Phosphorylation of casein and lysozyme by phosphorus oxychloride

Matheis, Guenter; Penner, Michael H.; Feeney, Robert E.; Whitaker, John R.

doi:10.1021/jf00116a049

Cited by 80 publications

(86 citation statements)

References 15 publications

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“…Due to the increase of the electronegativity of caseins after their phosphorylation, their foaming and emulsifying properties and also their solubility were improved (Girerd et al 1984;Medina et al 1992;Sitohy et al 1995). Nevertheless, Matheis et al (1983) showed that addition of 7.4 phosphate groups per mole of caseins increased their viscosity and capacity of water holding, but decreased their solubility and emulsification capacity.…”

Section: Phosphorylationmentioning

confidence: 98%

Modifications of structures and functions of caseins: a scientific and technological challenge

Broyard

Gaucheron

2015

Dairy Sci. & Technol.

250

133

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Casein molecules are used in food industry as ingredients. They can be used as isolated forms and under micellar form consisting in an association of different casein molecules and calcium phosphate. In this review, after a brief reminder of the main characteristics of casein molecules and casein micelles, the modifications of caseins induced by physical, chemical, and enzymatic actions are reported. The resulting new physicochemical properties (mineral and casein compositions, charge, hydrophobicity, aggregation state, and morphology) and techno-functionalities (heat stability, viscosity, gelation, emulsifying, and foaming properties) are described and discussed with a special attention paid to the results obtained in our laboratory since several decades.

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Section: Phosphorylationmentioning

confidence: 98%

Modifications of structures and functions of caseins: a scientific and technological challenge

Broyard

Gaucheron

2015

Dairy Sci. & Technol.

250

133

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“…As expected of a nitrogen-bound phosphate, the phosphorylated J3-lactoglobulin was acid labile, and it dephosphorylated rapidly under acidic pH conditions. Using somewhat different reaction conditions, Hirotsuka et al 46 reported that up to 140 mol of P/mol of protein could be incorporated into a soy isolate, whereas Matheis et al 42 incorporated 7·4 and 6·2 mol P/mol of casein and lysozyme, respectively. The phosphate in phosphorylated casein was exclusively bound to the hydroxyl oxygen whereas the majority of the phosphate in phosphorylated lysozyme appeared to be bound to nitrogen.…”

Section: Phosphorylationmentioning

confidence: 99%

Modification of Food Proteins by Non-Enzymatic Methods

Shih

1992

Biochemistry of Food Proteins

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“…The chemical shift range of the peak fits with the chemical shift range of 3-4.6 ppm, which has been published previously for serine monophosphate peaks (Ser-O-PO 3 2-) in casein solutions. [30][31][32][33] In the presence of silicate ions, the NMR spectrum shows also a broad-based quartet peak. Upon comparison of both spectra, it follows that in the presence of silicate ions, the NMR signal of Ser-O-PO 3 2-was shifted ca.…”

Section: Resultsmentioning

confidence: 99%

Initiation of Vaterite−Aragonite CaCO₃ Particles from Silicate−Casein Sols

et al. 2008

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31 P NMR difference spectra of sodium caseinate sols with and without silicate ions provide direct evidence of interactions between silicate ions and casein serine phosphate groups. The addition of Ca 2+ to sodium caseinate solution without silicate ions and, subsequently, the diffusion of atmospheric CO 2 to the resulting mixture do not lead to CaCO 3 mineralization, whereas comparable experiments in the presence of silicate ions induce the precipitation of hemispherical three-component microstructures composed of silica, casein, and calcium carbonate. Apparently, the silicate-protein interaction plays a role as promoter for calcium carbonate mineralization in aqueous sols. X-ray diffraction (XRD) and Fourier-transform infrared (FTIR) analyses reveal that vaterite is the crystalline phase of the composites. The observed materials are flat on one side and curved outward on the other side. In time, the flat surface cracks to display a star-like shape. Occasionally, in the center of the crack, layer-by-layer sphere-like particles grow, probably due to a secondary nucleation. These spheres are composed of a large number of two-dimensional aragonitic sheets, which are densely packed and form a multilayered structure.

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Phosphorylation of casein and lysozyme by phosphorus oxychloride

Cited by 80 publications

References 15 publications

Modifications of structures and functions of caseins: a scientific and technological challenge

Modifications of structures and functions of caseins: a scientific and technological challenge

Modification of Food Proteins by Non-Enzymatic Methods

Initiation of Vaterite−Aragonite CaCO₃ Particles from Silicate−Casein Sols

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Phosphorylation of casein and lysozyme by phosphorus oxychloride

Cited by 80 publications

References 15 publications

Modifications of structures and functions of caseins: a scientific and technological challenge

Modifications of structures and functions of caseins: a scientific and technological challenge

Modification of Food Proteins by Non-Enzymatic Methods

Initiation of Vaterite−Aragonite CaCO3 Particles from Silicate−Casein Sols

Contact Info

Product

Resources

About

Initiation of Vaterite−Aragonite CaCO₃ Particles from Silicate−Casein Sols