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Strong Uranium(VI) Binding Onto Bovine Milk Proteins, Selected Protein Sequences, and Model Peptides

Strong Uranium(VI) Binding Onto Bovine Milk Proteins, Selected Protein Sequences, and Model Peptides

Harald Zänker, Katja Heine, Stephan Weiss, Vinzenz Brendler, Richard Husar, Gert Bernhard, Karsten Gloe, Thomas Henle, Astrid Barkleit

Inorg Chem. 2019 Apr 1;58(7):4173-4189.

PMID: 30860361

Abstract:

Hexavalent uranium is ubiquitous in the environment. In view of the chemical and radiochemical toxicity of uranium(VI), a good knowledge of its possible interactions in the environment is crucial. The aim of this work was to identify typical binding and sorption characteristics of uranium(VI) with both the pure bovine milk protein β-casein and diverse related protein mixtures (caseins, whey proteins). For comparison, selected model peptides representing the amino acid sequence 13-16 of β-casein and dephosphorylated β-casein were also studied. Complexation studies using potentiometric titration and time-resolved laser-induced fluorescence spectroscopy revealed that the phosphoryl-containing proteins form uranium(VI) complexes of higher stability than the structure-analog phosphoryl-free proteins. That is in agreement with the sorption experiments showing a significantly higher affinity of caseins toward uranium(VI) in comparison to whey proteins. On the other hand, the total sorption capacity of caseins is lower than that of whey proteins. The discussed binding behavior of milk proteins to uranium(VI) might open up interesting perspectives for sustainable techniques of uranium(VI) removal from aqueous solutions. This was further demonstrated by batch experiments on the removal of uranium(VI) from mineral water samples.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP9000719-B	Casein solution from bovine milk		9000-71-9	Price

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