메뉴 건너뛰기




Volumn 79, Issue , 2018, Pages 145-157

Calcium-induced gelation of whey protein aggregates: Kinetics, structure and rheological properties

Author keywords

Calcium; Cold gelation; Fractal aggregates; Microgels; Texture; Whey protein

Indexed keywords

ACTIVATION ENERGY; AGGREGATES; BINDING ENERGY; CHLORINE COMPOUNDS; FRACTALS; GELATION; GELS; PROTEINS; STIFFNESS; TEMPERATURE DISTRIBUTION;

EID: 85042144768     PISSN: 0268005X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.foodhyd.2017.11.049     Document Type: Article
Times cited : (63)

References (69)
  • 1
    • 84856873460 scopus 로고    scopus 로고
    • Proteins fibrils from a polymer physics perspective
    • Adamcik, J., Mezzenga, R., Proteins fibrils from a polymer physics perspective. Macromolecules 45:3 (2011), 1137–1150.
    • (2011) Macromolecules , vol.45 , Issue.3 , pp. 1137-1150
    • Adamcik, J.1    Mezzenga, R.2
  • 2
    • 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 23:4 (2009), 1111–1119.
    • (2009) Food Hydrocolloids , vol.23 , Issue.4 , pp. 1111-1119
    • Ako, K.1    Durand, D.2    Nicolai, T.3    Becu, L.4
  • 3
    • 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 11:4 (2010), 864–871.
    • (2010) Biomacromolecules , vol.11 , Issue.4 , pp. 864-871
    • Ako, K.1    Nicolai, T.2    Durand, D.3
  • 4
    • 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 5:20 (2009), 4033–4041.
    • (2009) Soft Matter , vol.5 , Issue.20 , pp. 4033-4041
    • Ako, K.1    Nicolai, T.2    Durand, D.3    Brotons, G.4
  • 6
    • 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 17:4 (2003), 469–479.
    • (2003) Food Hydrocolloids , vol.17 , Issue.4 , pp. 469-479
    • Alting, A.C.1    Hamer, R.J.2    de Kruif, C.G.3    Paques, M.4    Visschers, R.W.5
  • 8
  • 10
    • 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 28:6 (1995), 598–603.
    • (1995) LWT-Food Science and Technology , vol.28 , Issue.6 , pp. 598-603
    • Barbut, S.1
  • 11
    • 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 30:6 (1997), 590–593.
    • (1997) LWT-Food Science and Technology , vol.30 , Issue.6 , pp. 590-593
    • Barbut, S.1
  • 12
    • 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 30:2 (1997), 153–157.
    • (1997) Food Research International , vol.30 , Issue.2 , pp. 153-157
    • Barbut, S.1    Drake, D.2
  • 13
    • 84893617475 scopus 로고
    • Ca2+-induced gelation of pre-heated whey protein isolate
    • Barbut, S., Foegeding, E.A., Ca2+-induced gelation of pre-heated whey protein isolate. Journal of Food Science 58:4 (1993), 867–871.
    • (1993) Journal of Food Science , vol.58 , Issue.4 , pp. 867-871
    • Barbut, S.1    Foegeding, E.A.2
  • 14
    • 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 15:4 (2001), 609–617.
    • (2001) Food Hydrocolloids , vol.15 , Issue.4 , pp. 609-617
    • Britten, M.1    Giroux, H.J.2
  • 15
    • 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 & Technology 9:4 (1998), 143–151.
    • (1998) Trends in Food Science & Technology , vol.9 , Issue.4 , pp. 143-151
    • Bryant, C.M.1    McClements, D.J.2
  • 16
    • 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 65:5 (2000), 801–804.
    • (2000) Journal of Food Science , vol.65 , Issue.5 , pp. 801-804
    • Bryant, C.M.1    McClements, D.J.2
  • 17
    • 41849095663 scopus 로고    scopus 로고
    • Whey protein interactions in acidic cold-set gels at different pH values
    • Cavallieri, A.L.F., Costa-Netto, A.P., Menossi, M., Da Cunha, R.L., Whey protein interactions in acidic cold-set gels at different pH values. Le Lait 87:6 (2007), 535–554.
    • (2007) Le Lait , vol.87 , Issue.6 , pp. 535-554
    • Cavallieri, A.L.F.1    Costa-Netto, A.P.2    Menossi, M.3    Da Cunha, R.L.4
  • 18
    • 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 22:3 (2008), 439–448.
    • (2008) Food Hydrocolloids , vol.22 , Issue.3 , pp. 439-448
    • Cavallieri, A.L.F.1    Da Cunha, R.L.2
  • 19
    • 85168719765 scopus 로고    scopus 로고
    • Kinetics of NaCl induced gelation of soy protein aggregates: Effects of temperature, aggregate size, and protein concentration
    • in Press
    • Chen, N., Chassenieux, C., Nicolai, T., Kinetics of NaCl induced gelation of soy protein aggregates: Effects of temperature, aggregate size, and protein concentration. Food Hydrocolloids, 2017 in Press.
    • (2017) Food Hydrocolloids
    • Chen, N.1    Chassenieux, C.2    Nicolai, T.3
  • 20
    • 0141567459 scopus 로고    scopus 로고
    • Physical stability of proteins in aqueous solution: Mechanism and driving forces in nonnative protein aggregation
    • Chi, E.Y., Krishnan, S., Randolph, T.W., Carpenter, J.F., Physical stability of proteins in aqueous solution: Mechanism and driving forces in nonnative protein aggregation. Pharmaceutical Research 20:9 (2003), 1325–1336.
    • (2003) Pharmaceutical Research , vol.20 , Issue.9 , pp. 1325-1336
    • Chi, E.Y.1    Krishnan, S.2    Randolph, T.W.3    Carpenter, J.F.4
  • 24
    • 84987367516 scopus 로고
    • Reaction kinetics of the denaturation of whey proteins in milk
    • Dannenberg, F., Kessler, H.-G., Reaction kinetics of the denaturation of whey proteins in milk. Journal of Food Science 53:1 (1988), 258–263.
    • (1988) Journal of Food Science , vol.53 , Issue.1 , pp. 258-263
    • Dannenberg, F.1    Kessler, H.-G.2
  • 25
    • 38749112076 scopus 로고
    • Gels and gelling of globular proteins
    • Doi, E., Gels and gelling of globular proteins. Trends in Food Science & Technology 4:1 (1993), 1–5.
    • (1993) Trends in Food Science & Technology , vol.4 , Issue.1 , pp. 1-5
    • Doi, E.1
  • 26
    • 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., Kolodziejcyk, 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 25:4 (2011), 734–742.
    • (2011) Food Hydrocolloids , vol.25 , Issue.4 , pp. 734-742
    • Donato, L.1    Kolodziejcyk, E.2    Rouvet, M.3
  • 27
    • 79961031305 scopus 로고    scopus 로고
    • Food protein functionality: A comprehensive approach
    • Foegeding, E.A., Davis, J.P., Food protein functionality: A comprehensive approach. Food Hydrocolloids 25:8 (2011), 1853–1864.
    • (2011) Food Hydrocolloids , vol.25 , Issue.8 , pp. 1853-1864
    • Foegeding, E.A.1    Davis, J.P.2
  • 29
    • 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 29:2 (1996), 135–139.
    • (1996) Food Research International , vol.29 , Issue.2 , pp. 135-139
    • Hongsprabhas, P.1    Barbut, S.2
  • 30
    • 0031070982 scopus 로고    scopus 로고
    • Effect of gelation temperature on Ca2+-induced gelation of whey protein isolate
    • Hongsprabhas, P., Barbut, S., Effect of gelation temperature on Ca2+-induced gelation of whey protein isolate. LWT-Food Science and Technology 30:1 (1997), 45–49.
    • (1997) LWT-Food Science and Technology , vol.30 , Issue.1 , pp. 45-49
    • Hongsprabhas, P.1    Barbut, S.2
  • 31
    • 0031582836 scopus 로고    scopus 로고
    • Structure-forming processes in Ca 2+-induced whey protein isolate cold gelation
    • Hongsprabhas, P., Barbut, S., Structure-forming processes in Ca 2+-induced whey protein isolate cold gelation. International Dairy Journal 7:12 (1997), 827–834.
    • (1997) International Dairy Journal , vol.7 , Issue.12 , pp. 827-834
    • Hongsprabhas, P.1    Barbut, S.2
  • 32
    • 0031200774 scopus 로고    scopus 로고
    • Ca 2+-induced cold gelation of whey protein isolate: Effect of two-stage gelation
    • Hongsprabhas, B., Barbut, S., Ca 2+-induced cold gelation of whey protein isolate: Effect of two-stage gelation. Food Research International 30:7 (1997), 523–527.
    • (1997) Food Research International , vol.30 , Issue.7 , pp. 523-527
    • Hongsprabhas, B.1    Barbut, S.2
  • 33
    • 0030919028 scopus 로고    scopus 로고
    • Protein and salt effects on Ca2+-Induced cold gelation of whey protein isolate
    • Hongsprabhas, B., Barbut, S., Protein and salt effects on Ca2+-Induced cold gelation of whey protein isolate. Journal of Food Science 62:2 (1997), 382–385.
    • (1997) Journal of Food Science , vol.62 , Issue.2 , pp. 382-385
    • Hongsprabhas, B.1    Barbut, S.2
  • 34
    • 0033147465 scopus 로고    scopus 로고
    • The structure of cold-set whey protein isolate gels prepared with Ca++
    • Hongsprabhas, P., Barbut, S., Marangoni, A.G., The structure of cold-set whey protein isolate gels prepared with Ca++. LWT-Food Science and Technology 32:4 (1999), 196–202.
    • (1999) LWT-Food Science and Technology , vol.32 , Issue.4 , pp. 196-202
    • Hongsprabhas, P.1    Barbut, S.2    Marangoni, A.G.3
  • 35
    • 84960194485 scopus 로고    scopus 로고
    • Structure and flow of dense suspensions of protein fractal aggregates in comparison with microgels
    • Inthavong, W., Kharlamova, A., Chassenieux, C., Nicolai, T., Structure and flow of dense suspensions of protein fractal aggregates in comparison with microgels. Soft Matter 12:10 (2016), 2785–2793.
    • (2016) Soft Matter , vol.12 , Issue.10 , pp. 2785-2793
    • Inthavong, W.1    Kharlamova, A.2    Chassenieux, C.3    Nicolai, T.4
  • 36
    • 0000362470 scopus 로고    scopus 로고
    • Effects of preheating on properties of aggregates and of cold-set gels of whey protein isolate
    • Ju, Z.Y., Kilara, A., Effects of preheating on properties of aggregates and of cold-set gels of whey protein isolate. Journal of Agricultural and Food Chemistry 46:9 (1998), 3604–3608.
    • (1998) Journal of Agricultural and Food Chemistry , vol.46 , Issue.9 , pp. 3604-3608
    • Ju, Z.Y.1    Kilara, A.2
  • 37
    • 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 63:2 (1998), 288–292.
    • (1998) Journal of Food Science , vol.63 , Issue.2 , pp. 288-292
    • Ju, Z.Y.1    Kilara, A.2
  • 38
    • 52649129277 scopus 로고    scopus 로고
    • Structure of heat-induced β-lactoglobulin aggregates and their complexes with sodium-dodecyl sulfate
    • Jung, J.-M., Savin, G., Pouzot, M., Schmitt, C., Mezzenga, R., Structure of heat-induced β-lactoglobulin aggregates and their complexes with sodium-dodecyl sulfate. Biomacromolecules 9:9 (2008), 2477–2486.
    • (2008) Biomacromolecules , vol.9 , Issue.9 , pp. 2477-2486
    • Jung, J.-M.1    Savin, G.2    Pouzot, M.3    Schmitt, C.4    Mezzenga, R.5
  • 39
    • 84963812434 scopus 로고    scopus 로고
    • The effect of aggregation into fractals or microgels on the charge density and the isoionic point of globular proteins
    • Kharlamova, A., Inthavong, W., Nicolai, T., Chassenieux, C., The effect of aggregation into fractals or microgels on the charge density and the isoionic point of globular proteins. Food Hydrocolloids 60 (2016), 470–475.
    • (2016) Food Hydrocolloids , vol.60 , pp. 470-475
    • Kharlamova, A.1    Inthavong, W.2    Nicolai, T.3    Chassenieux, C.4
  • 41
    • 84893063028 scopus 로고    scopus 로고
    • Mono-, di-and tri-valent ion induced protein gelation: Small-angle neutron scattering study
    • Kundu, S., Chinchalikar, A.J., Das, K., Aswal, V.K., Kohlbrecher, J., Mono-, di-and tri-valent ion induced protein gelation: Small-angle neutron scattering study. Chemical Physics Letters 593 (2014), 140–144.
    • (2014) Chemical Physics Letters , vol.593 , pp. 140-144
    • Kundu, S.1    Chinchalikar, A.J.2    Das, K.3    Aswal, V.K.4    Kohlbrecher, J.5
  • 43
    • 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 32:19 (1999), 6120–6127.
    • (1999) Macromolecules , vol.32 , Issue.19 , pp. 6120-6127
    • Le Bon, C.1    Nicolai, T.2    Durand, D.3
  • 45
    • 77956057232 scopus 로고    scopus 로고
    • Effect of preheating temperature and calcium ions on the properties of cold-set soybean protein gel
    • Lu, X., Lu, Z., Yin, L., Cheng, Y., Li, L., Effect of preheating temperature and calcium ions on the properties of cold-set soybean protein gel. Food Research International 43:6 (2010), 1673–1683.
    • (2010) Food Research International , vol.43 , Issue.6 , pp. 1673-1683
    • Lu, X.1    Lu, Z.2    Yin, L.3    Cheng, Y.4    Li, L.5
  • 46
    • 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 55:8 (2007), 3104–3111.
    • (2007) Journal of Agricultural and Food Chemistry , vol.55 , Issue.8 , pp. 3104-3111
    • Mahmoudi, N.1    Mehalebi, S.2    Nicolai, T.3    Durand, D.4    Riaublanc, A.5
  • 48
    • 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 14:1 (2000), 61–74.
    • (2000) Food Hydrocolloids , vol.14 , Issue.1 , pp. 61-74
    • Marangoni, A.G.1    Barbut, S.2    McGauley, S.E.3    Marcone, M.4    Narine, S.S.5
  • 49
    • 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 69:1 (1995), 7–14.
    • (1995) Journal of the Science of Food and Agriculture , vol.69 , Issue.1 , pp. 7-14
    • McClements, D.J.1    Keogh, M.K.2
  • 50
    • 84875939276 scopus 로고    scopus 로고
    • The self-assembly, aggregation and phase transitions of food protein systems in one, two and three dimensions
    • Mezzenga, R., Fischer, P., The self-assembly, aggregation and phase transitions of food protein systems in one, two and three dimensions. Reports on Progress in Physics, 76(4), 2013, 046601.
    • (2013) Reports on Progress in Physics , vol.76 , Issue.4
    • Mezzenga, R.1    Fischer, P.2
  • 51
    • 0034124057 scopus 로고    scopus 로고
    • pH induced aggregation and weak gel formation of whey protein polymers
    • Mleko, S., Foegeding, E.A., pH induced aggregation and weak gel formation of whey protein polymers. Journal of Food Science 65:1 (2000), 139–143.
    • (2000) Journal of Food Science , vol.65 , Issue.1 , pp. 139-143
    • Mleko, S.1    Foegeding, E.A.2
  • 52
    • 84895064849 scopus 로고    scopus 로고
    • Gelation behavior and rheological properties of salt-or acid-induced soy proteins soft tofu-type gels
    • Murekatete, N., Hua, Y., Chamba, M.V.M., Djakpo, O., Zhang, C., Gelation behavior and rheological properties of salt-or acid-induced soy proteins soft tofu-type gels. Journal of Texture Studies 45:1 (2014), 62–73.
    • (2014) Journal of Texture Studies , vol.45 , Issue.1 , pp. 62-73
    • Murekatete, N.1    Hua, Y.2    Chamba, M.V.M.3    Djakpo, O.4    Zhang, C.5
  • 54
    • 79961023076 scopus 로고    scopus 로고
    • β-Lactoglobulin and WPI aggregates: Formation, structure and applications
    • Nicolai, T., Britten, M., Schmitt, C., β-Lactoglobulin and WPI aggregates: Formation, structure and applications. Food Hydrocolloids 25:8 (2011), 1945–1962.
    • (2011) Food Hydrocolloids , vol.25 , Issue.8 , pp. 1945-1962
    • Nicolai, T.1    Britten, M.2    Schmitt, C.3
  • 56
    • 83455245412 scopus 로고    scopus 로고
    • On the crucial importance of the pH for the formation and self-stabilization of protein microgels and strands
    • Phan-Xuan, T., Durand, D., Nicolai, T., Donato, L., Schmitt, C., Bovetto, L., On the crucial importance of the pH for the formation and self-stabilization of protein microgels and strands. Langmuir 27:24 (2011), 15092–15101.
    • (2011) Langmuir , vol.27 , Issue.24 , pp. 15092-15101
    • Phan-Xuan, T.1    Durand, D.2    Nicolai, T.3    Donato, L.4    Schmitt, C.5    Bovetto, L.6
  • 57
    • 84884519184 scopus 로고    scopus 로고
    • Heat induced formation of beta-lactoglobulin microgels driven by addition of calcium ions
    • Phan-Xuan, T., Durand, D., Nicolai, T., Donato, L., Schmitt, C., Bovetto, L., Heat induced formation of beta-lactoglobulin microgels driven by addition of calcium ions. Food Hydrocolloids 34 (2014), 227–235.
    • (2014) Food Hydrocolloids , vol.34 , pp. 227-235
    • Phan-Xuan, T.1    Durand, D.2    Nicolai, T.3    Donato, L.4    Schmitt, C.5    Bovetto, L.6
  • 59
    • 75349105461 scopus 로고    scopus 로고
    • New directions towards structure formation and stability of protein-rich foods from globular proteins
    • Purwanti, N., van der Goot, A.J., Boom, R., Vereijken, J., New directions towards structure formation and stability of protein-rich foods from globular proteins. Trends in Food Science & Technology 21:2 (2010), 85–94.
    • (2010) Trends in Food Science & Technology , vol.21 , Issue.2 , pp. 85-94
    • Purwanti, N.1    van der Goot, A.J.2    Boom, R.3    Vereijken, J.4
  • 60
    • 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 23:3 (2009), 973–979.
    • (2009) Food Hydrocolloids , vol.23 , Issue.3 , pp. 973-979
    • Rabiey, L.1    Britten, M.2
  • 61
    • 0036214404 scopus 로고    scopus 로고
    • Cold gelation of β-lactoglobulin in the presence of iron
    • Remondetto, G.E., Paquin, P., Subirade, M., Cold gelation of β-lactoglobulin in the presence of iron. Journal of Food Science 67:2 (2002), 586–595.
    • (2002) Journal of Food Science , vol.67 , Issue.2 , pp. 586-595
    • Remondetto, G.E.1    Paquin, P.2    Subirade, M.3
  • 62
    • 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 69:4 (2003), 461–469.
    • (2003) Biopolymers , vol.69 , Issue.4 , pp. 461-469
    • Remondetto, G.E.1    Subirade, M.2
  • 63
    • 84886246769 scopus 로고    scopus 로고
    • Microemulsification–cold gelation of whey proteins for nanoencapsulation of date palm pit extract
    • Sadeghi, S., Madadlou, A., Yarmand, M., Microemulsification–cold gelation of whey proteins for nanoencapsulation of date palm pit extract. Food Hydrocolloids 35 (2014), 590–596.
    • (2014) Food Hydrocolloids , vol.35 , pp. 590-596
    • Sadeghi, S.1    Madadlou, A.2    Yarmand, M.3
  • 64
    • 80052753004 scopus 로고    scopus 로고
    • Measurements and theoretical interpretation of points of zero charge/potential of BSA protein
    • Salis, A., Boström, M., Medda, L., Cugia, F., Barse, B., Parsons, D.F., et al. Measurements and theoretical interpretation of points of zero charge/potential of BSA protein. Langmuir 27:18 (2011), 11597–11604.
    • (2011) Langmuir , vol.27 , Issue.18 , pp. 11597-11604
    • Salis, A.1    Boström, M.2    Medda, L.3    Cugia, F.4    Barse, B.5    Parsons, D.F.6
  • 65
    • 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 23:8 (2007), 4155–4166.
    • (2007) Langmuir , vol.23 , Issue.8 , pp. 4155-4166
    • Schmitt, C.1    Bovay, C.2    Rouvet, M.3    Shojaei-Rami, S.4    Kolodziejczyk, E.5
  • 66
    • 0000714568 scopus 로고
    • Physico-chemical comparison of β-lactoglobulins A and B
    • Tanford, C., Nozaki, Y., Physico-chemical comparison of β-lactoglobulins A and B. Journal of Biological Chemistry 234:11 (1959), 2874–2877.
    • (1959) Journal of Biological Chemistry , vol.234 , Issue.11 , pp. 2874-2877
    • Tanford, C.1    Nozaki, Y.2
  • 68
    • 84863353690 scopus 로고    scopus 로고
    • Stability and gelation behavior of bovine serum albumin pre-aggregates in the presence of calcium chloride
    • Wu, H., Arosio, P., Podolskaya, O.G., Wei, D., Morbidelli, M., Stability and gelation behavior of bovine serum albumin pre-aggregates in the presence of calcium chloride. Physical Chemistry Chemical Physics 14:14 (2012), 4906–4916.
    • (2012) Physical Chemistry Chemical Physics , vol.14 , Issue.14 , pp. 4906-4916
    • Wu, H.1    Arosio, P.2    Podolskaya, O.G.3    Wei, D.4    Morbidelli, M.5
  • 69
    • 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 6:6 (2005), 3189–3197.
    • (2005) Biomacromolecules , vol.6 , Issue.6 , pp. 3189-3197
    • Wu, H.1    Xie, J.2    Morbidelli, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.