1998
DOI: 10.1021/jf9710185
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Gelation of pH-Aggregated Whey Protein Isolate Solution Induced by Heat, Protease, Calcium Salt, and Acidulant

Abstract: Effects of pH (3.0−7.0) on aggregation of whey protein solution (WPS, 18%) were investigated by examination of turbidity, aggregate size, and microstructure. As expected, maximum turbidity and aggregate sizes occurred at the isoelectric point (pI 5.2) of whey proteins. Lower or higher pH than the pI resulted in a steady decrease of the turbidity and aggregate size. Microstructure analysis revealed that the WPS at pH 5.7 contained loose and irregular aggregates with 200−400 nm sizes. From the pH (5.7)-aggregate… Show more

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Cited by 122 publications
(77 citation statements)
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“…This is similar to methods employed previously (Verheul et al, 1998). Ju and Kilara (1998) claimed that at pH 4.6 some native whey proteins formed aggregates. This did not occur in our work as no protein precipitated when the unheated, time 0, sample was adjusted to pH 4.6.…”
Section: Heat Denaturationsupporting
confidence: 88%
“…This is similar to methods employed previously (Verheul et al, 1998). Ju and Kilara (1998) claimed that at pH 4.6 some native whey proteins formed aggregates. This did not occur in our work as no protein precipitated when the unheated, time 0, sample was adjusted to pH 4.6.…”
Section: Heat Denaturationsupporting
confidence: 88%
“…However, this process has limited application in some food products due to the loss of thermal sensible components during heat treatment. 5,6 An alternative technique has been developed to produce thickening solutions or gels from globular proteins at lower temperatures named cold-set gelation. This process is based on the formation of soluble aggregates by heat denaturation of solutions at relative lower concentrations of proteins than required in heat-set gelation conditions.…”
Section: Introductionmentioning
confidence: 99%
“…Moreover, depending on the chemical factor used to induce gelation (acids, salts, enzymes), the textural properties can be widely different. 6 The addition of polysaccharides can also interfere in the structure of the protein gels due to specific interactions between these two biopolymers. In solution, the proteins can show attraction or repulsion with the polysaccharides depending on their origin, concentration, system pH, ionic strength, and temperature.…”
Section: Introductionmentioning
confidence: 99%
“…Porém, nota-se que as amostras compostas por amido de amaranto gelatinizado previamente (acidificação lenta) possuíam maior valor de índice de consistência (k) e pseudoplasticidade que as amostras em que os componentes foram acidificados e gelatinizados simultaneamente (acidificação rápida). Diversos autores (CAVALLIERI; CUNHA, 2008;CAVALLIERI et al, 2007;BRAGA et al, 2006;JU et al, 1998) destacam a possibilidade de diferentes comportamentos dos géis em resposta aos processos de acidificação (lento ou rápido), dependendo dos diferentes tipos de biopolímeros envolvidos nos sistemas. De uma forma geral, géis acidificados lentamente tendem a formar géis mais fortes e mais elásticos do que sistemas acidificados rapidamente.…”
Section: Cisalhamento Estacionáriounclassified