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RESEARCH PRODUCT
Effect of iron chelates on oil–water interface, stabilized by milk proteins: The role of phosphate groups and pH. Prediction of iron transfer from aqueous phase toward fat globule surface by changes of interfacial properties
Philippe CayotTatiana Guzun-cojocaruEliane CasesCamille Loupiacsubject
030309 nutrition & dieteticsGeneral Chemical EngineeringInorganic chemistryIron fortificationSurface tension03 medical and health scienceschemistry.chemical_compound0404 agricultural biotechnologyOil-in-water emulsion[SDV.IDA]Life Sciences [q-bio]/Food engineeringChelationBeta-lactoglobulin2. Zero hunger0303 health sciencesAqueous solutionChromatographybiologyChemistryAqueous two-phase systemEmulsifying activityProteins04 agricultural and veterinary sciencesGeneral ChemistryPhosphate040401 food scienceEmulsionPhosphate groupsbiology.proteinChemical stabilityFood Sciencedescription
International audience; Iron incorporated into food systems induces oxidation and precipitation. The consequences are reduced bioavailability and a functional modification of other food components such as proteins. The iron-chelates such as ferrous bisglycinate represent a possibility to avoid side effects, since the iron is protected. The aim of this study is to investigate the effects of iron-chelates compounds on the properties of an oil/water interface stabilized by caseinate or β-lacotoglobulin, under environmental conditions at 20 °C. Analyses were performed using dynamic drop tensiometry during 5000 s. The aqueous bulk phase is an imidazole/acetate buffer (0.1 M), containing 0.4 × 10−6 M protein, and 0.2 × 10-6 9 M iron-chelates compounds. The results indicate that, under neutral conditions, the addition of some irons salts (NaFe-EDTA or Fe-bisglycinate) do not change the structure of the interface stabilized by a protein containing no phosphate groups (β-lactoglobulin). In the case of caseinate, NaFe-EDTA addition increases the lowering rate of surface tension at pH 6.5. On the contrary, the lowering rate of surface tension with caseinate is inhibited by Fe-bisglycinate at pH 6.5. Such an effect is not observed with β-lactoglobulin. The low transfer of irons ions from the bulk to the interface stabilized by β-lactoglobulin is confirmed by zetameter and FTIR measurements. These results indicate an effective strategy to follow for controlling the physical and chemical stability of an emulsion stabilized with proteins.
year | journal | country | edition | language |
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2010-06-01 | Food Hydrocolloids |