Interfacial and foaming properties of sulfydryl-modified bovine β-lactoglobulin

被引:47
作者
Croguennec, Thomas
Renault, Anne
Bouhallab, Said
Pezennec, Stephane
机构
[1] INRA, UMR Sci & Technol Lait & Oeuf 1253, F-35042 Rennes, France
[2] Univ Rennes 1, UMR 6626, CNRS, Grp Mat Condensee & Mat, F-35042 Rennes, France
关键词
beta-lactoglobulin; protein conformation; adsorption; surface load; surface pressure; interfacial rheology; foaming properties;
D O I
10.1016/j.jcis.2006.06.061
中图分类号
O64 [物理化学(理论化学)、化学物理学];
学科分类号
070304 ; 081704 ;
摘要
The effects of a control blocking of free cystein by N-ethylmaleimide on the interfacial behavior (kinetics of adsorption at the air/water interface, rheology of the interfacial layer) as well as on the foaming properties (density, stability) of beta-lactoglobulin were investigated. Compared to native beta-lactoglobulin (unmodified beta-lactoglobulin), sulfydryl-modified beta-lactoglobulin exhibited higher surface hydrophobicity, adsorbed faster at the air/water interface, had the capability to develop rapidly an interfacial layer with high shear elastic constant but exhibited a considerably lower shear elastic constant plateau value. Moreover, suifydryl-modified beta-lactoglobulin exhibited better foaming properties especially regarding the short-term foam stability suggesting that the initial rheology of the interfacial film is at least as much important for the general mechanism of foam stabilization as the potential viscoelasticity the interfacial film could reach on aging. (c) 2006 Elsevier Inc. All rights reserved.
引用
收藏
页码:32 / 39
页数:8
相关论文
共 52 条
  • [1] Apenten RKO, 1998, INT J BIOL MACROMOL, V23, P19, DOI 10.1016/S0141-8130(98)00008-7
  • [2] Apenten RKO, 2000, THERMOCHIM ACTA, V359, P181
  • [3] Bos MA, 2001, ADV COLLOID INTERFAC, V91, P437
  • [4] Copper-catalyzed formation of disulfide-linked dimer of bovine β-lactoglobulin
    Bouhallab, S
    Henry, G
    Caussin, F
    Croguennec, T
    Fauquant, J
    Mollé, D
    [J]. LAIT, 2004, 84 (06): : 517 - 525
  • [5] Role of free Cys121 in stabilization of bovine β-lactoglobulin B
    Burova, TV
    Choiset, Y
    Tran, V
    Haertlé, T
    [J]. PROTEIN ENGINEERING, 1998, 11 (11): : 1065 - 1073
  • [6] REVERSIBLE AND IRREVERSIBLE MODIFICATIONS OF BETA-LACTOGLOBULIN UPON EXPOSURE TO HEAT
    CAIROLI, S
    IAMETTI, S
    BONOMI, F
    [J]. JOURNAL OF PROTEIN CHEMISTRY, 1994, 13 (03): : 347 - 354
  • [7] Improvement of functional properties of β-lactoglobulin glycated through the Maillard reaction is related to the nature of the sugar
    Chevalier, F
    Chobert, JM
    Popineau, Y
    Nicolas, MG
    Haertlé, T
    [J]. INTERNATIONAL DAIRY JOURNAL, 2001, 11 (03) : 145 - 152
  • [8] Adsorption dynamics of α-lactalbumin and β-lactoglobulin at air-water interfaces
    Cornec, M
    Cho, D
    Narsimhan, G
    [J]. JOURNAL OF COLLOID AND INTERFACE SCIENCE, 1999, 214 (02) : 129 - 142
  • [9] Adsorption dynamics and interfacial properties of α-lactalbumin in native and molten globule state conformation at air-water interface
    Cornec, M
    Kim, DA
    Narsimhan, G
    [J]. FOOD HYDROCOLLOIDS, 2001, 15 (03) : 303 - 313
  • [10] Spectroscopic characterization of heat-induced nonnative β-lactoglobulin monomers
    Croguennec, T
    Mollé, D
    Mehra, R
    Bouhallab, S
    [J]. PROTEIN SCIENCE, 2004, 13 (05) : 1340 - 1346