High hydrostatic pressure improves protein solubility and dispersion stability of mineral-added soybean protein isolate

被引:50
作者
Manassero, Carlos A. [1 ,2 ,3 ]
Vaudagna, Sergio R. [1 ,2 ]
Cristina Anon, Maria [2 ,3 ,4 ,5 ]
Speroni, Francisco [2 ,4 ,5 ]
机构
[1] INTA, Ctr Invest Agroind, Inst Tecnol Alimentos, RA-1708 Moron, Argentina
[2] Consejo Nacl Invest Cient & Tecn, RA-1033 Buenos Aires, DF, Argentina
[3] Univ Nacl La Plata, Fac Ciencias Exactas, Dept Ciencias Biol, Area Bioquim & Control Alimentos, RA-1900 La Plata, Argentina
[4] Univ Nacl La Plata, Fac Ciencias Exactas, CCT La Plata, CIDCA, RA-1900 La Plata, Argentina
[5] Consejo Nacl Invest Cient & Tecn, RA-1900 La Plata, Argentina
关键词
Soybean proteins isolate; Calcium; Solubility; High hydrostatic pressure; SOY PROTEIN; CALCIUM; BINDING; PH; AGGREGATION; GLYCININ;
D O I
10.1016/j.foodhyd.2014.07.020
中图分类号
O69 [应用化学];
学科分类号
081704 ;
摘要
The influence of ion type, ion concentration and pH on the effect of high hydrostatic pressure (HHP) on solubility and dispersion stability of soybean protein isolate (SPI) was analyzed. Solubilizing effect of HHP was detected for calcium-, magnesium- and iron-added SPI, the magnitude of this effect was dependent on ion type, ion concentration and pH. The solubilizing effect was highest for calcium, followed by magnesium and iron at pH 7.0. The pH value affected the levels of solubility and the range of calcium concentration where solubility was increased. HHP-denatured soybean proteins may coexist with different minerals and at different pHs in the form of soluble species. For a given calcium concentration, pH may affect the structure of HHP-induced aggregates, leading to different solubilities and dispersion stabilities. HHP improved the stability of insoluble proteins in calcium- added SPI dispersions, avoiding their settling. Our results confirm that thermal treatment and HHP differentially affect proteineprotein interactions. A transient dissociation of calcium from proteins during HHP is postulated. This dissociation would play a role in the structure of aggregates. When calcium is present during denaturation, different aggregates may be formed if calcium is bound to (thermal treatment) or transiently dissociated from (HHP) SPI proteins. (C) 2014 Elsevier Ltd. All rights reserved.
引用
收藏
页码:629 / 635
页数:7
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