Separation of α-, β- and γ-Casein

Hipp, N. J.; Groves, M.L.; Custer, J.H.; McMeekin, T. L.

doi:10.3168/jds.s0022-0302(52)93702-8

Cited by 290 publications

(61 citation statements)

References 8 publications

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“…The isoelectric point increases on average by 1 pH unit. The enhancement of the differences of the electrostatic potential between the casein fractions by ethanol could be employed for the preparation of enriched or purified α S1 -casein [30,78].…”

Section: Electrostatic Surface and Zeta Potentialsmentioning

confidence: 99%

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Physicochemical analysis of casein solubility in water-ethanol solutions

Mezdour

Brulé²,

Korolczuk³

2006

Lait

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-Due to the change in the apparent acid dissociation constant, when ethanol was added to water solutions of an industrially produced spray-dried sodium caseinate, the solution's pH increased proportionally to the reciprocal relative dielectric constant (1/ε). The pH increased by 1 unit when the ethanol volume fraction reached about 0.60. The casein solubility profile at 20 °C as a function of pH (3-8) and the ethanol volume fraction (0-0.75) was quite well represented by the equation describing the ionisation process. The pH inflection point and the slope coefficient were approximately linearly related to 1/ε. The evolution of the electrostatic surface potential (ψ 0 ) and the zeta potential (ζ) explained the changes in casein solubility as a function of pH and the dielectric constant of the solvent. The increase in ψ 0 by 37 ± 5.2 mV or in ζ by 8.6 ± 1.4 mV raised casein solubility from 10 to 90%.casein / solubility / ethanol / dielectric constant / electrostatic potential 摘要 -水-乙醇溶液中酪蛋白溶解性的理化分析。将乙醇加入到由喷雾干燥生产的酪蛋白酸钠水溶液后，由于表观酸离解常数的变化，溶液的 pH 增加与介电常数的倒数 (1/ε) 成正比。当加入乙醇的体积分数达到 0.6 时，溶液的 pH 增加了 1 个单位。在 20 °C 时，酪蛋白的溶解性与pH (3-8) 和乙醇体积分数(0-0.75)之间的函数关系可以很好地用电离方程描述。 pH拐点和斜率系数与1/ε 基本上呈线性关系。表面静电势 (ψ 0 )和zeta电势(ζ)的变化进程可以很好地解释酪蛋白的溶解性与 pH 和溶剂的介电常数之间函数变化。当ψ 0 增加到 37 ± 5.2 mV 或者 ζ 增加到 08.6 ± 1.4 mV, 酪蛋白的溶解性由 10% 增加达到 90%。酪蛋白 / 溶解性 / 乙醇 / 介电常数 / 静电势 Résumé -Analyse physicochimique de la solubilité de la caséine dans des solutions d'éthanol-eau. En raison du changement de la constante apparente de la dissociation acide, l'ajout d'éthanol aux solutions aqueuses d'un caséinate de sodium industriel séché par pulvérisation, provoque une augmentation du pH des solutions inversement proportionnelle à la constante diélectrique (1/ε). Le pH augmente d'une unité quand la fraction volumique d'éthanol atteint environ 0.6. Le profil de la solubilité de la caséine à 20 °C, pour des pH de 3 à 8 et pour la fraction volumique d'éthanol entre 0 et 0.75, est assez bien représenté par une équation qui décrit le processus d'ionisation. Le point d'inflexion et la pente sont approximativement linéairement liés à 1/ε. L'évolution du potentiel électrostatique de surface (ψ 0 ) et du potentiel zeta (ζ) explique les changements de la solubilité de la caséine en fonction du pH et de la constante diélectrique du solvant. L'augmentation du ψ 0 de 37 ± 5.2 mV ou du ζ de 8.6 ± 1.4 mV élève la solubilité de la caséine de 10 à 90 %.caséine / solubilité / éthanol / constante diélectrique / potentiel électrostatique

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Section: Electrostatic Surface and Zeta Potentialsmentioning

confidence: 99%

“…Alcohol can also be used in the preparation and the purification of individual milk protein fractions [30,39,78,80].…”

Section: Introductionmentioning

confidence: 99%

Physicochemical analysis of casein solubility in water-ethanol solutions

Mezdour

Brulé²,

Korolczuk³

2006

Lait

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“…Whole acid casein was prepared from fresh skimmed milk by adjusting the pH to 4.7, as described by Hipp et al 4 ) The urea method by Hipp et al 5 ) was used to fractionate IX-and p-casein from the whole acid casein. The p-casein fraction was purified by repeating the fractionation procedure three times and dialyzed against a large volume of distilled water to remove any traces of urea.…”

Section: Methodsmentioning

confidence: 99%

Role ofβ-Casein in Milk Curdling

Yun¹,

Ohmiya²,

Shimizu³

1982

Agricultural and Biological Chemistry

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“…()(,l-and f3-Caseins were prepared from and individual Holstein cow's milk by the methods of Zittle et a [24.25) and Hipp et al,26) respectively. Crude soybean 7S and liS proteins were prepared from defatted soybean flour, a gift from Fuji Oil Co., Ltd., by the method of Thanh and Shibasaki.…”

Section: Methodsmentioning

confidence: 99%