메뉴 건너뛰기




Volumn 54, Issue 1, 2013, Pages 902-909

Glycation of heat-treated β-lactoglobulin: Effects on foaming properties

Author keywords

Beta lactoglobulin; Foaming properties; Glucose glycation; Heat treatment

Indexed keywords

BETA-LACTOGLOBULIN; DIFFERENT TREATMENTS; DISPROPORTIONATIONS; FLUORESCENCE QUENCHING; FOAMING PROPERTIES; GLUCOSE-GLYCATION; PROTEIN CONFORMATION; SPECTROSCOPIC MEASUREMENTS;

EID: 84884776236     PISSN: 09639969     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.foodres.2013.08.013     Document Type: Article
Times cited : (17)

References (36)
  • 1
    • 0017184389 scopus 로고
    • Rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. Rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical Biochemistry 1976, 72(1-2):248-254.
    • (1976) Analytical Biochemistry , vol.72 , Issue.1-2 , pp. 248-254
    • Bradford, M.M.1
  • 2
    • 15744402967 scopus 로고    scopus 로고
    • Thermal unfolding of bovine β-lactoglobulin studied by UV spectroscopy and fluorescence quenching
    • Busti P., Gatti C.A., Delorenzi N.J. Thermal unfolding of bovine β-lactoglobulin studied by UV spectroscopy and fluorescence quenching. Food Research International 2005, 38(5):543-550.
    • (2005) Food Research International , vol.38 , Issue.5 , pp. 543-550
    • Busti, P.1    Gatti, C.A.2    Delorenzi, N.J.3
  • 3
    • 32544442673 scopus 로고    scopus 로고
    • Binding of alkylsulfonate ligands to bovine β-lactoglobulin: Effects on protein thermal unfolding
    • Busti P., Gatti C.A., Delorenzi N.J. Binding of alkylsulfonate ligands to bovine β-lactoglobulin: Effects on protein thermal unfolding. Food Research International 2006, 39(4):503-509.
    • (2006) Food Research International , vol.39 , Issue.4 , pp. 503-509
    • Busti, P.1    Gatti, C.A.2    Delorenzi, N.J.3
  • 4
    • 0023693897 scopus 로고
    • Structural and conformational changes of β-lactoglobulin B: an infrared spectroscopy study of the effect of pH and temperature
    • Cassal H.L., Kohler U., Mantsch H.H. Structural and conformational changes of β-lactoglobulin B: an infrared spectroscopy study of the effect of pH and temperature. Biochimica et Biophysica Acta 1988, 957(1):11-20.
    • (1988) Biochimica et Biophysica Acta , vol.957 , Issue.1 , pp. 11-20
    • Cassal, H.L.1    Kohler, U.2    Mantsch, H.H.3
  • 5
    • 0034921222 scopus 로고    scopus 로고
    • Improvement of functional properties of β-lactoglobulin glycated through the Maillard reaction is related to the nature of sugar
    • Chevalier F., Chobert J.M., Popineau Y., Nicolas M.G., Haertlé T. Improvement of functional properties of β-lactoglobulin glycated through the Maillard reaction is related to the nature of sugar. International Dairy Journal 2001, 11(3):145-152.
    • (2001) International Dairy Journal , vol.11 , Issue.3 , pp. 145-152
    • Chevalier, F.1    Chobert, J.M.2    Popineau, Y.3    Nicolas, M.G.4    Haertlé, T.5
  • 6
    • 47049093974 scopus 로고    scopus 로고
    • Structural characterization of bovine β-lactoglobulin-galactose/tagatose Maillard complexes by electrophoretic, chromatographic, and spectroscopic methods
    • Corzo-Martínez M., Moreno F.J., Olano A., Villamiel M. Structural characterization of bovine β-lactoglobulin-galactose/tagatose Maillard complexes by electrophoretic, chromatographic, and spectroscopic methods. Journal of Agricultural and Food Chemistry 2008, 56(11):4244-4252.
    • (2008) Journal of Agricultural and Food Chemistry , vol.56 , Issue.11 , pp. 4244-4252
    • Corzo-Martínez, M.1    Moreno, F.J.2    Olano, A.3    Villamiel, M.4
  • 7
    • 0028989022 scopus 로고
    • Effect of sodium dodecyl sulfate and palmitic acid on the equilibrium unfolding of bovine beta-lactoglobulin
    • Creamer L.K. Effect of sodium dodecyl sulfate and palmitic acid on the equilibrium unfolding of bovine beta-lactoglobulin. Biochemistry 1995, 34(21):7170-7176.
    • (1995) Biochemistry , vol.34 , Issue.21 , pp. 7170-7176
    • Creamer, L.K.1
  • 8
    • 1942441014 scopus 로고    scopus 로고
    • Spectroscopic characterization of heat induced nonnative β-lactoglobulin monomers
    • Croguennec T., Mollé D., Mehra R., Bouhallab S. Spectroscopic characterization of heat induced nonnative β-lactoglobulin monomers. Protein Science 2004, 13(5):1340-1346.
    • (2004) Protein Science , vol.13 , Issue.5 , pp. 1340-1346
    • Croguennec, T.1    Mollé, D.2    Mehra, R.3    Bouhallab, S.4
  • 10
    • 21444443258 scopus 로고    scopus 로고
    • Stability and texture of protein foams: a study by video image analysis
    • Fains A., Bertrand D., Baniel A., Popineau Y. Stability and texture of protein foams: a study by video image analysis. Food Hydrocolloids 1997, 11(1):63-69.
    • (1997) Food Hydrocolloids , vol.11 , Issue.1 , pp. 63-69
    • Fains, A.1    Bertrand, D.2    Baniel, A.3    Popineau, Y.4
  • 11
    • 25844500998 scopus 로고    scopus 로고
    • Factors determining the physical properties of protein foams
    • Foegeding E.A., Luck P.J., Davis J.P. Factors determining the physical properties of protein foams. Food Hydrocolloids 2006, 20(2-3):284-292.
    • (2006) Food Hydrocolloids , vol.20 , Issue.2-3 , pp. 284-292
    • Foegeding, E.A.1    Luck, P.J.2    Davis, J.P.3
  • 13
    • 0034891796 scopus 로고    scopus 로고
    • Fluoroalcohol-induced structural changes of proteins: some aspects of cosolvent-protein interaction
    • Gast K., Siemer A., Zirwer D., Damaschem G. Fluoroalcohol-induced structural changes of proteins: some aspects of cosolvent-protein interaction. European Biophysics Journal 2001, 30(4):273-283.
    • (2001) European Biophysics Journal , vol.30 , Issue.4 , pp. 273-283
    • Gast, K.1    Siemer, A.2    Zirwer, D.3    Damaschem, G.4
  • 14
    • 0030042763 scopus 로고    scopus 로고
    • Methods to estimate the conformation of proteins and polypeptides from circular dichroism data
    • Greenfield N.J. Methods to estimate the conformation of proteins and polypeptides from circular dichroism data. Analytical Biochemistry 1996, 235(1):1-10.
    • (1996) Analytical Biochemistry , vol.235 , Issue.1 , pp. 1-10
    • Greenfield, N.J.1
  • 15
    • 0014592230 scopus 로고
    • Computed circular dichroism spectra for the evaluation of protein conformation
    • Greenfield N., Fasman G.D. Computed circular dichroism spectra for the evaluation of protein conformation. Biochemistry 1969, 8(10):4108-4116.
    • (1969) Biochemistry , vol.8 , Issue.10 , pp. 4108-4116
    • Greenfield, N.1    Fasman, G.D.2
  • 16
    • 0041169329 scopus 로고    scopus 로고
    • Recent progress in processing of dairy proteins: a review
    • Haertlé T., Chobert J.M. Recent progress in processing of dairy proteins: a review. Journal of Food Biochemistry 1999, 23(4):367-407.
    • (1999) Journal of Food Biochemistry , vol.23 , Issue.4 , pp. 367-407
    • Haertlé, T.1    Chobert, J.M.2
  • 18
    • 38949157661 scopus 로고    scopus 로고
    • Surface hydrophobicity of physicochemically and enzymatically treated milk proteins in relation to tecno-functional properties
    • Hiller B., Lorenzen P.C. Surface hydrophobicity of physicochemically and enzymatically treated milk proteins in relation to tecno-functional properties. Journal of Agricultural and Food Chemistry 2008, 56(2):461-468.
    • (2008) Journal of Agricultural and Food Chemistry , vol.56 , Issue.2 , pp. 461-468
    • Hiller, B.1    Lorenzen, P.C.2
  • 19
    • 0000008542 scopus 로고    scopus 로고
    • Heat induced aggregation of β-lactoglobulin: role of the free thiol group and disulfide bonds
    • Hoffmann M.A.M., van Mil P.J.J.M. Heat induced aggregation of β-lactoglobulin: role of the free thiol group and disulfide bonds. Journal of Agricultural and Food Chemistry 1997, 45(8):2942-2948.
    • (1997) Journal of Agricultural and Food Chemistry , vol.45 , Issue.8 , pp. 2942-2948
    • Hoffmann, M.A.M.1    van Mil, P.J.J.M.2
  • 20
    • 0025301439 scopus 로고
    • Protein secondary structure and circular dichroism: Apractical guide
    • Johnson W.C. Protein secondary structure and circular dichroism: Apractical guide. Proteins: Structure, Function, and Genetics 1990, 7(3):205-214.
    • (1990) Proteins: Structure, Function, and Genetics , vol.7 , Issue.3 , pp. 205-214
    • Johnson, W.C.1
  • 21
    • 25144518570 scopus 로고    scopus 로고
    • Effect of thermal treatment on interfacial properties of beta-lactoglobulin
    • Kim D.A., Cornec M., Narsimhan G. Effect of thermal treatment on interfacial properties of beta-lactoglobulin. Journal of Colloid and Interface Science 2005, 285(1):100-109.
    • (2005) Journal of Colloid and Interface Science , vol.285 , Issue.1 , pp. 100-109
    • Kim, D.A.1    Cornec, M.2    Narsimhan, G.3
  • 22
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227(5259):680-685.
    • (1970) Nature , vol.227 , Issue.5259 , pp. 680-685
    • Laemmli, U.K.1
  • 23
    • 84866028087 scopus 로고    scopus 로고
    • Glycation a promising method for food protein modification: physicochemical properties and structure, a review
    • Liu J., Ru Q., Ding Y. Glycation a promising method for food protein modification: physicochemical properties and structure, a review. Food Research International 2012, 49(1):170-183.
    • (2012) Food Research International , vol.49 , Issue.1 , pp. 170-183
    • Liu, J.1    Ru, Q.2    Ding, Y.3
  • 24
    • 0002447556 scopus 로고
    • A new apparatus for analyzing foaming properties of proteins
    • VCH Publishers, New York, K.D. Schwenke, R. Mothes (Eds.)
    • Loisel W., Guéguen J., Popineau Y. A new apparatus for analyzing foaming properties of proteins. Food proteins: structure and functionality 1993, 320-323. VCH Publishers, New York. K.D. Schwenke, R. Mothes (Eds.).
    • (1993) Food proteins: structure and functionality , pp. 320-323
    • Loisel, W.1    Guéguen, J.2    Popineau, Y.3
  • 25
    • 0033230053 scopus 로고    scopus 로고
    • Effect of heat treatment on the circular dichroism spectra of bovine β-lactoglobulin A, B, and C
    • Manderson G.A., Creamer L.K., Hardman M.J. Effect of heat treatment on the circular dichroism spectra of bovine β-lactoglobulin A, B, and C. Journal of Agricultural and Food Chemistry 1999, 47(11):4557-4567.
    • (1999) Journal of Agricultural and Food Chemistry , vol.47 , Issue.11 , pp. 4557-4567
    • Manderson, G.A.1    Creamer, L.K.2    Hardman, M.J.3
  • 26
    • 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(12):5052-5061.
    • (1998) Journal of Agricultural and Food Chemistry , vol.46 , Issue.12 , pp. 5052-5061
    • Manderson, G.A.1    Hardman, M.J.2    Creamer, L.K.3
  • 27
    • 0036403301 scopus 로고    scopus 로고
    • Network foaming properties of various proteins adsorbed at the air/water interface in relation to foam stability
    • Martin A.H., Grolle K., Bos M.A., Cohen Stuart M.A., van Vliet T. Network foaming properties of various proteins adsorbed at the air/water interface in relation to foam stability. Journal of Colloid and Interface Science 2002, 245(1):175-183.
    • (2002) Journal of Colloid and Interface Science , vol.245 , Issue.1 , pp. 175-183
    • Martin, A.H.1    Grolle, K.2    Bos, M.A.3    Cohen Stuart, M.A.4    van Vliet, T.5
  • 29
    • 52949111347 scopus 로고    scopus 로고
    • The effect of glycation on foam and structural properties of β-lactoglobulin
    • Medrano A., Abirached C., Panizzolo L., Moyna P., Añón M.C. The effect of glycation on foam and structural properties of β-lactoglobulin. Food Chemistry 2009, 113(1):127-133.
    • (2009) Food Chemistry , vol.113 , Issue.1 , pp. 127-133
    • Medrano, A.1    Abirached, C.2    Panizzolo, L.3    Moyna, P.4    Añón, M.C.5
  • 30
    • 0345059266 scopus 로고    scopus 로고
    • Modification of bovine β-lactoglobulin by glycation in a powdered state or in an aqueous solution: effect on association behavior and protein conformation
    • Morgan F., Léonil J., Mollé D., Bouhallab S. Modification of bovine β-lactoglobulin by glycation in a powdered state or in an aqueous solution: effect on association behavior and protein conformation. Journal of Food and Agricultural and Food Chemistry 1999, 47(1):83-91.
    • (1999) Journal of Food and Agricultural and Food Chemistry , vol.47 , Issue.1 , pp. 83-91
    • Morgan, F.1    Léonil, J.2    Mollé, D.3    Bouhallab, S.4
  • 31
    • 79952534829 scopus 로고    scopus 로고
    • Effects of heat-treated β-lactoglobulin and its aggregates on foaming properties
    • Moro A., Báez G.D., Busti P.A., Ballerini G.A., Delorenzi N.J. Effects of heat-treated β-lactoglobulin and its aggregates on foaming properties. Food Hydrocolloids 2011, 25(5):1009-1015.
    • (2011) Food Hydrocolloids , vol.25 , Issue.5 , pp. 1009-1015
    • Moro, A.1    Báez, G.D.2    Busti, P.A.3    Ballerini, G.A.4    Delorenzi, N.J.5
  • 32
    • 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.A., Delorenzi N.J. Hydrophobicity of whey protein concentrates measured by fluorescence quenching and its relation with surface functional properties. Journal of Agricultural and Food Chemistry 2001, 49(10):4784-4789.
    • (2001) Journal of Agricultural and Food Chemistry , vol.49 , Issue.10 , pp. 4784-4789
    • Moro, A.1    Gatti, C.A.2    Delorenzi, N.J.3
  • 34
    • 0035824880 scopus 로고    scopus 로고
    • Characterization of pH-induced transitions of β-lactoglobulin: ultrasonic, densimetric, and spectroscopic studies
    • Taulier N., Chalikian T.V. Characterization of pH-induced transitions of β-lactoglobulin: ultrasonic, densimetric, and spectroscopic studies. Journal of Molecular Biology 2001, 314(4):873-889.
    • (2001) Journal of Molecular Biology , vol.314 , Issue.4 , pp. 873-889
    • Taulier, N.1    Chalikian, T.V.2
  • 35
    • 0002285550 scopus 로고    scopus 로고
    • Foam formation and stability
    • Blackie Academic & Professional, London, G.M. Hall (Ed.)
    • Wilde P.J., Clark D.C. Foam formation and stability. Methods of testing protein functionality 1996, 110-152. Blackie Academic & Professional, London. G.M. Hall (Ed.).
    • (1996) Methods of testing protein functionality , pp. 110-152
    • Wilde, P.J.1    Clark, D.C.2
  • 36
    • 34547181324 scopus 로고    scopus 로고
    • The emulsion flocculation stability of protein-carbohydrate diblock copolymers
    • Wooster T.J., Augustin M.A. The emulsion flocculation stability of protein-carbohydrate diblock copolymers. Journal of Colloid and Interface Science 2007, 313(2):665-675.
    • (2007) Journal of Colloid and Interface Science , vol.313 , Issue.2 , pp. 665-675
    • Wooster, T.J.1    Augustin, M.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.