Properties of dephosphorylated α<sub>s1</sub>-casein. Precipitation by calcium ions and micelle formation

Bingham, Elizabeth W.; Farrell, Harold M.; Carroll, Robert J.

doi:10.1021/bi00763a010

Cited by 72 publications

(22 citation statements)

References 17 publications

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“…α s -casein, β-casein, κ-casein, β-lactoglobulin, or α-lactalbumin) is often more studied in the literature [2,5,13,14,20,21]. Hence, whole milk protein solution (prepared from industrial skim milk powder) was titrated with CC (50 mmol·L ) at 25°C to thermodynamically characterize Ca-protein interactions.…”

Section: Resultsmentioning

confidence: 99%

Thermodynamic characterization of calcium-milk protein interaction by isothermal titration calorimetry

Canabady-Rochelle¹,

Sánchez²,

Mellema

et al. 2009

Dairy Sci. Technol.

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-In milk, casein micelles are the natural vectors of calcium (Ca) and constitute an ideal vehicle for the delivery of additional Ca, through Ca-protein interactions. Isothermal titration calorimetry (ITC) is a technique of choice in the study of biomolecular interactions and especially in mineral-protein interactions. Calcium-milk protein interactions were thermodynamically characterized by titration of cow's milk protein with calcium chloride (CC) using ITC. Experiments similar to that of ITC were reproduced and analyzed with other techniques (granulometry and electrophoretic mobility measurement) to better understand the nature of interactions. Binding titration curves were fitted with the "one set of sites model" to determine the thermodynamic parameters (N, 6 mol Ca·mol ). Milk proteins bound up to 8 mg Ca·g −1 of protein at saturation. The global thermodynamic signal obtained upon titration was endothermic. The electrophoretic mobility variations of casein micelles occurring upon CC titration were indicative of Ca-protein interactions of electrostatic nature. Hence, the usual exothermic signal involved in electrostatic interactions was completely hidden by the strong endothermic signal coming from the release of water molecules, either from the hydration shell of the Ca ions and/or dehydration of hydrophobic core of proteins. Particle size variations were indicative of casein micelle retraction upon CC titration.calcium / milk protein / interaction / isothermal titration calorimetry / nano-sizer 摘要 -等温滴定量热法研究钙-乳蛋白质相互作用的热力学性质○ 在乳中，钙与酪蛋白相互作用，使得酪蛋白胶束成为钙的天然载体和理想的传递者○ 等温滴定量热法是用来研究生物分子之间相互作用，特别是矿物元素-蛋白质间相互作用的一种有效方法○ 采用等温滴定量热法用氯化钙滴定乳蛋白质就可以研究钙-乳蛋白相互作用的热力学性质○ 本文同时还采用粒度测定和电泳迁移测定法进行了对比分析○ 根据测定的热力学参数 (N, 6 mol·Ca· mol −1 乳蛋白; 束缚参数 K, 1070 mol·L −1 ; 束缚热焓 H, 1910 cal·mol −1 氯化钙; 熵 S, cal·mol −1 ·K −1 ) 确定的束缚滴定曲线符合 "one set of sited" 模型○ 在饱和状态下每克乳蛋白

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Section: Resultsmentioning

confidence: 99%

Thermodynamic characterization of calcium-milk protein interaction by isothermal titration calorimetry

Canabady-Rochelle¹,

Sánchez²,

Mellema

et al. 2009

Dairy Sci. Technol.

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“…The loss of phosphate groups reduced the number of calcium bridges (Aoki et al 1985). Formation of artificial micelles with dephosphorylated caseins was difficult because of the removal of the majority of calcium-binding sites (Pepper and Thompson 1963;Yamauchi et al 1967;Bingham et al 1972;Pearse et al 1986;McCarthy et al 2013) and resulted in the formation of abnormal micelles less stable in presence of calcium and smaller in size (Pepper and Thompson 1963;Knoop and Peters 1975;Pearse et al 1986;Hiller and Lorenzen 2009).…”

Section: Dephosphorylationmentioning

confidence: 99%

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

Broyard

Gaucheron

2015

Dairy Sci. & Technol.

252

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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“…[1][2][3][4][5][6][7] The authors 2 ) have reported about the effect of enzymatic dephosphorylation on the interaction of calcium ions with whole and as ,-caseins. The binding of calcium ions to the phosphate groups of (lsI-casein did not seem essential for precipitation.…”

mentioning

confidence: 99%

Effect of Dephosphorylation of Casein on Its Coagulation and Proteolysis by Chymosin

Yamauchi

Yoneda²

1978

Agricultural and Biological Chemistry

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Properties of dephosphorylated α_s1-casein. Precipitation by calcium ions and micelle formation

Cited by 72 publications

References 17 publications

Thermodynamic characterization of calcium-milk protein interaction by isothermal titration calorimetry

Thermodynamic characterization of calcium-milk protein interaction by isothermal titration calorimetry

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

Effect of Dephosphorylation of Casein on Its Coagulation and Proteolysis by Chymosin

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Properties of dephosphorylated αs1-casein. Precipitation by calcium ions and micelle formation

Cited by 72 publications

References 17 publications

Thermodynamic characterization of calcium-milk protein interaction by isothermal titration calorimetry

Thermodynamic characterization of calcium-milk protein interaction by isothermal titration calorimetry

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

Effect of Dephosphorylation of Casein on Its Coagulation and Proteolysis by Chymosin

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Properties of dephosphorylated α_s1-casein. Precipitation by calcium ions and micelle formation