Critical phosphate salt concentrations leading to altered micellar casein structures and functional intermediates
| Autor: | Charith A. Hettiarachchi, Federico Harte, Y. Saricay, M.D. Culler |
|---|---|
| Rok vydání: | 2019 |
| Předmět: |
chemistry.chemical_classification
Viscosity Caseins Salt (chemistry) Concentration effect Hydrogen-Ion Concentration Apparent viscosity Phosphate Micellar casein Elasticity Phosphates Solutions chemistry.chemical_compound chemistry Rheology Nephelometry and Turbidimetry Genetics Animals Salts Animal Science and Zoology Turbidity Exponential decay Micelles Food Science Nuclear chemistry |
| Zdroj: | Journal of Dairy Science. 102:6820-6829 |
| ISSN: | 0022-0302 |
| DOI: | 10.3168/jds.2018-15746 |
| Popis: | We investigated the effect of different phosphate salts on the structural integrity of micellar casein (MC) at pH 7.0. With the increase of salt concentration, a reduction in turbidity was observed for the MC solutions, and it was modeled using an exponential decay function. The inflection point of the model was defined as the first critical salt concentration (C*), and it is suggested that the salt concentration initiates the disintegration of MC. For linear polyphosphates, C* decreased with the number of phosphate groups. Apparent viscosity (ηapp) of MC solutions increased with the increase of salt concentration, and they recorded a peak while the turbidity decreased to a minimum. The salt concentration that resulted in the highest ηapp was identified as the second critical salt concentration (C**). It is hypothesized that the interactions among protein species present in the mixtures are at an optimum state at C**. Both C* and C** were found to be dependent on the MC concentration. The work presented herein supports an understanding of the concentration effect of phosphate salts on MC for structuring dairy products. |
| Databáze: | OpenAIRE |
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