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Volumn 57, Issue , 2016, Pages 46-54

Identification of critical concentrations determining foam ability and stability of β-lactoglobulin

Author keywords

Adsorbed amount; Interfacial properties; Protein structure; Thin liquid films; potential

Indexed keywords

EMULSIFICATION; LIQUID FILMS; PROTEINS;

EID: 84965113836     PISSN: 0268005X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.foodhyd.2016.01.005     Document Type: Article
Times cited : (36)

References (34)
  • 2
    • 84861909382 scopus 로고    scopus 로고
    • Effects of ionic strength on the enzymatic hydrolysis of diluted and concentrated whey protein isolate
    • Butré C.I., Wierenga P.A., Gruppen H. Effects of ionic strength on the enzymatic hydrolysis of diluted and concentrated whey protein isolate. Journal of Agricultural and Food Chemistry 2012, 60(22):5644-5651.
    • (2012) Journal of Agricultural and Food Chemistry , vol.60 , Issue.22 , pp. 5644-5651
    • Butré, C.I.1    Wierenga, P.A.2    Gruppen, H.3
  • 4
    • 0017858702 scopus 로고
    • Ellipsometry as a tool to study the adsorption behavior of synthetic and biopolymers at the air-water interface
    • De Feijter J.A., Benjamins J., Veer F.A. Ellipsometry as a tool to study the adsorption behavior of synthetic and biopolymers at the air-water interface. Biopolymers 1978, 17(7):1759-1772.
    • (1978) Biopolymers , vol.17 , Issue.7 , pp. 1759-1772
    • De Feijter, J.A.1    Benjamins, J.2    Veer, F.A.3
  • 9
    • 84884232301 scopus 로고    scopus 로고
    • PH effects on the molecular structure of β-lactoglobulin modified air-water interfaces and its impact on foam rheology
    • Engelhardt K., Lexis M., Gochev G., Konnerth C., Miller R., Willenbacher N., et al. pH effects on the molecular structure of β-lactoglobulin modified air-water interfaces and its impact on foam rheology. Langmuir 2013, 29(37):11646-11655.
    • (2013) Langmuir , vol.29 , Issue.37 , pp. 11646-11655
    • Engelhardt, K.1    Lexis, M.2    Gochev, G.3    Konnerth, C.4    Miller, R.5    Willenbacher, N.6
  • 10
    • 77649270954 scopus 로고    scopus 로고
    • Size and shape of protein molecules at the nanometer level determined by sedimentation, gel filtration, and electron microscopy
    • Erickson H.P. Size and shape of protein molecules at the nanometer level determined by sedimentation, gel filtration, and electron microscopy. Biological Procedures Online 2009, 11(1):32-51.
    • (2009) Biological Procedures Online , vol.11 , Issue.1 , pp. 32-51
    • Erickson, H.P.1
  • 12
    • 32944461715 scopus 로고    scopus 로고
    • Characterization of β-lactoglobulin-sodium alginate interactions in aqueous solutions: a calorimetry, light scattering, electrophoretic mobility and solubility study
    • Harnsilawat T., Pongsawatmanit R., McClements D.J. Characterization of β-lactoglobulin-sodium alginate interactions in aqueous solutions: a calorimetry, light scattering, electrophoretic mobility and solubility study. Food Hydrocolloids 2006, 20(5):577-585.
    • (2006) Food Hydrocolloids , vol.20 , Issue.5 , pp. 577-585
    • Harnsilawat, T.1    Pongsawatmanit, R.2    McClements, D.J.3
  • 13
    • 70149121260 scopus 로고    scopus 로고
    • Electrostatic effects on β-lactoglobulin transitions during heat denaturation as studied by differential scanning calorimetry
    • Haug I.J., Skar H.M., Vegarud G.E., Langsrud T., Draget K.I. Electrostatic effects on β-lactoglobulin transitions during heat denaturation as studied by differential scanning calorimetry. Food Hydrocolloids 2009, 23(8):2287-2293.
    • (2009) Food Hydrocolloids , vol.23 , Issue.8 , pp. 2287-2293
    • Haug, I.J.1    Skar, H.M.2    Vegarud, G.E.3    Langsrud, T.4    Draget, K.I.5
  • 14
    • 0000587723 scopus 로고    scopus 로고
    • Improved emulsifying properties of β-barrel domain peptides obtained by membrane-fractionation of a limited tryptic hydrolysate of β-lactoglobulin
    • Huang X.L., Catignani G.L., Swaisgood H.E. Improved emulsifying properties of β-barrel domain peptides obtained by membrane-fractionation of a limited tryptic hydrolysate of β-lactoglobulin. Journal of Agricultural and Food Chemistry 1996, 44(11):3437-3443.
    • (1996) Journal of Agricultural and Food Chemistry , vol.44 , Issue.11 , pp. 3437-3443
    • Huang, X.L.1    Catignani, G.L.2    Swaisgood, H.E.3
  • 15
    • 47349120456 scopus 로고    scopus 로고
    • Characterization of globular protein solutions by dynamic light scattering, electrophoretic mobility, and viscosity measurements
    • Jachimska B., Wasilewska M., Adamczyk Z. Characterization of globular protein solutions by dynamic light scattering, electrophoretic mobility, and viscosity measurements. Langmuir 2008, 24(13):6866-6872.
    • (2008) Langmuir , vol.24 , Issue.13 , pp. 6866-6872
    • Jachimska, B.1    Wasilewska, M.2    Adamczyk, Z.3
  • 17
    • 84924402376 scopus 로고    scopus 로고
    • Stability properties of surfactant-free thin films at different ionic strengths: measurements and modeling
    • Lech F.J., Wierenga P.A., Gruppen H., Meinders M.B.J. Stability properties of surfactant-free thin films at different ionic strengths: measurements and modeling. Langmuir 2015, 31(9):2777-2782.
    • (2015) Langmuir , vol.31 , Issue.9 , pp. 2777-2782
    • Lech, F.J.1    Wierenga, P.A.2    Gruppen, H.3    Meinders, M.B.J.4
  • 18
    • 33751421851 scopus 로고    scopus 로고
    • Electrostatically driven protein aggregation: β-Lactoglobulin at low ionic strength
    • Majhi P.R., Ganta R.R., Vanam R.P., Seyrek E., Giger K., Dubin P.L. Electrostatically driven protein aggregation: β-Lactoglobulin at low ionic strength. Langmuir 2006, 22(22):9150-9159.
    • (2006) Langmuir , vol.22 , Issue.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
  • 19
    • 33947092713 scopus 로고
    • Emulsifying properties of proteins: evaluation of a turbidimetric technique
    • Pearce K.N., Kinsella J.E. Emulsifying properties of proteins: evaluation of a turbidimetric technique. Journal of Agricultural and Food Chemistry 1978, 26(3):716-723.
    • (1978) Journal of Agricultural and Food Chemistry , vol.26 , Issue.3 , pp. 716-723
    • Pearce, K.N.1    Kinsella, J.E.2
  • 20
    • 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(4):1116-1119.
    • (1990) Journal of Food Science , vol.55 , Issue.4 , pp. 1116-1119
    • Phillips, L.G.1    Schulman, W.2    Kinsella, J.E.3
  • 22
    • 84876334262 scopus 로고    scopus 로고
    • Foam properties of algae soluble protein isolate: effect of pH and ionic strength
    • Schwenzfeier A., Lech F., Wierenga P.A., Eppink M.H.M., Gruppen H. Foam properties of algae soluble protein isolate: effect of pH and ionic strength. Food Hydrocolloids 2013, 33(1):111-117.
    • (2013) Food Hydrocolloids , vol.33 , Issue.1 , pp. 111-117
    • Schwenzfeier, A.1    Lech, F.2    Wierenga, P.A.3    Eppink, M.H.M.4    Gruppen, H.5
  • 23
    • 84954965877 scopus 로고
    • Emulsifying and structural properties of β-lactoglobulin at different pHs
    • Shimizu M., Saito M., Yamauchi K. Emulsifying and structural properties of β-lactoglobulin at different pHs. Agricultural and Biological Chemistry 1985, 49(1):189-194.
    • (1985) Agricultural and Biological Chemistry , vol.49 , Issue.1 , pp. 189-194
    • Shimizu, M.1    Saito, M.2    Yamauchi, K.3
  • 24
    • 0037069481 scopus 로고    scopus 로고
    • Coalescence in β-lactoglobulin-stabilized emulsions: effects of protein adsorption and drop size
    • Tcholakova S., Denkov N.D., Ivanov I.B., Campbell B. Coalescence in β-lactoglobulin-stabilized emulsions: effects of protein adsorption and drop size. Langmuir 2002, 18(23):8960-8971.
    • (2002) Langmuir , vol.18 , Issue.23 , pp. 8960-8971
    • Tcholakova, S.1    Denkov, N.D.2    Ivanov, I.B.3    Campbell, B.4
  • 25
    • 40749130423 scopus 로고    scopus 로고
    • Comparison of solid particles, globular proteins and surfactants as emulsifiers
    • Tcholakova S., Denkov N.D., Lips A. Comparison of solid particles, globular proteins and surfactants as emulsifiers. Physical Chemistry Chemical Physics 2008, 10(12):1608-1627.
    • (2008) Physical Chemistry Chemical Physics , vol.10 , Issue.12 , pp. 1608-1627
    • Tcholakova, S.1    Denkov, N.D.2    Lips, A.3
  • 26
    • 0000819132 scopus 로고
    • Molecular interactions in β-lactoglobulin. IV: the dissociation of β-lactoglobulin below pH 3.52
    • Townend R., Weinberger L., Timasheff S.N. Molecular interactions in β-lactoglobulin. IV: the dissociation of β-lactoglobulin below pH 3.52. Journal of the American Chemical Society 1960, 82(12):3175-3179.
    • (1960) Journal of the American Chemical Society , vol.82 , Issue.12 , pp. 3175-3179
    • Townend, R.1    Weinberger, L.2    Timasheff, S.N.3
  • 29
    • 85168415004 scopus 로고    scopus 로고
    • Appendix H: physical properties of water at 0°C to 100°C
    • Marcel Dekker, New York, NY, USA
    • Walstra P. Appendix H: physical properties of water at 0°C to 100°C. Physical chemistry of foods 2009, 807. Marcel Dekker, New York, NY, USA.
    • (2009) Physical chemistry of foods , pp. 807
    • Walstra, P.1
  • 30
    • 0001015301 scopus 로고
    • Surface properties of β-lactoglobulin: adsorption and rearrangement during film formation
    • Waniska R.D., Kinsella J.E. Surface properties of β-lactoglobulin: adsorption and rearrangement during film formation. Journal of Agricultural and Food Chemistry 1985, 33(6):1143-1148.
    • (1985) Journal of Agricultural and Food Chemistry , vol.33 , Issue.6 , pp. 1143-1148
    • Waniska, R.D.1    Kinsella, J.E.2
  • 32
    • 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. The Journal of Physical Chemistry B 2005, 109(35):16946-16952.
    • (2005) The 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
  • 34
    • 1442335307 scopus 로고    scopus 로고
    • Effect of pH and ionic strength on competitive protein adsorption to air/water interfaces in aqueous foams made with mixed milk proteins
    • Zhang Z., Dalgleish D.G., Goff H.D. Effect of pH and ionic strength on competitive protein adsorption to air/water interfaces in aqueous foams made with mixed milk proteins. Colloids and Surfaces B: Biointerfaces 2004, 34(2):113-121.
    • (2004) Colloids and Surfaces B: Biointerfaces , vol.34 , Issue.2 , pp. 113-121
    • Zhang, Z.1    Dalgleish, D.G.2    Goff, H.D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.