Olive oil-in-water emulsions stabilized with caseinate: Elucidation of protein-lipid interactions by infrared spectroscopy

被引:77
作者
Herrero, A. M. [1 ]
Carmona, P. [2 ]
Pintado, T. [1 ]
Jimenez-Colmenero, F. [1 ]
Ruiz-Capillas, C. [1 ]
机构
[1] CSIC, Inst Frio, ICTAN, E-28040 Madrid, Spain
[2] CSIC, Inst Estructura Mat, E-28006 Madrid, Spain
关键词
Oil-in-water emulsion; FT-IR; Lipid structure; Protein structure; HIGH-PRESSURE HOMOGENIZATION; REPLACING PORK BACKFAT; SECONDARY STRUCTURE; MICROBIAL TRANSGLUTAMINASE; BETA-LACTOGLOBULIN; CIRCULAR-DICHROISM; SODIUM CASEINATE; CROSS-LINKING; WHEY-PROTEIN; EDIBLE OILS;
D O I
10.1016/j.foodhyd.2010.04.014
中图分类号
O69 [应用化学];
学科分类号
081704 ;
摘要
This paper reports a FT-IR study for probing lipid and protein structural changes and their interactions in various oil-in-water emulsions. Two different emulsions were prepared using sodium caseinate, as stabilizer system, without and with microbial transglutaminase (MTG), denominated E/SC and E/SC + MTG respectively. Proximate composition, fat and water binding properties and textural characteristics were also evaluated in the emulsions. Penetration force and gel strength values were used to distinguish different (P < 0.05) textural behaviours depending on the formulation of emulsifying system. E/SC + MTG emulsion showed gel textural behaviour while E/SC lack of this property. The spectral results showed frequency upshifting of the amide I band in going from protein stabilizer systems isolate (the solution used as reference) to their corresponding emulsions, what is attributable to greater protein structural order upon emulsion formation. Enzymatic action of MTG in the sodium caseinate stabilizing system induces structural changes, in terms of lipid chain disorder or lipid-protein interactions and protein secondary modifications, which may reflect the formation of a gel structure in the emulsion. These results could help to choose the stabilizing system that is most suitable and effective for its use in the formulation of food products. (C) 2010 Elsevier Ltd. All rights reserved.
引用
收藏
页码:12 / 18
页数:7
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