scopus 로고    scopus 로고
    • Influence of sucrose on NaCl-induced gelation of heat denatured whey protein solutions
    • Bryant C.M., McClements D.J. Influence of sucrose on NaCl-induced gelation of heat denatured whey protein solutions. Food Research International 2000, 33:649-653.
    • (2000) Food Research International , vol.33 , pp. 649-653
    • Bryant, C.M.1    McClements, D.J.2
  • 44
    • 0028290324 scopus 로고
    • Reversible and irreversible modifications of β-lactoglobulin upon exposure to heat
    • Cairoli S., Iametti S., Bonomi F. Reversible and irreversible modifications of β-lactoglobulin upon exposure to heat. Journal of Protein Chemistry 1994, 13:347-354.
    • (1994) Journal of Protein Chemistry , vol.13 , pp. 347-354
    • Cairoli, S.1    Iametti, S.2    Bonomi, F.3
  • 45
    • 0000053442 scopus 로고
    • Influence of other whey proteins on the heat-induced aggregation of α-lactalbumin
    • Calvo M.M., Leaver J., Banks J.M. Influence of other whey proteins on the heat-induced aggregation of α-lactalbumin. International Dairy Journal 1993, 3:719-727.
    • (1993) International Dairy Journal , vol.3 , pp. 719-727
    • Calvo, M.M.1    Leaver, J.2    Banks, J.M.3
  • 46
    • 23644455100 scopus 로고    scopus 로고
    • The effect of edible eggshell coatings on egg quality and consumer perception
    • Caner C. The effect of edible eggshell coatings on egg quality and consumer perception. Journal of the Science of Food and Agriculture 2005, 85:1897-1902.
    • (2005) Journal of the Science of Food and Agriculture , vol.85 , pp. 1897-1902
    • Caner, C.1
  • 47
    • 26444619899 scopus 로고    scopus 로고
    • Whey protein isolate coating and concentration effects on egg shelf life
    • Caner C. Whey protein isolate coating and concentration effects on egg shelf life. Journal of the Science of Food and Agriculture 2005, 85:2143-2148.
    • (2005) Journal of the Science of Food and Agriculture , vol.85 , pp. 2143-2148
    • Caner, C.1
  • 48
    • 0242720341 scopus 로고    scopus 로고
    • Small-angle X-ray scattering studies of metastable intermediates of - lactoglobulin isolated after heat-induced aggregation
    • Carrotta R., Arleth L., Pedersen J., Bauer R. Small-angle X-ray scattering studies of metastable intermediates of - lactoglobulin isolated after heat-induced aggregation. Biopolymers 2003, 70:377-390.
    • (2003) Biopolymers , vol.70 , pp. 377-390
    • Carrotta, R.1    Arleth, L.2    Pedersen, J.3    Bauer, R.4
  • 49
    • 0034967751 scopus 로고    scopus 로고
    • Conformational characterization of oligomeric intermediates and aggregates in beta-lactoglobulin heat aggregation
    • Carrotta R., Bauer R., Waninge R., Rischel C. Conformational characterization of oligomeric intermediates and aggregates in beta-lactoglobulin heat aggregation. Protein Science 2001, 10:1312-1318.
    • (2001) Protein Science , vol.10 , pp. 1312-1318
    • Carrotta, R.1    Bauer, R.2    Waninge, R.3    Rischel, C.4
  • 51
    • 34748907965 scopus 로고    scopus 로고
    • The effects of acidification rate, pH and ageing time on the acidic cold set gelation of whey proteins
    • Cavallieri A.L.F., da Cunha R.L. The effects of acidification rate, pH and ageing time on the acidic cold set gelation of whey proteins. Food Hydrocolloids 2008, 22:439-448.
    • (2008) Food Hydrocolloids , vol.22 , pp. 439-448
    • Cavallieri, A.L.F.1    da Cunha, R.L.2
  • 52
    • 77955992292 scopus 로고    scopus 로고
    • Effects of the free and pre-encapsulated calcium ions on the physical properties of whey protein edible film
    • Chai Z., Shang J., Jiang Y., Ren F., Leng X. Effects of the free and pre-encapsulated calcium ions on the physical properties of whey protein edible film. International Journal of Food Science and Technology 2010, 45:1532-1538.
    • (2010) International Journal of Food Science and Technology , vol.45 , pp. 1532-1538
    • Chai, Z.1    Shang, J.2    Jiang, Y.3    Ren, F.4    Leng, X.5
  • 56
    • 1942441014 scopus 로고    scopus 로고
    • Spectroscopic characterization of heat-induced nonnative beta-lactoglobulin monomers
    • Croguennec T., Molle D., Mehra R., Bouhallab S. Spectroscopic characterization of heat-induced nonnative beta-lactoglobulin monomers. Protein Science 2004, 13:1340-1346.
    • (2004) Protein Science , vol.13 , pp. 1340-1346
    • Croguennec, T.1    Molle, D.2    Mehra, R.3    Bouhallab, S.4
  • 57
    • 1542575976 scopus 로고    scopus 로고
    • Heat-induced denaturation/aggregation of β-lactoglobulin A and B: kinetics of the first intermediates formed
    • Croguennec T., O'Kennedy B.T., Mehra R. Heat-induced denaturation/aggregation of β-lactoglobulin A and B: kinetics of the first intermediates formed. International Dairy Journal 2004, 14:399-409.
    • (2004) International Dairy Journal , vol.14 , pp. 399-409
    • Croguennec, T.1    O'Kennedy, B.T.2    Mehra, R.3
  • 58
    • 0001406422 scopus 로고    scopus 로고
    • Interaction between α-lactalbumin and β-lactoglobulin in the early stage s of heat denaturation
    • Dalgleish D.G., Senaratne V., Francois S. Interaction between α-lactalbumin and β-lactoglobulin in the early stage s of heat denaturation. Journal of Agricultural and Food Chemistry 1997, 45:3459-3464.
    • (1997) Journal of Agricultural and Food Chemistry , vol.45 , pp. 3459-3464
    • Dalgleish, D.G.1    Senaratne, V.2    Francois, S.3
  • 59
    • 84987367516 scopus 로고
    • Reaction kinetics on the denaturation of whey proteins in milk
    • Dannenberg F., Kessler H.G. Reaction kinetics on the denaturation of whey proteins in milk. Journal of Food Science 1988, 53:258-263.
    • (1988) Journal of Food Science , vol.53 , pp. 258-263
    • Dannenberg, F.1    Kessler, H.G.2
  • 60
    • 3142571046 scopus 로고    scopus 로고
    • Foaming and interfacial properties of polymerized whey protein isolate
    • Davis J.P., Foegeding E.A. Foaming and interfacial properties of polymerized whey protein isolate. Journal of Food Science 2004, 69:C404-C410.
    • (2004) Journal of Food Science , vol.69
    • Davis, J.P.1    Foegeding, E.A.2
  • 61
    • 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. Journal of Dairy Science 2009, 92:1387-1397.
    • (2009) Journal of Dairy Science , vol.92 , pp. 1387-1397
    • Dissanayake, M.1    Vasiljevic, T.2
  • 62
    • 77952308745 scopus 로고    scopus 로고
    • Efficacy of whey protein gel networks as potential viability-enhancing scaffolds for cell immobilization of lactobacillus rhamnosus GG
    • Doherty S.B., Gee V.L., Ross R.P., Stanton C., Fitzgerald G.F., Brodkorb A. Efficacy of whey protein gel networks as potential viability-enhancing scaffolds for cell immobilization of lactobacillus rhamnosus GG. Journal of Microbiological Methods 2010, 80:231-241.
    • (2010) Journal of Microbiological Methods , vol.80 , pp. 231-241
    • Doherty, S.B.1    Gee, V.L.2    Ross, R.P.3    Stanton, C.4    Fitzgerald, G.F.5    Brodkorb, A.6
  • 64
    • 38049062509 scopus 로고    scopus 로고
    • Thermal dependence of thermally induced protein spherulite formation and growth: kinetics of beta-lactoglobulin and insulin
    • Domike K.R., Donald A.M. Thermal dependence of thermally induced protein spherulite formation and growth: kinetics of beta-lactoglobulin and insulin. Biomacromolecules 2007, 8:3930-3937.
    • (2007) Biomacromolecules , vol.8 , pp. 3930-3937
    • Domike, K.R.1    Donald, A.M.2
  • 65
    • 79851510676 scopus 로고    scopus 로고
    • Mixtures of whey protein microgels and soluble aggregates as building blocks to control rheology and structure of acid induced cold-set gels
    • Donato L., Kolodziejczyk E., Rouvet M. Mixtures of whey protein microgels and soluble aggregates as building blocks to control rheology and structure of acid induced cold-set gels. Food Hydrocolloids 2011, 25:734-742.
    • (2011) Food Hydrocolloids , vol.25 , pp. 734-742
    • Donato, L.1    Kolodziejczyk, E.2    Rouvet, M.3
  • 66
    • 60349109570 scopus 로고    scopus 로고
    • Mechanism of formation of stable heat-induced β-lactoglobulin microgels
    • Donato L., Schmitt C., Bovetto L., Rouvet M. Mechanism of formation of stable heat-induced β-lactoglobulin microgels. International Dairy Journal 2009, 19:295-306.
    • (2009) International Dairy Journal , vol.19 , pp. 295-306
    • Donato, L.1    Schmitt, C.2    Bovetto, L.3    Rouvet, M.4
  • 68
    • 21644432768 scopus 로고    scopus 로고
    • Acid-induced gelation of enzymatically modified, preheated whey proteins
    • Eissa A.S., Khan S.A. Acid-induced gelation of enzymatically modified, preheated whey proteins. Journal of Agricultural and Food Chemistry 2005, 53:5010-5017.
    • (2005) Journal of Agricultural and Food Chemistry , vol.53 , pp. 5010-5017
    • Eissa, A.S.1    Khan, S.A.2
  • 70
    • 40849094204 scopus 로고    scopus 로고
    • Dynamic rearrangement of disulfide bridges influences solubility of whey protein coatings
    • Floris R., Bodnár I., Weinbreck F., Alting A.C. Dynamic rearrangement of disulfide bridges influences solubility of whey protein coatings. International Dairy Journal 2008, 18:566-573.
    • (2008) International Dairy Journal , vol.18 , pp. 566-573
    • Floris, R.1    Bodnár, I.2    Weinbreck, F.3    Alting, A.C.4
  • 71
    • 0000706426 scopus 로고    scopus 로고
    • Heat-induced denaturation and aggregation of beta-lactoglobulin: kinetics of formation of hydrophobic and disulphide-linked aggregates
    • Galani D., Apenten R.K.O. Heat-induced denaturation and aggregation of beta-lactoglobulin: kinetics of formation of hydrophobic and disulphide-linked aggregates. International Journal of Food Science and Technology 1999, 34:467-476.
    • (1999) International Journal of Food Science and Technology , vol.34 , pp. 467-476
    • Galani, D.1    Apenten, R.K.O.2
  • 72
    • 0001592750 scopus 로고    scopus 로고
    • Heat-induced interactions and gelation of mixtures of beta-lactoglobulin and α-lactalbumin
    • Gezimati J., Creamer L.K., Singh H. Heat-induced interactions and gelation of mixtures of beta-lactoglobulin and α-lactalbumin. Journal of Agricultural and Food Chemistry 1997, 45:1130-1136.
    • (1997) Journal of Agricultural and Food Chemistry , vol.45 , pp. 1130-1136
    • Gezimati, J.1    Creamer, L.K.2    Singh, H.3
  • 73
    • 75149130837 scopus 로고    scopus 로고
    • Preparation of nanoparticles from denatured whey protein by pH-cycling treatment
    • Giroux H.J., Houde J., Britten M. Preparation of nanoparticles from denatured whey protein by pH-cycling treatment. Food Hydrocolloids 2010, 24:341-346.
    • (2010) Food Hydrocolloids , vol.24 , pp. 341-346
    • Giroux, H.J.1    Houde, J.2    Britten, M.3
  • 74
    • 33745956842 scopus 로고    scopus 로고
    • Effect of two-stage heating on Na+-induced gelation of whey protein isolate
    • Glibowski P., Mleko S., Wasko A., Kristinsson H.G. Effect of two-stage heating on Na+-induced gelation of whey protein isolate. Milchwissenschaft 2006, 61:252-255.
    • (2006) Milchwissenschaft , vol.61 , pp. 252-255
    • Glibowski, P.1    Mleko, S.2    Wasko, A.3    Kristinsson, H.G.4
  • 75
    • 9744228666 scopus 로고    scopus 로고
    • Fibrillar β-lactoglobulin gels: part 1. Fibril formation and structure
    • Gosal W.S., Clark A.H., Ross-Murphy S.B. Fibrillar β-lactoglobulin gels: part 1. Fibril formation and structure. Biomacromolecules 2004, 5:2408-2419.
    • (2004) Biomacromolecules , vol.5 , pp. 2408-2419
    • Gosal, W.S.1    Clark, A.H.2    Ross-Murphy, S.B.3
  • 76
    • 33645991503 scopus 로고    scopus 로고
    • Properties of and mechanisms of protein interactions in films formed from different proportions of heated and unheated whey protein solutions
    • Guckian S., Dwyer C., O'Sullivan M., O'Riordan E.D., Monahan F.J. Properties of and mechanisms of protein interactions in films formed from different proportions of heated and unheated whey protein solutions. European Food Research and Technology 2006, 223:91-95.
    • (2006) European Food Research and Technology , vol.223 , pp. 91-95
    • Guckian, S.1    Dwyer, C.2    O'Sullivan, M.3    O'Riordan, E.D.4    Monahan, F.J.5
  • 77
    • 0242489071 scopus 로고    scopus 로고
    • Protection of bifidobacteria encapsulated in polysaccharide-protein gel beads against gastric juice and bile
    • Guérin D., Vuillemard J.C., Subirade M. Protection of bifidobacteria encapsulated in polysaccharide-protein gel beads against gastric juice and bile. Journal of Food Protection 2003, 66:2076-2084.
    • (2003) Journal of Food Protection , vol.66 , pp. 2076-2084
    • Guérin, D.1    Vuillemard, J.C.2    Subirade, M.3
  • 78
    • 34249039632 scopus 로고    scopus 로고
    • Use of whey proteins for encapsulation and controlled delivery applications
    • Gunasekaran S., Ko S., Xiao L. Use of whey proteins for encapsulation and controlled delivery applications. Journal of Food Engineering 2007, 83:31-40.
    • (2007) Journal of Food Engineering , vol.83 , pp. 31-40
    • Gunasekaran, S.1    Ko, S.2    Xiao, L.3
  • 81
    • 53549135187 scopus 로고    scopus 로고
    • Coating of peanuts with edible whey protein film containing α-tocopherol and ascorbyl palmitate
    • Han J.H., Hwang H.M., Min S., Krochta J.M. Coating of peanuts with edible whey protein film containing α-tocopherol and ascorbyl palmitate. Journal of Food Science 2008, 73:E349-E355.
    • (2008) Journal of Food Science , vol.73
    • Han, J.H.1    Hwang, H.M.2    Min, S.3    Krochta, J.M.4
  • 82
    • 34250903534 scopus 로고    scopus 로고
    • Physical properties of whey protein coating solutions and films containing antioxidants
    • Han J.H., Krochta J.M. Physical properties of whey protein coating solutions and films containing antioxidants. Journal of Food Science 2007, 72:E308-E314.
    • (2007) Journal of Food Science , vol.72
    • Han, J.H.1    Krochta, J.M.2
  • 83
    • 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. Journal of Dairy Research 2001, 68:483-497.
    • (2001) Journal of Dairy Research , vol.68 , pp. 483-497
    • Havea, P.1    Singh, H.2    Creamer, L.K.3
  • 86
    • 0031973267 scopus 로고    scopus 로고
    • Preparation and evaluation of microspheres prepared from whey protein isolate
    • Heelan B.A., Corrigan O.I. Preparation and evaluation of microspheres prepared from whey protein isolate. Journal of Microencapsulation 1998, 15:93-105.
    • (1998) Journal of Microencapsulation , vol.15 , pp. 93-105
    • Heelan, B.A.1    Corrigan, O.I.2
  • 87
    • 0002677279 scopus 로고
    • Thermal stability of β-lactoglobulin as a function of pH and the relative concentration of sodium dodecylsulphate
    • Hegg P.-O. Thermal stability of β-lactoglobulin as a function of pH and the relative concentration of sodium dodecylsulphate. Acta Agriculture Scandinavica 1980, 30.
    • (1980) Acta Agriculture Scandinavica , vol.30
    • Hegg, P.-O.1
  • 88
  • 89
    • 0000266449 scopus 로고
    • Interactions of α-lactalbumin and bovine serum albumin with β-lactoglobulin in thermally induced gelation
    • Hines M.E., Foegeding E.A. Interactions of α-lactalbumin and bovine serum albumin with β-lactoglobulin in thermally induced gelation. Journal of Agricultural and Food Chemistry 1993, 41:341-346.
    • (1993) Journal of Agricultural and Food Chemistry , vol.41 , pp. 341-346
    • Hines, M.E.1    Foegeding, E.A.2
  • 90
    • 0000008542 scopus 로고    scopus 로고
    • Heat-induced agregation of β-lactoglobulin: role of free thiol group and disulfide bonds
    • Hoffmann M.A.M., van Mil P.J.J.M. Heat-induced agregation of β-lactoglobulin: role of free thiol group and disulfide bonds. Journal of Agricultural and Food Chemistry 1997, 45:2942.
    • (1997) Journal of Agricultural and Food Chemistry , vol.45 , pp. 2942
    • Hoffmann, M.A.M.1    van Mil, P.J.J.M.2
  • 92
    • 0036230909 scopus 로고    scopus 로고
    • Changed protein structures of bovine β-lactoglobulin B and α-lactalbumin as a consequence of heat treatment
    • Hong Y.H., Creamer L.K. Changed protein structures of bovine β-lactoglobulin B and α-lactalbumin as a consequence of heat treatment. International Dairy Journal 2002, 12:345-359.
    • (2002) International Dairy Journal , vol.12 , pp. 345-359
    • Hong, Y.H.1    Creamer, L.K.2
  • 93
    • 0030093730 scopus 로고    scopus 로고
    • Ca2+-induced gelation of whey protein isolate: effects of pre-heating
    • Hongsprabhas P., Barbut S. Ca2+-induced gelation of whey protein isolate: effects of pre-heating. Food Research International 1996, 29:135-139.
    • (1996) Food Research International , vol.29 , pp. 135-139
    • Hongsprabhas, P.1    Barbut, S.2
  • 94
    • 0030919028 scopus 로고    scopus 로고
    • Protein and salt effects on Ca2+-induced cold gelation of whey protein isolate
    • Hongsprabhas P., Barbut S. Protein and salt effects on Ca2+-induced cold gelation of whey protein isolate. Journal of Food Science 1997, 62:382-385.
    • (1997) Journal of Food Science , vol.62 , pp. 382-385
    • Hongsprabhas, P.1    Barbut, S.2
  • 95
    • 0031582836 scopus 로고    scopus 로고
    • Structure-forming processes in Ca2+-induced whey protein isolate cold gelation
    • Hongsprabhas P., Barbut S. Structure-forming processes in Ca2+-induced whey protein isolate cold gelation. International Dairy Journal 1997, 7:827-834.
    • (1997) International Dairy Journal , vol.7 , pp. 827-834
    • Hongsprabhas, P.1    Barbut, S.2
  • 96
    • 0031200774 scopus 로고    scopus 로고
    • Calcium-induced cold gelation of whey protein isolate: effect of two-stage gelation
    • Hongsprabhas P., Barbut S. Calcium-induced cold gelation of whey protein isolate: effect of two-stage gelation. Food Research International 1998, 30:523-527.
    • (1998) Food Research International , vol.30 , pp. 523-527
    • Hongsprabhas, P.1    Barbut, S.2
  • 97
    • 0032863353 scopus 로고    scopus 로고
    • Effect of pre-heated whey protein level and salt on texture development of poultry meat batters
    • Hongsprabhas P., Barbut S. Effect of pre-heated whey protein level and salt on texture development of poultry meat batters. Food Research International 1999, 32:145-149.
    • (1999) Food Research International , vol.32 , pp. 145-149
    • Hongsprabhas, P.1    Barbut, S.2
  • 98
    • 0033160341 scopus 로고    scopus 로고
    • Use of cold-set whey protein gelation to improve poultry meat batters
    • Hongsprabhas P., Barbut S. Use of cold-set whey protein gelation to improve poultry meat batters. Poultry Science 1999, 78:1074-1078.
    • (1999) Poultry Science , vol.78 , pp. 1074-1078
    • Hongsprabhas, P.1    Barbut, S.2
  • 99
    • 0002284922 scopus 로고
    • Modifications of higher order structures upon heating of β-lactoglobulin: dependence on the protein concentration
    • Iametti S., Cairoli S., De Gregori B., Bonomi F. Modifications of higher order structures upon heating of β-lactoglobulin: dependence on the protein concentration. Journal of Agricultural and Food Chemistry 1995, 43:53.
    • (1995) Journal of Agricultural and Food Chemistry , vol.43 , pp. 53
    • Iametti, S.1    Cairoli, S.2    De Gregori, B.3    Bonomi, F.4
  • 100
    • 0029924648 scopus 로고    scopus 로고
    • Modifications occur at different structural levels during the heat denaturation of β-lactoglobulin
    • Iametti S., De Gregori B., Vecchio G., Bonomi F. Modifications occur at different structural levels during the heat denaturation of β-lactoglobulin. European Journal of Biochemistry 1996, 237.
    • (1996) European Journal of Biochemistry , vol.237
    • Iametti, S.1    De Gregori, B.2    Vecchio, G.3    Bonomi, F.4
  • 101
    • 1542299045 scopus 로고    scopus 로고
    • Raman spectroscopy of heat-induced fine-stranded and particulate β-lactoglobulin gels
    • Ikeda S., Li-Chan E.C.Y. Raman spectroscopy of heat-induced fine-stranded and particulate β-lactoglobulin gels. Food Hydrocolloids 2004, 18:489-498.
    • (2004) Food Hydrocolloids , vol.18 , pp. 489-498
    • Ikeda, S.1    Li-Chan, E.C.Y.2
  • 102
    • 0001356218 scopus 로고    scopus 로고
    • Gelation of pH-aggregated whey protein isolate solution induced by heat, protease, calcium salt, and acidulant
    • Ju Y.Z., Kilara A. Gelation of pH-aggregated whey protein isolate solution induced by heat, protease, calcium salt, and acidulant. Journal of Agricultural and Food Chemistry 1998, 46:1830-1835.
    • (1998) Journal of Agricultural and Food Chemistry , vol.46 , pp. 1830-1835
    • Ju, Y.Z.1    Kilara, A.2
  • 103
    • 0001356218 scopus 로고    scopus 로고
    • Gelation of pH-aggregated whey protein isolate solution induced by heat, protease, calcium salt, and acidulant
    • Ju Z.Y., Kilara A. Gelation of pH-aggregated whey protein isolate solution induced by heat, protease, calcium salt, and acidulant. Journal of Agricultural and Food Chemistry 1998, 46:1830-1835.
    • (1998) Journal of Agricultural and Food Chemistry , vol.46 , pp. 1830-1835
    • Ju, Z.Y.1    Kilara, A.2
  • 104
    • 0011809763 scopus 로고    scopus 로고
    • Properties of Gels Induced by heat, protease, calcium salt, and acidulant from calcium ion-aggregated whey protein isolate
    • Ju Z.Y., Kilara A. Properties of Gels Induced by heat, protease, calcium salt, and acidulant from calcium ion-aggregated whey protein isolate. Journal of Dairy Science 1998, 81:1236-1243.
    • (1998) Journal of Dairy Science , vol.81 , pp. 1236-1243
    • Ju, Z.Y.1    Kilara, A.2
  • 105
    • 0031878278 scopus 로고    scopus 로고
    • Textural properties of cold-set gels induced from heat-denatured whey protein isolates
    • Ju Z.Y., Kilara A. Textural properties of cold-set gels induced from heat-denatured whey protein isolates. Journal of Food Science 1998, 63:288-292.
    • (1998) Journal of Food Science , vol.63 , pp. 288-292
    • Ju, Z.Y.1    Kilara, A.2
  • 106
    • 79952112477 scopus 로고    scopus 로고
    • Interfacial activity and interfacial shear rheology of native β-lactoglobulin monomers and their heat-induced fibers
    • Jung J.-M., Gunes D., Mezzenga R. Interfacial activity and interfacial shear rheology of native β-lactoglobulin monomers and their heat-induced fibers. Langmuir 2010, 26:15366-15375.
    • (2010) Langmuir , vol.26 , pp. 15366-15375
    • Jung, J.-M.1    Gunes, D.2    Mezzenga, R.3
  • 107
    • 52649129277 scopus 로고    scopus 로고
    • Structure of heat-induced beta-lactoglobulin aggregates and their complexes with sodium-dodecyl sulfate
    • Jung J.M., Savin G., Pouzot M., Schmitt C., Mezzenga R. Structure of heat-induced beta-lactoglobulin aggregates and their complexes with sodium-dodecyl sulfate. Biomacromolecules 2008, 9:2477-2486.
    • (2008) Biomacromolecules , vol.9 , pp. 2477-2486
    • Jung, J.M.1    Savin, G.2    Pouzot, M.3    Schmitt, C.4    Mezzenga, R.5
  • 108
    • 0034270555 scopus 로고    scopus 로고
    • Heat-induced gelation of α-lactalbumin/β-lactoglobulin blends at pH 3 and pH 7
    • Kavanagh G.M., Clark A.H., Gosal W.S., Ross-Murphy S.B. Heat-induced gelation of α-lactalbumin/β-lactoglobulin blends at pH 3 and pH 7. Macromolecules 2000, 33:7029-7037.
    • (2000) Macromolecules , vol.33 , pp. 7029-7037
    • Kavanagh, G.M.1    Clark, A.H.2    Gosal, W.S.3    Ross-Murphy, S.B.4
  • 110
    • 0142123418 scopus 로고    scopus 로고
    • Characterization of soluble aggregates from whey protein isolate
    • Kazmierski M., Corredig M. Characterization of soluble aggregates from whey protein isolate. Food Hydrocolloids 2003, 17:685-692.
    • (2003) Food Hydrocolloids , vol.17 , pp. 685-692
    • Kazmierski, M.1    Corredig, M.2
  • 112
  • 113
    • 0034835681 scopus 로고    scopus 로고
    • Solubility and moisture sorption isotherms of whey-protein-based edible films as influenced by lipid and plasticizer incorporation
    • Kim S.J., Ustunol Z. Solubility and moisture sorption isotherms of whey-protein-based edible films as influenced by lipid and plasticizer incorporation. Journal of Agricultural and Food Chemistry 2001, 49:4388-4391.
    • (2001) Journal of Agricultural and Food Chemistry , vol.49 , pp. 4388-4391
    • Kim, S.J.1    Ustunol, Z.2
  • 114
    • 0029838336 scopus 로고    scopus 로고
    • Viscous sol and gel formation from process whey protein below 25 °C
    • Kitabatake N., Fujita Y., Kinekawa Y.I. Viscous sol and gel formation from process whey protein below 25 °C. Journal of Food Science 1996, 61:500-503.
    • (1996) Journal of Food Science , vol.61 , pp. 500-503
    • Kitabatake, N.1    Fujita, Y.2    Kinekawa, Y.I.3
  • 115
    • 0001281310 scopus 로고
    • Heat-induced and transparent gel prepared from hen egg ovalbumin in the presence of salt by a two-step heating method
    • Kitabatake N., Hatta H., Doi E. Heat-induced and transparent gel prepared from hen egg ovalbumin in the presence of salt by a two-step heating method. Agricultural & Biological Chemistry 1987, 51:771-778.
    • (1987) Agricultural & Biological Chemistry , vol.51 , pp. 771-778
    • Kitabatake, N.1    Hatta, H.2    Doi, E.3
  • 116
    • 42149148462 scopus 로고    scopus 로고
    • Droplet surface properties and rheology of concentrated oil in water emulsions stabilized by heat-modified β-lactoglobulin B
    • Knudsen J.C., Øgendal L.H., Skibsted L.H. Droplet surface properties and rheology of concentrated oil in water emulsions stabilized by heat-modified β-lactoglobulin B. Langmuir 2008, 24:2603-2610.
    • (2008) Langmuir , vol.24 , pp. 2603-2610
    • Knudsen, J.C.1    Øgendal, L.H.2    Skibsted, L.H.3
  • 117
    • 68949142908 scopus 로고    scopus 로고
    • Amyloid fibril-like structure underlies the aggregate structure across the ph range for beta-lactoglobulin
    • Krebs M.R.H., Devlin G.L., Donald A.M. Amyloid fibril-like structure underlies the aggregate structure across the ph range for beta-lactoglobulin. Biophysical Journal 2009, 96:5013-5019.
    • (2009) Biophysical Journal , vol.96 , pp. 5013-5019
    • Krebs, M.R.H.1    Devlin, G.L.2    Donald, A.M.3
  • 118
    • 67249141423 scopus 로고    scopus 로고
    • The critical aggregation concentration of beta-lactoglobulin-based fibril formation
    • Kroes-Nijboer A., Venema P., Bouman J., van der Linden E. The critical aggregation concentration of beta-lactoglobulin-based fibril formation. Food Biophysics 2009, 4:59-63.
    • (2009) Food Biophysics , vol.4 , pp. 59-63
    • Kroes-Nijboer, A.1    Venema, P.2    Bouman, J.3    van der Linden, E.4
  • 121
    • 53649087847 scopus 로고    scopus 로고
    • In vitro analysis of protection of the enzyme bile salt hydrolase against enteric conditions by whey protein-gum arabic microencapsulation
    • Lambert J.M., Weinbreck F., Kleerebezem M. In vitro analysis of protection of the enzyme bile salt hydrolase against enteric conditions by whey protein-gum arabic microencapsulation. Journal of Agricultural and Food Chemistry 2008, 56:8360-8364.
    • (2008) Journal of Agricultural and Food Chemistry , vol.56 , pp. 8360-8364
    • Lambert, J.M.1    Weinbreck, F.2    Kleerebezem, M.3
  • 122
    • 85025567869 scopus 로고
    • Fine-stranded and particulate gels of β-lactoglobulin and whey protein at varying pH
    • Langton M., Hermannsson A. Fine-stranded and particulate gels of β-lactoglobulin and whey protein at varying pH. Food Hydrocolloids 1992, 5:523-539.
    • (1992) Food Hydrocolloids , vol.5 , pp. 523-539
    • Langton, M.1    Hermannsson, A.2
  • 123
    • 0034030911 scopus 로고    scopus 로고
    • Effect of pH on the thermal denaturation of whey proteins in milk
    • Law A.J.R., Leaver J. Effect of pH on the thermal denaturation of whey proteins in milk. Journal of Agricultural and Food Chemistry 2000, 48:672-679.
    • (2000) Journal of Agricultural and Food Chemistry , vol.48 , pp. 672-679
    • Law, A.J.R.1    Leaver, J.2
  • 124
    • 0036380798 scopus 로고    scopus 로고
    • Influence of genetic variation on the aggregation of heat-denatured β-lactoglobulin
    • Le Bon C., Durand D., Nicolai T. Influence of genetic variation on the aggregation of heat-denatured β-lactoglobulin. International Dairy Journal 2002, 12:671-678.
    • (2002) International Dairy Journal , vol.12 , pp. 671-678
    • Le Bon, C.1    Durand, D.2    Nicolai, T.3
  • 126
    • 0342374989 scopus 로고    scopus 로고
    • Kinetics of aggregation and gelation of globular proteins after heat-induced denaturation
    • Le Bon C., Nicolai T., Durand D. Kinetics of aggregation and gelation of globular proteins after heat-induced denaturation. Macromolecules 1999, 32:6120-6127.
    • (1999) Macromolecules , vol.32 , pp. 6120-6127
    • Le Bon, C.1    Nicolai, T.2    Durand, D.3
  • 127
    • 0034940208 scopus 로고    scopus 로고
    • Milk protein coatings prevent oxidative browning of apples and potatoes
    • Le Tien C., Vachon C., Mateescu M.A., Lacroix M. Milk protein coatings prevent oxidative browning of apples and potatoes. Journal of Food Science 2001, 66:512-516.
    • (2001) Journal of Food Science , vol.66 , pp. 512-516
    • Le Tien, C.1    Vachon, C.2    Mateescu, M.A.3    Lacroix, M.4
  • 129
    • 33748975516 scopus 로고    scopus 로고
    • Fluidized-bed system for whey protein film coating of peanuts
    • Lin S.Y., Krochta J.M. Fluidized-bed system for whey protein film coating of peanuts. Journal of Food Process Engineering 2006, 29:532-546.
    • (2006) Journal of Food Process Engineering , vol.29 , pp. 532-546
    • Lin, S.Y.1    Krochta, J.M.2
  • 130
    • 21644478516 scopus 로고    scopus 로고
    • Whey protein coating efficiency on surfactant-modified hydrophobic surfaces
    • Lin S.Y.D., Krochta J.M. Whey protein coating efficiency on surfactant-modified hydrophobic surfaces. Journal of Agricultural and Food Chemistry 2005, 53:5018-5023.
    • (2005) Journal of Agricultural and Food Chemistry , vol.53 , pp. 5018-5023
    • Lin, S.Y.D.1    Krochta, J.M.2
  • 131
    • 8644288237 scopus 로고    scopus 로고
    • Cold gelation of β-lactoglobulin oil-in-water emulsion
    • Line V.L.S., Remondetto G.E., Subirade M. Cold gelation of β-lactoglobulin oil-in-water emulsion. Food Hydrocolloids 2005, 19:269-278.
    • (2005) Food Hydrocolloids , vol.19 , pp. 269-278
    • Line, V.L.S.1    Remondetto, G.E.2    Subirade, M.3
  • 133
    • 0346336103 scopus 로고    scopus 로고
    • Steric effects governing disulfide bond interchange during thermal aggregation in solutions of β-lactoglobulin B and α-lactalbumin
    • Livney Y.D., Verespej E., Dalgleish D.G. Steric effects governing disulfide bond interchange during thermal aggregation in solutions of β-lactoglobulin B and α-lactalbumin. Journal of Agricultural and Food Chemistry 2003, 51:8098-8106.
    • (2003) Journal of Agricultural and Food Chemistry , vol.51 , pp. 8098-8106
    • Livney, Y.D.1    Verespej, E.2    Dalgleish, D.G.3
  • 134
    • 84988213629 scopus 로고
    • Physical properties of cold-setting gels formed from heat-denatured whey protein isolate
    • McClements D.J., Keogh M.K. Physical properties of cold-setting gels formed from heat-denatured whey protein isolate. Journal of the Science of Food and Agriculture 1995, 69:7-14.
    • (1995) Journal of the Science of Food and Agriculture , vol.69 , pp. 7-14
    • McClements, D.J.1    Keogh, M.K.2
  • 135
    • 84988213629 scopus 로고
    • Physical properties of cold-setting gels formed from heat-denatured whey protein isolate
    • McClements D.J., Keogh M.K. Physical properties of cold-setting gels formed from heat-denatured whey protein isolate. Journal of the Science of Food Agriculture 1995, 69:7-14.
    • (1995) Journal of the Science of Food Agriculture , vol.69 , pp. 7-14
    • McClements, D.J.1    Keogh, M.K.2
  • 138
    • 34247639374 scopus 로고    scopus 로고
    • Light-scattering study of the structure of aggregates and gels formed by heat-denatured whey protein isolate and β-lactoglobulin at neutral pH
    • Mahmoudi N., Mehalebi S., Nicolai T., Durand D., Riaublanc A. Light-scattering study of the structure of aggregates and gels formed by heat-denatured whey protein isolate and β-lactoglobulin at neutral pH. Journal of Agricultural and Food Chemistry 2007, 55:3104-3111.
    • (2007) Journal of Agricultural and Food Chemistry , vol.55 , pp. 3104-3111
    • Mahmoudi, N.1    Mehalebi, S.2    Nicolai, T.3    Durand, D.4    Riaublanc, A.5
  • 139
    • 33751421851 scopus 로고    scopus 로고
    • Electrostatically driven protein aggregation: α-lactalbumin at low ionic strength
    • Majhi P.R., Ganta R.R., Vanam R.P., Seyrek E., Giger K., Dubin P.L. Electrostatically driven protein aggregation: α-lactalbumin at low ionic strength. Langmuir 2006, 22:9150-9159.
    • (2006) Langmuir , vol.22 , pp. 9150-9159
    • Majhi, P.R.1    Ganta, R.R.2    Vanam, R.P.3    Seyrek, E.4    Giger, K.5    Dubin, P.L.6
  • 140
    • 0001205312 scopus 로고    scopus 로고
    • Effect of heat-treatment on the conformation and aggregation of β-lactoglobulin A, B and C
    • Manderson G.A., Hardman M.J., Creamer L.K. Effect of heat-treatment on the conformation and aggregation of β-lactoglobulin A, B and C. Journal of Agricultural and Food Chemistry 1998, 46:5052-5061.
    • (1998) Journal of Agricultural and Food Chemistry , vol.46 , pp. 5052-5061
    • Manderson, G.A.1    Hardman, M.J.2    Creamer, L.K.3
  • 141
    • 0032839589 scopus 로고    scopus 로고
    • Effect of heat treatment on bovine β-lactoglobulin A, B and C explored using thiol availibility 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 availibility and fluorescence. Journal of Agricultural and Food Chemistry 1999, 47:3617-3627.
    • (1999) Journal of Agricultural and Food Chemistry , vol.47 , pp. 3617-3627
    • Manderson, G.A.1    Hardman, M.J.2    Creamer, L.K.3
  • 142
    • 0033833121 scopus 로고    scopus 로고
    • On the structure of particulate gels - the case of salt-induced cold gelation of heat-denatured whey protein isolate
    • Marangoni A.G., Barbut S., McGauley S.E., Marcone M., Narine S.S. On the structure of particulate gels - the case of salt-induced cold gelation of heat-denatured whey protein isolate. Food Hydrocolloids 2000, 14:61-74.
    • (2000) Food Hydrocolloids , vol.14 , pp. 61-74
    • Marangoni, A.G.1    Barbut, S.2    McGauley, S.E.3    Marcone, M.4    Narine, S.S.5
  • 144
    • 41149173263 scopus 로고    scopus 로고
    • The influence of electrostatic interaction on the structure and the shear modulus of heat-set globular protein gels
    • Mehalebi S., Nicolai T., Durand D. The influence of electrostatic interaction on the structure and the shear modulus of heat-set globular protein gels. Soft Matter 2008, 4:893-900.
    • (2008) Soft Matter , vol.4 , pp. 893-900
    • Mehalebi, S.1    Nicolai, T.2    Durand, D.3
  • 146
    • 0037467401 scopus 로고    scopus 로고
    • Barrier and mechanical properties of milk protein-based edible films containing nutraceuticals
    • Mei Y., Zhao Y. Barrier and mechanical properties of milk protein-based edible films containing nutraceuticals. Journal of Agricultural and Food Chemistry 2003, 51:1914-1918.
    • (2003) Journal of Agricultural and Food Chemistry , vol.51 , pp. 1914-1918
    • Mei, Y.1    Zhao, Y.2
  • 147
    • 34547494548 scopus 로고    scopus 로고
    • Diffusion of the antimicrobial lysozyme from a whey protein coating on smoked salmon
    • Min S., Rumsey T.R., Krochta J.M. Diffusion of the antimicrobial lysozyme from a whey protein coating on smoked salmon. Journal of Food Engineering 2008, 84:39-47.
    • (2008) Journal of Food Engineering , vol.84 , pp. 39-47
    • Min, S.1    Rumsey, T.R.2    Krochta, J.M.3
  • 148
    • 0000805588 scopus 로고    scopus 로고
    • Studies on permeability and rheology of heat and sodium ions-induced whey protein gels
    • Mleko S. Studies on permeability and rheology of heat and sodium ions-induced whey protein gels. Journal of Food Science and Technology 2000, 37:307-310.
    • (2000) Journal of Food Science and Technology , vol.37 , pp. 307-310
    • Mleko, S.1
  • 150
    • 0034774241 scopus 로고    scopus 로고
    • Hydrophobicity of whey protein concentrates measured by fluorescence quenching and its relation with surface functional properties
    • Moro A., Gatti C., Delorenzi N. Hydrophobicity of whey protein concentrates measured by fluorescence quenching and its relation with surface functional properties. Journal of Agricultural and Food Chemistry 2001, 49:4784-4789.
    • (2001) Journal of Agricultural and Food Chemistry , vol.49 , pp. 4784-4789
    • Moro, A.1    Gatti, C.2    Delorenzi, N.3
  • 151
    • 34250001656 scopus 로고    scopus 로고
    • Conditions limiting the influence of thiol-disulphide interchange reactions on the heat-induced aggregation kinetics of beta-lactoglobulin
    • Mounsey J.S., O'Kennedy B.T. Conditions limiting the influence of thiol-disulphide interchange reactions on the heat-induced aggregation kinetics of beta-lactoglobulin. International Dairy Journal 2007, 17:1034-1042.
    • (2007) International Dairy Journal , vol.17 , pp. 1034-1042
    • Mounsey, J.S.1    O'Kennedy, B.T.2
  • 152
    • 67349276424 scopus 로고    scopus 로고
    • Cold-set thickening mechanism of beta-lactoglobulin at low pH: concentration effects
    • Mudgal P., Daubert C.R., Foegeding E.A. Cold-set thickening mechanism of beta-lactoglobulin at low pH: concentration effects. Food Hydrocolloids 2009, 23:1762-1770.
    • (2009) Food Hydrocolloids , vol.23 , pp. 1762-1770
    • Mudgal, P.1    Daubert, C.R.2    Foegeding, E.A.3
  • 153
    • 0002503424 scopus 로고    scopus 로고
    • Scattering properties and modelling of aggregating and gelling systems
    • Clarendon Press, Oxford, W. Brown (Ed.)
    • Nicolai T., Durand D., Gimel J.-C. Scattering properties and modelling of aggregating and gelling systems. Light scattering: Principles and development 1996, 201-231. Clarendon Press, Oxford. W. Brown (Ed.).
    • (1996) Light scattering: Principles and development , pp. 201-231
    • Nicolai, T.1    Durand, D.2    Gimel, J.-C.3
  • 154
    • 55849089956 scopus 로고    scopus 로고
    • Combined effect of dynamic heat treatment and ionic strength on the properties of whey protein foams - part II
    • Nicorescu I., Loisel C., Vial C., Riaublanc A., Djelveh G., Cuvelier G., et al. Combined effect of dynamic heat treatment and ionic strength on the properties of whey protein foams - part II. Food Research International 2008, 41:980-988.
    • (2008) Food Research International , vol.41 , pp. 980-988
    • Nicorescu, I.1    Loisel, C.2    Vial, C.3    Riaublanc, A.4    Djelveh, G.5    Cuvelier, G.6
  • 157
    • 57449085310 scopus 로고    scopus 로고
    • The dominating effect of ionic strength on the heat-induced denaturation and aggregation of beta-lactoglobulin in simulated milk ultrafiltrate
    • O'Kennedy B.T., Mounsey J.S. The dominating effect of ionic strength on the heat-induced denaturation and aggregation of beta-lactoglobulin in simulated milk ultrafiltrate. International Dairy Journal 2009, 19:123-128.
    • (2009) International Dairy Journal , vol.19 , pp. 123-128
    • O'Kennedy, B.T.1    Mounsey, J.S.2
  • 158
    • 77249124284 scopus 로고    scopus 로고
    • Real-time monitoring of heat-induced aggregation of beta-lactoglobulin in aqueous solutions using high-resolution ultrasonic spectroscopy
    • Ochenduszko A., Buckin V. Real-time monitoring of heat-induced aggregation of beta-lactoglobulin in aqueous solutions using high-resolution ultrasonic spectroscopy. International Journal of Thermophysics 2010, 31:113-130.
    • (2010) International Journal of Thermophysics , vol.31 , pp. 113-130
    • Ochenduszko, A.1    Buckin, V.2
  • 159
    • 43249089612 scopus 로고    scopus 로고
    • Use of edible films based on whey protein isolate to protect foods rich in polyunsaturated fatty acids
    • Osés J., Fernández-Pan I., Ziani K., Maté J.I. Use of edible films based on whey protein isolate to protect foods rich in polyunsaturated fatty acids. European Food Research and Technology 2008, 227:623-628.
    • (2008) European Food Research and Technology , vol.227 , pp. 623-628
    • Osés, J.1    Fernández-Pan, I.2    Ziani, K.3    Maté, J.I.4
  • 160
    • 0034089645 scopus 로고    scopus 로고
    • Involvement of disulfide bonds in bovine β-lactoglobulin B gels thermally at various pH
    • Otte J., Zakora M., Qvist K.B. Involvement of disulfide bonds in bovine β-lactoglobulin B gels thermally at various pH. Journal of Food Science 2000, 65:384-389.
    • (2000) Journal of Food Science , vol.65 , pp. 384-389
    • Otte, J.1    Zakora, M.2    Qvist, K.B.3
  • 161
    • 0034877450 scopus 로고    scopus 로고
    • Denaturation time and temperature effects on solubility, tensile properties, and oxygen permeability of whey protein edible films
    • Pérez-Gago M.B., Krochta J.M. Denaturation time and temperature effects on solubility, tensile properties, and oxygen permeability of whey protein edible films. Journal of Food Science 2001, 66:705-710.
    • (2001) Journal of Food Science , vol.66 , pp. 705-710
    • Pérez-Gago, M.B.1    Krochta, J.M.2
  • 162
    • 0035114539 scopus 로고    scopus 로고
    • Lipid particle size effect on water vapor permeability and mechanical properties of whey protein/beeswax emulsion films
    • Pérez-Gago M.B., Krochta J.M. Lipid particle size effect on water vapor permeability and mechanical properties of whey protein/beeswax emulsion films. Journal of Agricultural and Food Chemistry 2001, 49:996-1002.
    • (2001) Journal of Agricultural and Food Chemistry , vol.49 , pp. 996-1002
    • Pérez-Gago, M.B.1    Krochta, J.M.2
  • 163
    • 0033379642 scopus 로고    scopus 로고
    • Water vapor permeability, solubility, and tensile properties of heat-denatured versus native whey protein films
    • Pérez-Gago M.B., Nadaud P., Krochta J.M. Water vapor permeability, solubility, and tensile properties of heat-denatured versus native whey protein films. Journal of Food Science 1999, 64:1034-1037.
    • (1999) Journal of Food Science , vol.64 , pp. 1034-1037
    • Pérez-Gago, M.B.1    Nadaud, P.2    Krochta, J.M.3
  • 164
    • 15244360794 scopus 로고    scopus 로고
    • Effect of whey protein- and hydroxypropyl methylcellulose-based edible composite coatings on color change of fresh-cut apples
    • Pérez-Gago M.B., Serra M., Alonso M., Mateos M., Del Río M.A. Effect of whey protein- and hydroxypropyl methylcellulose-based edible composite coatings on color change of fresh-cut apples. Postharvest Biology and Technology 2005, 36:77-85.
    • (2005) Postharvest Biology and Technology , vol.36 , pp. 77-85
    • Pérez-Gago, M.B.1    Serra, M.2    Alonso, M.3    Mateos, M.4    Del Río, M.A.5
  • 165
    • 0001752728 scopus 로고
    • PH and heat treatment effects on foaming of whey protein isolate
    • Phillips L.G., Schulman W., Kinsella J.E. pH and heat treatment effects on foaming of whey protein isolate. Journal of Food Science 1990, 55:1116-1119.
    • (1990) Journal of Food Science , vol.55 , pp. 1116-1119
    • Phillips, L.G.1    Schulman, W.2    Kinsella, J.E.3
  • 166
    • 1842591242 scopus 로고    scopus 로고
    • Encapsulation of bifidobacteria in whey protein-based microcapsules and survival in simulated gastrointestinal conditions and in yoghurt
    • Picot A., Lacroix C. Encapsulation of bifidobacteria in whey protein-based microcapsules and survival in simulated gastrointestinal conditions and in yoghurt. International Dairy Journal 2004, 14:505-515.
    • (2004) International Dairy Journal , vol.14 , pp. 505-515
    • Picot, A.1    Lacroix, C.2
  • 167
    • 0442326631 scopus 로고    scopus 로고
    • Influence of the ionic strength on the structure of heat set globular protein gels of β-lactoglobulin
    • Pouzot M., Durand D., Nicolai T. Influence of the ionic strength on the structure of heat set globular protein gels of β-lactoglobulin. Macromolecules 2004, 37:614-620.
    • (2004) Macromolecules , vol.37 , pp. 614-620
    • Pouzot, M.1    Durand, D.2    Nicolai, T.3
  • 168
    • 8644266740 scopus 로고    scopus 로고
    • X-ray and light scattering study of the structure of large protein aggregates at neutral pH
    • Pouzot M., Nicolai T., Visschers R.W., Weijers M. X-ray and light scattering study of the structure of large protein aggregates at neutral pH. Food Hydrocolloids 2005, 19:231-238.
    • (2005) Food Hydrocolloids , vol.19 , pp. 231-238
    • Pouzot, M.1    Nicolai, T.2    Visschers, R.W.3    Weijers, M.4
  • 169
    • 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. Biochemical Journal 1997, 324:341-346.
    • (1997) Biochemical Journal , 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
  • 170
    • 0035981078 scopus 로고    scopus 로고
    • Environment-sensitive hydrogels for drug delivery
    • Qiu Y., Park K. Environment-sensitive hydrogels for drug delivery. Advanced Drug Delivery Reviews 2001, 53:321-339.
    • (2001) Advanced Drug Delivery Reviews , vol.53 , pp. 321-339
    • Qiu, Y.1    Park, K.2
  • 171
    • 54049112576 scopus 로고    scopus 로고
    • Effect of protein composition on the rheological properties of acid-induced whey protein gels
    • Rabiey L., Britten M. Effect of protein composition on the rheological properties of acid-induced whey protein gels. Food Hydrocolloids 2009, 23:973-979.
    • (2009) Food Hydrocolloids , vol.23 , pp. 973-979
    • Rabiey, L.1    Britten, M.2
  • 172
    • 70149096181 scopus 로고    scopus 로고
    • Effect of whey protein enzymatic hydrolysis on the rheological properties of acid-induced gels
    • Rabiey L., Britten M. Effect of whey protein enzymatic hydrolysis on the rheological properties of acid-induced gels. Food Hydrocolloids 2009, 23:2302-2308.
    • (2009) Food Hydrocolloids , vol.23 , pp. 2302-2308
    • Rabiey, L.1    Britten, M.2
  • 173
    • 33846988222 scopus 로고    scopus 로고
    • Survival in food systems of Lactobacillus rhamnosus R011 microentrapped in whey protein gel particles
    • Reid A.A., Champagne C.P., Gardner N., Fustier P., Vuillemard J.C. Survival in food systems of Lactobacillus rhamnosus R011 microentrapped in whey protein gel particles. Journal of Food Science 2007, 72:M031-M037.
    • (2007) Journal of Food Science , vol.72
    • Reid, A.A.1    Champagne, C.P.2    Gardner, N.3    Fustier, P.4    Vuillemard, J.C.5
  • 174
    • 30844470928 scopus 로고    scopus 로고
    • Microentrapment of probiotic bacteria in a Ca2+-induced whey protein gel and effects on their viability in a dynamic gastro-intestinal model
    • Reid A.A., Vuillemard J.C., Britten M., Arcand Y., Farnworth E., Champagne C.P. Microentrapment of probiotic bacteria in a Ca2+-induced whey protein gel and effects on their viability in a dynamic gastro-intestinal model. Journal of Microencapsulation 2005, 22:603-619.
    • (2005) Journal of Microencapsulation , vol.22 , pp. 603-619
    • Reid, A.A.1    Vuillemard, J.C.2    Britten, M.3    Arcand, Y.4    Farnworth, E.5    Champagne, C.P.6
  • 178
    • 0043065429 scopus 로고    scopus 로고
    • Molecular mechanisms of Fe2+-induced β-lactoglobulin cold gelation
    • Remondetto G.E., Subirade M. Molecular mechanisms of Fe2+-induced β-lactoglobulin cold gelation. Biopolymers 2003, 69:461-469.
    • (2003) Biopolymers , vol.69 , pp. 461-469
    • Remondetto, G.E.1    Subirade, M.2
  • 179
    • 0026649396 scopus 로고
    • Gelation of globular proteins: effect of pH and ionic strength on the critical concentration for gel formation. A simple model and its application to β-lactoglobulin heat-induced gelation
    • Renard D., Lefebvre J. Gelation of globular proteins: effect of pH and ionic strength on the critical concentration for gel formation. A simple model and its application to β-lactoglobulin heat-induced gelation,. International Journal of Biological Macromolecules 1992, 14:287-291.
    • (1992) International Journal of Biological Macromolecules , vol.14 , pp. 287-291
    • Renard, D.1    Lefebvre, J.2
  • 181
    • 0011043381 scopus 로고    scopus 로고
    • Aggregation and gelation of whey proteins: specific effect of divalent cations?
    • The Royal Society of Chemistry, Cambridge, E. Dickinson, R. Miller (Eds.)
    • Roefs S.P.F.M., Peppelman H.A. Aggregation and gelation of whey proteins: specific effect of divalent cations?. Food colloids, fundamentals of formulation 2001, 358-368. The Royal Society of Chemistry, Cambridge. E. Dickinson, R. Miller (Eds.).
    • (2001) Food colloids, fundamentals of formulation , pp. 358-368
    • Roefs, S.P.F.M.1    Peppelman, H.A.2
  • 182
    • 21344458129 scopus 로고    scopus 로고
    • Dicationic-induced gelation of pre-denatured whey protein isolate
    • Roff C.F., Foegeding A.E. Dicationic-induced gelation of pre-denatured whey protein isolate. Food Hydrocolloids 1996, 10:193-198.
    • (1996) Food Hydrocolloids , vol.10 , pp. 193-198
    • Roff, C.F.1    Foegeding, A.E.2
  • 183
    • 17044440175 scopus 로고    scopus 로고
    • Measuring the length distribution of a fibril system: a flow birefringence technique applied to amyloid fibrils
    • Rogers S.S., Venema P., Sagis L.M.C., van der Linden E., Donald A.M. Measuring the length distribution of a fibril system: a flow birefringence technique applied to amyloid fibrils,. Macromolecules 2005, 38:2948-2958.
    • (2005) Macromolecules , vol.38 , pp. 2948-2958
    • Rogers, S.S.1    Venema, P.2    Sagis, L.M.C.3    van der Linden, E.4    Donald, A.M.5
  • 186
    • 1242277394 scopus 로고    scopus 로고
    • Water-insoluble, whey protein-based microspheres prepared by an all-aqueous process
    • Rosenberg M., Lee S.J. Water-insoluble, whey protein-based microspheres prepared by an all-aqueous process. Journal of Food Science 2004, 69:FEP50-FEP58.
    • (2004) Journal of Food Science , vol.69
    • Rosenberg, M.1    Lee, S.J.2
  • 187
  • 188
    • 74449092339 scopus 로고    scopus 로고
    • β-Lactoglobulin aggregates in foam films: effect of the concentration and size of the protein aggregates
    • Rullier B., Axelos M.A.V., Langevin D., Novales B. β-Lactoglobulin aggregates in foam films: effect of the concentration and size of the protein aggregates. Journal of Colloid and Interface Science 2010, 343:330-337.
    • (2010) Journal of Colloid and Interface Science , vol.343 , pp. 330-337
    • Rullier, B.1    Axelos, M.A.V.2    Langevin, D.3    Novales, B.4
  • 190
    • 34247360046 scopus 로고    scopus 로고
    • Whey protein soluble aggregates from heating with NaCl: physicochemical, interfacial, and foaming properties
    • Schmitt C., Bovay C., Rouvet M., Shojaei-Rami S., Kolodziejczyk E. Whey protein soluble aggregates from heating with NaCl: physicochemical, interfacial, and foaming properties. Langmuir 2007, 23:4155-4166.
    • (2007) Langmuir , vol.23 , pp. 4155-4166
    • Schmitt, C.1    Bovay, C.2    Rouvet, M.3    Shojaei-Rami, S.4    Kolodziejczyk, E.5
  • 191
    • 79851511849 scopus 로고    scopus 로고
    • Influence of protein and mineral composition on the formation of whey protein heat-induced microgels
    • Schmitt C., Bovay C., Vuilliomenet A.M., Rouvet M., Bovetto L. Influence of protein and mineral composition on the formation of whey protein heat-induced microgels. Food Hydrocolloids 2011, 25:558-567.
    • (2011) Food Hydrocolloids , vol.25 , pp. 558-567
    • Schmitt, C.1    Bovay, C.2    Vuilliomenet, A.M.3    Rouvet, M.4    Bovetto, L.5
  • 192
    • 67651115509 scopus 로고    scopus 로고
    • Multiscale characterization of individualized β-lactoglobulin microgels formed upon heat treatment under narrow pH range conditions
    • Schmitt C., Bovay C., Vuilliomenet A.M., Rouvet M., Bovetto L., Barbar R., et al. Multiscale characterization of individualized β-lactoglobulin microgels formed upon heat treatment under narrow pH range conditions. Langmuir 2009, 25:7899-7909.
    • (2009) Langmuir , vol.25 , pp. 7899-7909
    • Schmitt, C.1    Bovay, C.2    Vuilliomenet, A.M.3    Rouvet, M.4    Bovetto, L.5    Barbar, R.6
  • 193
    • 77956928324 scopus 로고    scopus 로고
    • Internal structure and colloidal behaviour of covalent whey protein microgels obtained by heat treatment
    • Schmitt C., Moitzi C., Bovay C., Rouvet M., Bovetto L., Donato L., et al. Internal structure and colloidal behaviour of covalent whey protein microgels obtained by heat treatment. Soft Matter 2010, 6:4876-4884.
    • (2010) Soft Matter , vol.6 , pp. 4876-4884
    • Schmitt, C.1    Moitzi, C.2    Bovay, C.3    Rouvet, M.4    Bovetto, L.5    Donato, L.6
  • 194
    • 0034462997 scopus 로고    scopus 로고
    • Heat-induced aggregation of β-lactoglobulin A and B with α-lactalbumin
    • Schokker E.P., Singh H., Creamer L.K. Heat-induced aggregation of β-lactoglobulin A and B with α-lactalbumin. International Dairy Journal 2000, 10:843-853.
    • (2000) International Dairy Journal , vol.10 , pp. 843-853
    • Schokker, E.P.1    Singh, H.2    Creamer, L.K.3
  • 195
    • 0033846408 scopus 로고    scopus 로고
    • Heat-induced aggregation of β-lactoglobulin AB at pH 2.5 as influenced by ionic strength and protein concentration
    • Schokker E.P., Singh H., Pinder D.N., Creamer L.K. Heat-induced aggregation of β-lactoglobulin AB at pH 2.5 as influenced by ionic strength and protein concentration. International Dairy Journal 2000, 10:233-240.
    • (2000) International Dairy Journal , vol.10 , pp. 233-240
    • Schokker, E.P.1    Singh, H.2    Pinder, D.N.3    Creamer, L.K.4
  • 196
    • 0033501546 scopus 로고    scopus 로고
    • Characterization of intermediates formed during heat-induced aggregation of [beta]-lactoglobulin AB at neutral pH
    • Schokker E.P., Singh H., Pinder D.N., Norris G.E., Creamer L.K. Characterization of intermediates formed during heat-induced aggregation of [beta]-lactoglobulin AB at neutral pH. International Dairy Journal 1999, 9:791-800.
    • (1999) International Dairy Journal , vol.9 , pp. 791-800
    • Schokker, E.P.1    Singh, H.2    Pinder, D.N.3    Norris, G.E.4    Creamer, L.K.5
  • 197
    • 33644853479 scopus 로고    scopus 로고
    • Antimicrobial activity of whey protein based edible films incorporated with oregano, rosemary and garlic essential oils
    • Seydim A.C., Sarikus G. Antimicrobial activity of whey protein based edible films incorporated with oregano, rosemary and garlic essential oils. Food Research International 2006, 39:639-644.
    • (2006) Food Research International , vol.39 , pp. 639-644
    • Seydim, A.C.1    Sarikus, G.2
  • 199
    • 0036189113 scopus 로고    scopus 로고
    • Physical properties of WPI films plasticized with glycerol, xylitol, or sorbitol
    • Shaw N.B., Monahan F.J., O'Riordan E.D., O'Sullivan M. Physical properties of WPI films plasticized with glycerol, xylitol, or sorbitol. Journal of Food Science 2002, 67:164-167.
    • (2002) Journal of Food Science , vol.67 , pp. 164-167
    • Shaw, N.B.1    Monahan, F.J.2    O'Riordan, E.D.3    O'Sullivan, M.4
  • 200
    • 0033799942 scopus 로고    scopus 로고
    • Oxygen permeability and mechanical properties of films from hydrolyzed whey protein
    • Sothornvit R., Krochta J.M. Oxygen permeability and mechanical properties of films from hydrolyzed whey protein. Journal of Agricultural and Food Chemistry 2000, 48:3913-3916.
    • (2000) Journal of Agricultural and Food Chemistry , vol.48 , pp. 3913-3916
    • Sothornvit, R.1    Krochta, J.M.2
  • 201
    • 0033410063 scopus 로고    scopus 로고
    • Whey protein aggregation under shear conditions -effects of lactose and heating temperature on aggregate size and structure
    • Spiegel T. Whey protein aggregation under shear conditions -effects of lactose and heating temperature on aggregate size and structure. International Journal of Food Science and Technology 1999, 34:523-531.
    • (1999) International Journal of Food Science and Technology , vol.34 , pp. 523-531
    • Spiegel, T.1
  • 202
    • 0036077429 scopus 로고    scopus 로고
    • Whey protein aggregation under shear conditions - effects of pH-value and removal of calcium
    • Spiegel T., Huss M. Whey protein aggregation under shear conditions - effects of pH-value and removal of calcium. International Journal of Food Science and Technology 2002, 37:559-568.
    • (2002) International Journal of Food Science and Technology , vol.37 , pp. 559-568
    • Spiegel, T.1    Huss, M.2
  • 203
    • 85025575777 scopus 로고
    • Viscoelastic behaviour of β-lactoglobulin gel structures
    • Stading M., Hermannsson A. Viscoelastic behaviour of β-lactoglobulin gel structures. Food Hydrocolloids 1990, 4:121-135.
    • (1990) Food Hydrocolloids , vol.4 , pp. 121-135
    • Stading, M.1    Hermannsson, A.2
  • 205
    • 0037073089 scopus 로고    scopus 로고
    • Towards the understanding of molecular mechanisms in the early stages of heat-induced aggregation of β-lactoglobulin AB
    • Surroca Y., Haverkamp J., Heck A.J.R. Towards the understanding of molecular mechanisms in the early stages of heat-induced aggregation of β-lactoglobulin AB. Journal of Chromatography A 2002, 970:275-285.
    • (2002) Journal of Chromatography A , vol.970 , pp. 275-285
    • Surroca, Y.1    Haverkamp, J.2    Heck, A.J.R.3
  • 206
    • 17644417143 scopus 로고    scopus 로고
    • Plasticizing effects of beeswax and carnauba wax on tensile and water vapor permeability properties of whey protein films
    • Talens P., Krochta J.M. Plasticizing effects of beeswax and carnauba wax on tensile and water vapor permeability properties of whey protein films. Journal of Food Science 2005, 70:E239-E243.
    • (2005) Journal of Food Science , vol.70
    • Talens, P.1    Krochta, J.M.2
  • 208
    • 22244485011 scopus 로고    scopus 로고
    • Effect of pH and temperature on the reaction kinetic parameters of the thermal denaturation of β-lactoglobulin
    • Tolkach A., Kulozik U. Effect of pH and temperature on the reaction kinetic parameters of the thermal denaturation of β-lactoglobulin. Milchwissenschaft-Milk Science International 2005, 60:249-252.
    • (2005) Milchwissenschaft-Milk Science International , vol.60 , pp. 249-252
    • Tolkach, A.1    Kulozik, U.2
  • 209
    • 41949117726 scopus 로고    scopus 로고
    • Reaction kinetic pathway of reversible and irreversible thermal denaturation of β-lactoglobulin
    • Tolkach A., Kulozik U. Reaction kinetic pathway of reversible and irreversible thermal denaturation of β-lactoglobulin. Lait 2007, 87:301-315.
    • (2007) Lait , vol.87 , pp. 301-315
    • Tolkach, A.1    Kulozik, U.2
  • 210
    • 29544447014 scopus 로고    scopus 로고
    • Optimization of thermal pretreatment conditions for the separation of native α-lactalbumin from whey protein concentrates by means of selective denaturation of beta-lactoglobulin
    • Tolkach A., Steinle S., Kulozik U. Optimization of thermal pretreatment conditions for the separation of native α-lactalbumin from whey protein concentrates by means of selective denaturation of beta-lactoglobulin. Journal of Food Science 2005, 70:E557-E566.
    • (2005) Journal of Food Science , vol.70
    • Tolkach, A.1    Steinle, S.2    Kulozik, U.3
  • 211
    • 85168542525 scopus 로고    scopus 로고
    • Controlled heat-denaturation and aggregation of β-lactoglobulin in presence of cosolutes. Consequences on foaming properties. PhD dissertation. INPL, Nancy, France
    • Unterhaslberger, G. (2004). Controlled heat-denaturation and aggregation of β-lactoglobulin in presence of cosolutes. Consequences on foaming properties. PhD dissertation. INPL, Nancy, France, 191p.
    • (2004) , pp. 191
    • Unterhaslberger, G.1
  • 212
    • 33746219698 scopus 로고    scopus 로고
    • Heat denaturation and aggregation of β-lactoglobulin enriched WPI in the presence of arginine HCl, NaCl and guanidinium HCl at pH 4.0 and 7.0
    • Unterhaslberger G., Schmitt C., Sanchez C., Appolonia-Nouzille C., Raemy A. Heat denaturation and aggregation of β-lactoglobulin enriched WPI in the presence of arginine HCl, NaCl and guanidinium HCl at pH 4.0 and 7.0. Food Hydrocolloids 2006, 20:1006-1019.
    • (2006) Food Hydrocolloids , vol.20 , pp. 1006-1019
    • Unterhaslberger, G.1    Schmitt, C.2    Sanchez, C.3    Appolonia-Nouzille, C.4    Raemy, A.5
  • 213
    • 34247323371 scopus 로고    scopus 로고
    • β-lactoglobulin aggregates from heating with charged cosolutes: formation, characterization and foaming
    • E. Dickinson, M.E. Leser (Eds.)
    • Unterhaslberger G., Schmitt C., Shojaei-Rami S., Sanchez C. β-lactoglobulin aggregates from heating with charged cosolutes: formation, characterization and foaming. Food colloids: Self-assembly and material science 2007, 175-192. E. Dickinson, M.E. Leser (Eds.).
    • (2007) Food colloids: Self-assembly and material science , pp. 175-192
    • Unterhaslberger, G.1    Schmitt, C.2    Shojaei-Rami, S.3    Sanchez, C.4
  • 215
    • 77955584694 scopus 로고    scopus 로고
    • Impact of Mg2+ and tara gum concentrations on flow and textural properties of WPI solutions and cold-set gels
    • Vazquez da Silva M., Delgado J.M.P.Q., Goncalves M.P. Impact of Mg2+ and tara gum concentrations on flow and textural properties of WPI solutions and cold-set gels. International Journal of Food Properties 2010, 13:972-982.
    • (2010) International Journal of Food Properties , vol.13 , pp. 972-982
    • Vazquez da Silva, M.1    Delgado, J.M.P.Q.2    Goncalves, M.P.3
  • 217
    • 0036054901 scopus 로고    scopus 로고
    • Effect of electrostatic interactions on the percolation concentration of fibrillar β-lactoglobulin gels
    • Veerman C., Ruis H., Sagis L.M.C., van der Linden E. Effect of electrostatic interactions on the percolation concentration of fibrillar β-lactoglobulin gels. Biomacromolecules 2002, 3:869-873.
    • (2002) Biomacromolecules , vol.3 , pp. 869-873
    • Veerman, C.1    Ruis, H.2    Sagis, L.M.C.3    van der Linden, E.4
  • 219
    • 0000289106 scopus 로고    scopus 로고
    • Structure of particulate whey protein gels: effect of NaCl concentration, pH, heating temperature, and protein composition
    • Verheul M., Roefs S.P.F.M. Structure of particulate whey protein gels: effect of NaCl concentration, pH, heating temperature, and protein composition. Journal of Agricultural and Food Chemistry 1998, 46:4909-4916.
    • (1998) Journal of Agricultural and Food Chemistry , vol.46 , pp. 4909-4916
    • Verheul, M.1    Roefs, S.P.F.M.2
  • 222
    • 42149100530 scopus 로고    scopus 로고
    • Effect of pH and addition of corn oil on the properties of whey protein isolate-based films using response surface methodology
    • Wang L., Liu L., Holmes J., Huang J., Kerry J.F., Kerry J.P. Effect of pH and addition of corn oil on the properties of whey protein isolate-based films using response surface methodology. International Journal of Food Science and Technology 2008, 43:787-796.
    • (2008) International Journal of Food Science and Technology , vol.43 , pp. 787-796
    • Wang, L.1    Liu, L.2    Holmes, J.3    Huang, J.4    Kerry, J.F.5    Kerry, J.P.6
  • 223
    • 58149196312 scopus 로고    scopus 로고
    • Thermal behaviour of bovine β-lactoglobulin at temperatures up to 150 degrees C. a review
    • de Wit J.N. Thermal behaviour of bovine β-lactoglobulin at temperatures up to 150 degrees C. a review. Trends in Food Science & Technology 2009, 20:27-34.
    • (2009) Trends in Food Science & Technology , vol.20 , pp. 27-34
    • de Wit, J.N.1
  • 225
    • 28844495394 scopus 로고    scopus 로고
    • Kinetics of cold-set diffusion-limited aggregations of denatured whey protein isolate colloids
    • Wu H., Xie J., Morbidelli M. Kinetics of cold-set diffusion-limited aggregations of denatured whey protein isolate colloids. Biomacromolecules 2005, 6:3189.
    • (2005) Biomacromolecules , vol.6 , pp. 3189
    • Wu, H.1    Xie, J.2    Morbidelli, M.3
  • 226
    • 69749124541 scopus 로고    scopus 로고
    • Characterization of cold-set gels produced from heated emulsions stabilized by whey protein
    • Ye A., Taylor S. Characterization of cold-set gels produced from heated emulsions stabilized by whey protein. International Dairy Journal 2009, 19:721-727.
    • (2009) International Dairy Journal , vol.19 , pp. 721-727
    • Ye, A.1    Taylor, S.2
  • 227
    • 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. Journal of Agricultural and Food Chemistry 1994, 42:846-855.
    • (1994) Journal of Agricultural and Food Chemistry , vol.42 , pp. 846-855
    • Zhu, H.1    Damodaran, S.2
  • 228
    • 70349968257 scopus 로고    scopus 로고
    • Physical and thermo-mechanical properties of whey protein isolate films containing antimicrobials, and their effect against spoilage flora of fresh beef
    • Zinoviadou K.G., Koutsoumanis K.P., Biliaderis C.G. Physical and thermo-mechanical properties of whey protein isolate films containing antimicrobials, and their effect against spoilage flora of fresh beef. Food Hydrocolloids 2010, 24:49-59.
    • (2010) Food Hydrocolloids , vol.24 , pp. 49-59
    • Zinoviadou, K.G.1    Koutsoumanis, K.P.2    Biliaderis, C.G.3
  • 229
    • 79952532956 scopus 로고    scopus 로고
    • Ultrasonic generation of aerated gelatin gels stabilized by whey protein β-lactoglobulin
    • Zuniga R.N., Kulozik U., Aguilera J.M. Ultrasonic generation of aerated gelatin gels stabilized by whey protein β-lactoglobulin. Food Hydrocolloids 2010, 10.1016/j.foodhyd.2010.09.010.
    • (2010) Food Hydrocolloids
    • Zuniga, R.N.1    Kulozik, U.2    Aguilera, J.M.3
  • 230
    • 77956131588 scopus 로고    scopus 로고
    • Kinetics of formation and physicochemical characterization of thermally-induced beta-lactoglobulin aggregates
    • Zuniga R.N., Tolkach A., Kulozik U., Aguilera J.M. Kinetics of formation and physicochemical characterization of thermally-induced beta-lactoglobulin aggregates. Journal of Food Science 2010, 75:E261-E268.
    • (2010) Journal of Food Science , vol.75
    • Zuniga, R.N.1    Tolkach, A.2    Kulozik, U.3    Aguilera, J.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.