메뉴 건너뛰기




Volumn 91, Issue , 2019, Pages 263-274

Investigating the effect of temperature on the formation and stabilization of ovalbumin foams

Author keywords

Concentration; Interfacial properties; Protein; Structural characterization; Viscosity

Indexed keywords

ADSORPTION; STABILIZATION; TEMPERATURE;

EID: 85060946526     PISSN: 0268005X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.foodhyd.2019.01.030     Document Type: Article
Times cited : (34)

References (41)
  • 1
    • 0023438805 scopus 로고
    • Adsorption of α-lactalbumin and β-lactoglobulin on metal surfaces versus temperature
    • Arnebrant, T., Barton, K., Nylander, T., Adsorption of α-lactalbumin and β-lactoglobulin on metal surfaces versus temperature. Journal of Colloid and Interface Science 119:2 (1987), 383–390 https://doi.org/10.1016/0021-9797(87)90284-0.
    • (1987) Journal of Colloid and Interface Science , vol.119 , Issue.2 , pp. 383-390
    • Arnebrant, T.1    Barton, K.2    Nylander, T.3
  • 2
    • 0003835011 scopus 로고    scopus 로고
    • Static and dynamic properties of proteins adsorbed at liquid interfaces
    • Wageningen university Wageningen
    • Benjamins, J., Static and dynamic properties of proteins adsorbed at liquid interfaces. 2000, Wageningen university, Wageningen.
    • (2000)
    • Benjamins, J.1
  • 4
    • 0032798799 scopus 로고    scopus 로고
    • Protein adsorption at the oil/water interface: Characterization of adsorption kinetics by dynamic interfacial tension measurements
    • Beverung, C.J., Radke, C.J., Blanch, H.W., Protein adsorption at the oil/water interface: Characterization of adsorption kinetics by dynamic interfacial tension measurements. Biophyical Chemistry 81:1 (1999), 59–80 https://doi.org/10.1016/S0301-4622(99)00082-4.
    • (1999) Biophyical Chemistry , vol.81 , Issue.1 , pp. 59-80
    • Beverung, C.J.1    Radke, C.J.2    Blanch, H.W.3
  • 5
    • 11844299475 scopus 로고
    • Adsorption kinetics of ovalbumin monolayers
    • Blank, M., Lee, B.B., Britten, J.S., Adsorption kinetics of ovalbumin monolayers. Journal of Colloid and Interface Science 50:2 (1975), 215–222 https://doi.org/10.1016/0021-9797(75)90223-4.
    • (1975) Journal of Colloid and Interface Science , vol.50 , Issue.2 , pp. 215-222
    • Blank, M.1    Lee, B.B.2    Britten, J.S.3
  • 6
    • 17644396054 scopus 로고    scopus 로고
    • Protein stabilization of emulsions and foams
    • Damodaran, S., Protein stabilization of emulsions and foams. Journal of Food Science 70:3 (2005), R54–R66 https://doi.org/10.1111/j.1365-2621.2005.tb07150.x.
    • (2005) Journal of Food Science , vol.70 , Issue.3 , pp. R54-R66
    • Damodaran, S.1
  • 7
    • 84915753481 scopus 로고    scopus 로고
    • Quantitative description of the parameters affecting the adsorption behaviour of globular proteins
    • Delahaije, R.J.B.M., Gruppen, H., Giuseppin, M.L.F., Wierenga, P.A., Quantitative description of the parameters affecting the adsorption behaviour of globular proteins. Colloids and Surfaces B: Biointerfaces 123 (2014), 199–206 https://doi.org/10.1016/j.colsurfb.2014.09.015.
    • (2014) Colloids and Surfaces B: Biointerfaces , vol.123 , pp. 199-206
    • Delahaije, R.J.B.M.1    Gruppen, H.2    Giuseppin, M.L.F.3    Wierenga, P.A.4
  • 10
    • 84944080843 scopus 로고    scopus 로고
    • Enzymatic cross-linking of α-lactalbumin to produce nanoparticles with increased foam stability
    • Dhayal, S.K., Delahaije, R.J.B.M., de Vries, R.J., Gruppen, H., Wierenga, P.A., Enzymatic cross-linking of α-lactalbumin to produce nanoparticles with increased foam stability. Soft Matter 11:40 (2015), 7888–7898 https://doi.org/10.1039/C5SM01112D.
    • (2015) Soft Matter , vol.11 , Issue.40 , pp. 7888-7898
    • Dhayal, S.K.1    Delahaije, R.J.B.M.2    de Vries, R.J.3    Gruppen, H.4    Wierenga, P.A.5
  • 11
    • 49249153429 scopus 로고
    • Proteins at liquid interfaces: I. Kinetics of adsorption and surface denaturation
    • Graham, D.E., Phillips, M.C., Proteins at liquid interfaces: I. Kinetics of adsorption and surface denaturation. Journal of Colloid and Interface Science 70:3 (1979), 403–414 https://doi.org/10.1016/0021-9797(79)90048-1.
    • (1979) Journal of Colloid and Interface Science , vol.70 , Issue.3 , pp. 403-414
    • Graham, D.E.1    Phillips, M.C.2
  • 12
    • 0019363851 scopus 로고
    • Protein-stabilized foams and emulsions
    • Halling, P.J., Protein-stabilized foams and emulsions. CRC Critical Reviews in Food Science & Nutrition 15:2 (1981), 155–203 https://doi.org/10.1080/10408398109527315.
    • (1981) CRC Critical Reviews in Food Science & Nutrition , vol.15 , Issue.2 , pp. 155-203
    • Halling, P.J.1
  • 13
    • 0033961193 scopus 로고    scopus 로고
    • A calorimetric study of the influence of calcium on the stability of bovine α-lactalbumin
    • Hendrix, T., Griko, Y.V., Privalov, P.L., A calorimetric study of the influence of calcium on the stability of bovine α-lactalbumin. Biophysical Chemistry 84:1 (2000), 27–34 https://doi.org/10.1016/S0301-4622(99)00140-4.
    • (2000) Biophysical Chemistry , vol.84 , Issue.1 , pp. 27-34
    • Hendrix, T.1    Griko, Y.V.2    Privalov, P.L.3
  • 14
    • 84995478962 scopus 로고    scopus 로고
    • Intermolecular and surface forces
    • 3rd ed. Academic Press New York
    • Israelachvili, J.N., Intermolecular and surface forces. 3rd ed., 2011, Academic Press, New York.
    • (2011)
    • Israelachvili, J.N.1
  • 16
    • 84998379089 scopus 로고
    • Protein flexibility and functional properties of heat-denatured ovalbumin and lysozyme
    • Kato, A., Fujimoto, K., Matsudomi, N., Kobayashi, K., Protein flexibility and functional properties of heat-denatured ovalbumin and lysozyme. Agricultural & Biological Chemistry 50:2 (1986), 417–420 https://doi.org/10.1271/bbb1961.50.417.
    • (1986) Agricultural & Biological Chemistry , vol.50 , Issue.2 , pp. 417-420
    • Kato, A.1    Fujimoto, K.2    Matsudomi, N.3    Kobayashi, K.4
  • 18
    • 77953865084 scopus 로고    scopus 로고
    • Principles of fluorescence spectroscopy
    • 3rd ed. Springer New York
    • Lakowicz, J.R., Principles of fluorescence spectroscopy. 3rd ed., 2006, Springer, New York.
    • (2006)
    • Lakowicz, J.R.1
  • 19
    • 84965113836 scopus 로고    scopus 로고
    • Identification of critical concentrations determining foam ability and stability of β-lactoglobulin
    • Lech, F.J., Delahaije, R.J.B.M., Meinders, M.B.J., Gruppen, H., Wierenga, P.A., Identification of critical concentrations determining foam ability and stability of β-lactoglobulin. Food Hydrocolloids 57 (2016), 46–54 https://doi.org/10.1016/j.foodhyd.2016.01.005.
    • (2016) Food Hydrocolloids , vol.57 , pp. 46-54
    • Lech, F.J.1    Delahaije, R.J.B.M.2    Meinders, M.B.J.3    Gruppen, H.4    Wierenga, P.A.5
  • 20
    • 35648946288 scopus 로고
    • Kinetics of adsorption of proteins at interfaces. Part I. The role of bulk diffusion in adsorption
    • MacRitchie, F., Alexander, A.E., Kinetics of adsorption of proteins at interfaces. Part I. The role of bulk diffusion in adsorption. Journal of Colloid Science 18:5 (1963), 453–457 https://doi.org/10.1016/0095-8522(63)90036-9.
    • (1963) Journal of Colloid Science , vol.18 , Issue.5 , pp. 453-457
    • MacRitchie, F.1    Alexander, A.E.2
  • 22
    • 0034737923 scopus 로고    scopus 로고
    • Viscosity analysis of the temperature dependence of the solution conformation of ovalbumin
    • Monkos, K., Viscosity analysis of the temperature dependence of the solution conformation of ovalbumin. Biophysical Chemistry 85:1 (2000), 7–16 https://doi.org/10.1016/S0301-4622(00)00127-7.
    • (2000) Biophysical Chemistry , vol.85 , Issue.1 , pp. 7-16
    • Monkos, K.1
  • 23
    • 0000197271 scopus 로고
    • Structural characteristics and foaming properties of β-lactoglobulin: Effects of shear rate and temperature
    • Phillips, L.G., Hawks, S.E., German, J.B., Structural characteristics and foaming properties of β-lactoglobulin: Effects of shear rate and temperature. Journal of Agricultural and Food Chemistry 43:3 (1995), 613–619 https://doi.org/10.1021/jf00051a011.
    • (1995) Journal of Agricultural and Food Chemistry , vol.43 , Issue.3 , pp. 613-619
    • Phillips, L.G.1    Hawks, S.E.2    German, J.B.3
  • 26
    • 0038717733 scopus 로고    scopus 로고
    • Interrelation between drop size and protein adsorption at various emulsification conditions
    • Tcholakova, S., Denkov, N.D., Sidzhakova, D., Ivanov, I.B., Campbell, B., Interrelation between drop size and protein adsorption at various emulsification conditions. Langmuir 19:14 (2003), 5640–5649 https://doi.org/10.1021/la034411f.
    • (2003) Langmuir , vol.19 , Issue.14 , pp. 5640-5649
    • Tcholakova, S.1    Denkov, N.D.2    Sidzhakova, D.3    Ivanov, I.B.4    Campbell, B.5
  • 27
    • 0002123958 scopus 로고
    • Adsorption of globular proteins at the air/water interface as measured via dynamic surface tension: Concentration dependence, mass-transfer considerations, and adsorption kinetics
    • Tripp, B.C., Magda, J.J., Andrade, J.D., Adsorption of globular proteins at the air/water interface as measured via dynamic surface tension: Concentration dependence, mass-transfer considerations, and adsorption kinetics. Journal of Colloid and Interface Science 173:1 (1995), 16–27 https://doi.org/10.1006/jcis.1995.1291.
    • (1995) Journal of Colloid and Interface Science , vol.173 , Issue.1 , pp. 16-27
    • Tripp, B.C.1    Magda, J.J.2    Andrade, J.D.3
  • 29
    • 4444240383 scopus 로고
    • Possible mechanism for the spontaneous rupture of thin, free liquid films
    • Vrij, A., Possible mechanism for the spontaneous rupture of thin, free liquid films. Discussions of the Faraday Society 42 (1966), 23–33 https://doi.org/10.1039/DF9664200023.
    • (1966) Discussions of the Faraday Society , vol.42 , pp. 23-33
    • Vrij, A.1
  • 30
    • 33947308102 scopus 로고
    • Rupture of thin liquid films due to spontaneous fluctuations in thickness
    • Vrij, A., Overbeek, J.T.G., Rupture of thin liquid films due to spontaneous fluctuations in thickness. Journal of the American Chemical Society 90:12 (1968), 3074–3078 https://doi.org/10.1021/ja01014a015.
    • (1968) Journal of the American Chemical Society , vol.90 , Issue.12 , pp. 3074-3078
    • Vrij, A.1    Overbeek, J.T.G.2
  • 31
    • 0025756767 scopus 로고
    • Protein adsorption to solid surfaces
    • Wahlgren, M., Arnebrant, T., Protein adsorption to solid surfaces. Trends in Biotechnology 9:1 (1991), 201–208 https://doi.org/10.1016/0167-7799(91)90064-O.
    • (1991) Trends in Biotechnology , vol.9 , Issue.1 , pp. 201-208
    • Wahlgren, M.1    Arnebrant, T.2
  • 32
    • 36849122851 scopus 로고
    • Time-dependence of boundary tensions of solutions I. The role of diffusion in time-effects
    • Ward, A.F.H., Tordai, L., Time-dependence of boundary tensions of solutions I. The role of diffusion in time-effects. The Journal of Chemical Physics 14:7 (1946), 453–461 https://doi.org/10.1063/1.1724167.
    • (1946) The Journal of Chemical Physics , vol.14 , Issue.7 , pp. 453-461
    • Ward, A.F.H.1    Tordai, L.2
  • 33
    • 0344413605 scopus 로고    scopus 로고
    • Heat-induced denaturation and aggregation of ovalbumin at neutral pH described by irreversible first-order kinetics
    • Weijers, M., Barneveld, P.A., Cohen Stuart, M.A., Visschers, R.W., Heat-induced denaturation and aggregation of ovalbumin at neutral pH described by irreversible first-order kinetics. Protein Science 12:12 (2003), 2693–2703 https://doi.org/10.1110/ps.03242803.
    • (2003) Protein Science , vol.12 , Issue.12 , pp. 2693-2703
    • Weijers, M.1    Barneveld, P.A.2    Cohen Stuart, M.A.3    Visschers, R.W.4
  • 34
    • 33646904280 scopus 로고    scopus 로고
    • The adsorption and unfolding kinetics determines the folding state of proteins at the air-water interface and thereby the equation of state
    • Wierenga, P.A., Egmond, M.R., Voragen, A.G.J., de Jongh, H.H.J., The adsorption and unfolding kinetics determines the folding state of proteins at the air-water interface and thereby the equation of state. Journal of Colloid and Interface Science 299:2 (2006), 850–857 https://doi.org/10.1016/j.jcis.2006.03.016.
    • (2006) Journal of Colloid and Interface Science , vol.299 , Issue.2 , pp. 850-857
    • Wierenga, P.A.1    Egmond, M.R.2    Voragen, A.G.J.3    de Jongh, H.H.J.4
  • 35
    • 0142216171 scopus 로고    scopus 로고
    • Protein exposed hydrophobicity reduces the kinetic barrier for adsorption of ovalbumin to the air-water interface
    • Wierenga, P.A., Meinders, M.B.J., Egmond, M.R., Voragen, A.G.J., de Jongh, H.H.J., Protein exposed hydrophobicity reduces the kinetic barrier for adsorption of ovalbumin to the air-water interface. Langmuir 19:21 (2003), 8964–8970 https://doi.org/10.1021/la034868p.
    • (2003) Langmuir , vol.19 , Issue.21 , pp. 8964-8970
    • Wierenga, P.A.1    Meinders, M.B.J.2    Egmond, M.R.3    Voragen, A.G.J.4    de Jongh, H.H.J.5
  • 36
    • 25444511609 scopus 로고    scopus 로고
    • Quantitative description of the relation between protein net charge and protein adsorption to air-water interfaces
    • Wierenga, P.A., Meinders, M.B.J., Egmond, M.R., Voragen, A.G.J., De Jongh, H.H.J., Quantitative description of the relation between protein net charge and protein adsorption to air-water interfaces. Journal of Physical Chemistry B 109:35 (2005), 16946–16952 https://doi.org/10.1021/jp050990g.
    • (2005) Journal of Physical Chemistry B , vol.109 , Issue.35 , pp. 16946-16952
    • Wierenga, P.A.1    Meinders, M.B.J.2    Egmond, M.R.3    Voragen, A.G.J.4    De Jongh, H.H.J.5
  • 37
    • 0033764172 scopus 로고    scopus 로고
    • Interfaces: Their role in foam and emulsion behaviour
    • Wilde, P.J., Interfaces: Their role in foam and emulsion behaviour. Current Opinion in Colloid & Interface Science 5:3–4 (2000), 176–181 https://doi.org/10.1016/S1359-0294(00)00056-X.
    • (2000) Current Opinion in Colloid & Interface Science , vol.5 , Issue.3-4 , pp. 176-181
    • Wilde, P.J.1
  • 38
    • 33847088763 scopus 로고
    • Low-pressure solubility of gases in liquid water
    • Wilhelm, E., Battino, R., Wilcock, R.J., Low-pressure solubility of gases in liquid water. Chemical Reviews 77:2 (1977), 219–262 https://doi.org/10.1021/cr60306a003.
    • (1977) Chemical Reviews , vol.77 , Issue.2 , pp. 219-262
    • Wilhelm, E.1    Battino, R.2    Wilcock, R.J.3
  • 39
    • 0026900461 scopus 로고
    • The role of chemical potential in the adsorption of lysozyme at the air-water interface
    • Xu, S., Damodaran, S., The role of chemical potential in the adsorption of lysozyme at the air-water interface. Langmuir 8:8 (1992), 2021–2027 https://doi.org/10.1021/la00044a024.
    • (1992) Langmuir , vol.8 , Issue.8 , pp. 2021-2027
    • Xu, S.1    Damodaran, S.2
  • 41
    • 0000909358 scopus 로고
    • Kinetics of protein foam destabilization: Evaluation of a method using bovine serum albumin
    • Yu, M.A., Damodaran, S., Kinetics of protein foam destabilization: Evaluation of a method using bovine serum albumin. Journal of Agricultural and Food Chemistry 39:9 (1991), 1555–1562 https://doi.org/10.1021/jf00009a004.
    • (1991) Journal of Agricultural and Food Chemistry , vol.39 , Issue.9 , pp. 1555-1562
    • Yu, M.A.1    Damodaran, S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.