Preparation of β‐Lactoglobulin and p‐Lactoglobulin‐Free Proteins from Whey Retentate by NaCI Salting Out at Low pH

Mailliart, P.; Ribadeau‐Dumas, B.

doi:10.1111/j.1365-2621.1988.tb08945.x

Cited by 173 publications

(98 citation statements)

References 7 publications

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“…The results were in good agreement with the literature data for individual whey proteins, which show salting out effect at pH < 5.0 [25] and denaturation at pH > 8.0 [45].…”

Section: Resultssupporting

confidence: 82%

Prepurification of ?-lactalbumin with ultrafiltration ceramic membranes from acid casein whey: study of operating conditions

Muller

Chaufer

Merin

et al. 2003

Lait

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-A promising way to produce purified a-lactalbumin (a-LA) is to perform a two-step cascade. The first step of pre-purifying presented herein, consists of ultrafiltration (UF) fractionation of acid casein whey, aiming at increasing the purity of a-LA in the filtrate by total retention of bovine serum albumin and immunoglobulins with only a limited transmission of b-lactoglobulin. The outcome of the present work is a guideline which includes the proper selection of ceramic UF membrane molecular mass cut-off (MMCO) (from 150 to 300 kg·mol -1 ), operating conditions (physico-chemistry, hydrodynamics) and operation mode for achieving satisfactory performance. Irreversible membrane fouling, mainly due to b-lactoblobulin (b-LG), the major protein of the feed solution, and physico-chemical characteristics of the whey protein sources (initial a-LA purity and concentration; heat denaturation of proteins) were shown as selection parameters of prime importance with regard to the target of the prepurification step. Whey protein concentrate in liquid form (PS 90) was to be preferred versus the same grade in powder form and the less concentrated liquid (PS 75). By processing that liquid PS 90, a-LA purity in the permeate was increased from around 0.25 in the initial feed to around 0.44 with a yield of around 0.53 with Céram membranes of MMCO of 300 kg·mol -1 . Stationary ultrafiltration flux was around 64 L·h -1 ·m -2 at a volume reduction ratio of 9.a-lactalbumin / whey / purity / ultrafiltration Résumé -Pré-purification de l'a-lactalbumine par ultrafiltration de lactosérum acide sur membrane céramique : étude des conditions opératoires. La production d'a-lactalbumine (a-LA) de pureté élevée peut se faire par une cascade de 2 opérations, dont la première, présentée ici, est une étape de pré-purification. Il s'agit d'un fractionnement par ultrafiltration d'un lactosérum de caséine acide afin d'obtenir une pureté en a-LA améliorée dans le filtrat en retenant totalement la sérum-albumine bovine et les immunoglobulines. Le présent travail débouche sur un recueil de recommandations qui inclut le choix du seuil de coupure de la membrane, des conditions physicochimiques et hydrodynamiques et du mode de conduite pour obtenir des performances satisfaisantes. Le colmatage irréversible de la membrane et les caractéristiques physico-chimiques de la source de protéines de lactosérum (pureté et concentration initiale en a-LA ; dénaturation des * Correspondence and reprints

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“…The results were in good agreement with the literature data for individual whey proteins, which show salting out effect at pH < 5.0 [25] and denaturation at pH > 8.0 [45].…”

Section: Resultssupporting

confidence: 82%

Prepurification of ?-lactalbumin with ultrafiltration ceramic membranes from acid casein whey: study of operating conditions

Muller

Chaufer

Merin

et al. 2003

Lait

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“…Protein purification ␤-Lactoglobulin AB (␤-Lg) was fractionated from the whey powder according to a slight modification of the method of Mailliart and Ribadeau-Dumas (1988) as described earlier (Haque & Sharma, 1997). The fraction thus prepared was apparently pure by alkaline-urea-polyacrylamide gel electrophoresis (Haque & Sharma, 1997) and was not subjected to gel permeation or size exclusion chromatography for further purification as was done in an earlier experiment to remove tenaciously bound trace impurities that absorb at 280 nm (Sharma et al, 1996).…”

Section: Methodsmentioning

confidence: 99%

Influence of Cation Sequestering and pH on Quiescent Thermal Association of .BETA.-Lacto-globulin NB from Fresh Cheddar Whey: An Insight into Gelation Mechanism.

Haque

Sharma

2002

FSTR

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Freshly fractionated ␤-lactoglobulin AB (␤-Lg) from Cheddar whey was dispersed at pH 3.5, 7, and 9 buffers containing 20 mM EDTA, and circulated at 25˚C through a closed loop containing a 200 nm pore size membrane, to remove traces of dust and large aggregates, and an water jacketed cuvette placed within a Dynamic Light Scattering (DLS) device for real-time data acquisition. Filtered samples were step-wise heated from 25˚C to 90˚C with continuous data acquisition to study dynamic changes in mean aggregate diameter (MAD). Data were analyzed by cumulant method for apparent MAD and CONTIN for size distribution. Initial MAD (IMAD) of about 200 nm, reflecting the pore size of the filter used, was observed for all experiments prior to heating. Mid-range aggregate, Agg3 (100-599 nm), was ubiquitous in all distributions and Agg1 (monomer-dimer) was only seen at pH 7 and 25˚C. Increased temperatures gave rise to larger aggregates (>micron) (Agg4 and 5) with concomitant disappearance of Agg3. The greatest increase in MAD was at pH 3.5 and the lowest was at pH 9. Pre-gelation (<70˚C) kinetic rates were 4.29, 1.53, and -0.11¥ ¥ ¥ ¥10 -4 s -1 for pH 3.5, 7.0, and 9.0, respectively, giving MADs that were 3.5, 2.2 and 0.8 fold compared to IMAD. Above 70˚C (apparent gelation range), relative aggregate enlargement was greatest at pH 3.5 being 55, 21, and 4.2 fold of IMAD, respectively, for pH 3.5, 7, and 9 at 90˚C. An apparent gel formed at pH 3.5 and a turbid gel/coagulum formed at pH 7 and none at pH 9. It is conceivable that increased association at pre-gelation temperatures is required for gelation. A mechanism has been postulated.

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“…(3-Lactoglobulin (a mixture of variants A and B) was purchased from Laiteries Triballat (NoyaINilaine, France) and purified according to the procedure of Mailliart and Ribadeau Dumas (1988). Ali other chemicals were reagent grade.…”

Section: Methodsmentioning

confidence: 99%

Functional properties of β-lactoglobulin phosphorylated in the presence of different aliphatic amines

Sitohy

Chobert

Popineau

et al. 1995

Lait

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Summary -Phosphorylation of~-Iactoglobulin was carried out with 20, 40 and 80 mol POCI:!mol protein in the presence of different aliphatic amines. The physicochemical properties of the modified proteins changed according to the nature of amine (tertiary or primary; shorter or longer aliphatic chain). The use of butylamine during the phosphorylation of~-Iactoglobulin with POCI 3 resulted in a low phosphorylation yield (2-4 mol P/mol protein), conferring, however, excellent foaming and emulsifying properties to the phosphobutylated protein. The use of longer aliphatic primary amines (8-12 C) as bases and nucleophiles du ring the phosphorylation of~-Iactoglobulin gave rise to low phosphorylation, reduced solubility, poor foaming and emulsifying properties. {3-lactoglobuline / phosphorylation / amine aliphatique / propriétés fonctionnelles• On a

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Preparation of β‐Lactoglobulin and p‐Lactoglobulin‐Free Proteins from Whey Retentate by NaCI Salting Out at Low pH

Cited by 173 publications

References 7 publications

Prepurification of ?-lactalbumin with ultrafiltration ceramic membranes from acid casein whey: study of operating conditions

Prepurification of ?-lactalbumin with ultrafiltration ceramic membranes from acid casein whey: study of operating conditions

Influence of Cation Sequestering and pH on Quiescent Thermal Association of .BETA.-Lacto-globulin NB from Fresh Cheddar Whey: An Insight into Gelation Mechanism.

Functional properties of β-lactoglobulin phosphorylated in the presence of different aliphatic amines

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