Rehydration of casein powders: effects of added mineral salts and salt addition methods on water transfer

Schuck, Pierre; Davenel, A.; Mariette, François; Briard, Valérie; Méjean, Serge; Piot, Michel

doi:10.1016/s0958-6946(01)00090-5

Cited by 89 publications

(88 citation statements)

References 15 publications

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“…Improvement in foaming properties was also described after addition of hexametaphosphate (Kelly and Burgess 1978), EDTA (Ward et al 1997), or citrate (Augustin and Clarke 2008) to milk. Schuck et al (2002) and Schokker et al (2011) indicated that solubilization of micellar powder was improved in presence of citrate (in comparison with solubilization in water). Ye (2011) indicated that stable emulsions were formed in presence of protein concentrates having low micellar calcium content.…”

Section: Addition Of Calcium Chelatantsmentioning

confidence: 99%

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

Broyard

Gaucheron

2015

Dairy Sci. & Technol.

264

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: Addition Of Calcium Chelatantsmentioning

confidence: 99%

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

Broyard

Gaucheron

2015

Dairy Sci. & Technol.

264

133

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“…NaCl is more effective if it is included in the concentrate and dried with the milk solution [42]. It can be deduced that NaCl is most effective when it alters the binding forces within the micelle during drying.…”

Section: Modification Of Composition and The Role Of Mineral Ionsmentioning

confidence: 99%

Insolubility of milk powder products – A minireview

Baldwin

2010

Dairy Sci. Technol.

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-In this paper, the formation of insolubility in milk powder is described, and the factors affecting the reaction are discussed. The zone in which casein proteins are most sensitive to heat is in the moisture range that occurs during spray drying. The rate of reaction has been determined and shows differences of orders of magnitude with the moisture content. The effect of chemical reagents on the extent of reaction gives insights into the chemical bonds that inhibit hydration. Information on the drying of casein products and individual proteins is used to infer that the withdrawal of moisture from casein proteins and the concentration of divalent cations during drying lead to alterations in the conformation of proteins that have an adverse effect on their rehydration during reconstitution. Further work to fully characterise these effects is required.spray drying / powder / casein / insolubility / kineticsRésumé -Insolubilité des poudres laitières -une mini-revue. L'apparition de l'insolubilité des poudres laitières est décrite et les facteurs affectant cette réaction sont discutés dans cet article. La zone dans laquelle les caséines sont les plus sensibles à la chaleur se situe dans la gamme d'humidité intervenant au cours du procédé de séchage par atomisation. La vitesse de réaction a été déterminée et montre des différences d'ordres de grandeur des taux d'humidité. L'effet des réactifs chimiques sur l'étendue de la réaction donne un aperçu des liaisons chimiques qui inhibent l'hydratation. On peut déduire de l'information obtenue sur le séchage des caséines et des protéines individuelles que l'élimination de l'humidité des caséines et la concentration en cations divalents au cours du séchage conduisent à des modifications de la conformation des protéines qui peuvent avoir des effets négatifs sur leur réhydratation au cours de la reconstitution des poudres. Un travail ultérieur est nécessaire pour caractériser complètement ces effets.séchage par atomisation / poudre / caséine / insolubilité / cinétique

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“…[13][14][15][16] Addition of NaCl generally increases hydration, voluminosity, screening of charges of caseins and calcium ion activity in the milk serum whereas it decreases pH and the amount of supernatant casein, 17,18 improves rehydration of casein micellar powder, 19 imparts changes in casein micellar structure and micellar mineral composition. [20][21][22] In earlier investigations, various but limited techniques have been employed to study the effect of NaCl on the structural properties of casein micelles or milk systems including transmission electron microscopy (TEM) [23][24][25] , scanning electron microscopy (SEM) 26 and dynamic light scattering (DLS). 27,28 Several methods with their certain merits have been used for the analysis of proteins structure.…”

Section: Introductionmentioning

confidence: 99%

Multiscale Characterization of Casein Micelles Under NaCl Range Conditions

et al. 2011

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Micellar casein (MC) dispersions were studied at a constant protein concentration of 5 wt % in high NaCl environment. The micellar edifices were characterized as to their morphology, size, and content of proteins in the supernatant after ultracentrifugation. Additionally, changes in secondary structures of the protein upon salt increase were followed by Fourier Transform Infrared Spectroscopy (FTIR). For the first time, the estimations of secondary structural elements (irregular, ß-sheet, α-helix and turn) from Amide III assignments were correlated with results from Amide I. Casein micelles dispersions in water were characterized by Transmission Electron Microscopy (TEM) by a spherical shape and a size between 100 and 200 nm. A salt increase resulted to a destabilization of the micelle and the formation of mini-micelles more or less aggregated. The size of the new edifice was almost similar to the native micelle. These TEM observations were confirmed by a constant casein micelle hydrodynamic diameter determined by Dynamic Light Scattering (DLS) and ranging between 150 and 180 nm. Upon salt increase, FTIR revealed an increase in irregular structures and a concurrent decrease in ß-sheet structures. Secondary structural elements percentages were almost similar from Amide I and Amide III. The use of these multiscale techniques led to a better understanding of the micellar edifice under high salt environment. Around 3% NaCl addition, a good correlation was observed between destabilization of the micellar edifice, modifications of the caseins secondary structure and repartition of caseins between supernatant and pellet after ultracentrifugation.

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Rehydration of casein powders: effects of added mineral salts and salt addition methods on water transfer

Cited by 89 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

Insolubility of milk powder products – A minireview

Multiscale Characterization of Casein Micelles Under NaCl Range Conditions

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