Simultaneous anion and cation exchange chromatography of whey proteins using a customizable mixed matrix membrane

Saufi, Syed M.; Fee, Conan J.

doi:10.1016/j.chroma.2011.09.045

Cited by 31 publications

(21 citation statements)

References 27 publications

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“…Different types of HPLC methods are also well developed for milk protein detection. Reversed‐phase , size exclusion , and ion‐exchange chromatography coupled to diode array detection or to MS detection are applied for whey proteins identification and characterization.…”

Section: Introductionmentioning

confidence: 99%

Analysis of major milk whey proteins by immunoaffinity capillary electrophoresis coupled with MALDI‐MS

Gasilova

Gassner

2012

Electrophoresis

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Two major milk whey proteins, ␤-lactoglobulin and ␣-lactalbumin, are among the main cow milk allergens and can cause allergy even at a very low concentrations. Therefore, these proteins are interesting targets in food analysis, not only for food quality control but also for highlighting the presence of allergens. Herein, a sensitive analysis for ␤-lactoglobulin and ␣-lactalbumin was developed using immunoaffinity capillary electrophoresis hyphenated with MALDI-MS. Magnetic beads functionalized with appropriate antibodies were used for ␤-lactoglobulin and ␣-lactalbumin immunocapture inside the capillary. After elution from the beads, analyte focusing and separation were performed by transient isotachophoresis followed by MALDI-MS analysis performed through an automated iontophoretic fraction collection interface. A LOD in the low nanomolar range was attained for both whey proteins. The method developed was further applied to the analysis of different milk samples including fortified soy milk.

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Section: Introductionmentioning

confidence: 99%

Analysis of major milk whey proteins by immunoaffinity capillary electrophoresis coupled with MALDI‐MS

Gasilova

Gassner

2012

Electrophoresis

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“…Historically, conventional particle packed-bed chromatography has occupied an important position in the biopharmaceutical industry. In recent years, membrane chromatography has become a promising alternative to conventional resin chromatography for the separation and purification of proteins due to its low pressure drop, the elimination of pores with long diffusive path lengths, and the ease of packing and scale-up [1][2][3]. In this technology, the membrane plays an important role in the achievement of highperformance separation.…”

Section: Introductionmentioning

confidence: 99%

Preparation of high-capacity strong cation exchange membrane for protein adsorption via surface-initiated atom transfer radical polymerization

Wei

Wang

2013

Journal of Membrane Science

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“…25,26 Hydroxy groups on EVAL chains increase the wettability and reduce the non-selective and irreversible adsorption of biomolecules, especially in protein separation. 27,28 The P(DMAEMA)grafted EVAL membrane was firstly prepared via UV-grafting method by our previous work, 29 and the pH-responsive adsorption of model protein BSA was also studied. 30 However, the separation property of protein from mixture by the membrane has not yet been reported.…”

Section: Introductionmentioning

confidence: 99%

Similarly sized protein separation of charge‐selective ethylene‐vinyl alcohol copolymer membrane by grafting dimethylaminoethyl methacrylate

Huang

et al. 2018

J of Applied Polymer Sci

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Similarly sized protein separation was investigated using a charge‐selective membrane, which prepared by grafting dimethylaminoethyl methacrylate (DMAEMA) onto ethylene vinyl alcohol copolymer (EVAL) membrane. Bovine serum albumin (BSA) and bovine hemoglobin (BHb) was used as model proteins. P(DMAEMA), the weak cationic polyelectrolyte with ionizable tertiary amine groups, contributed to the charge‐selective separation for BSA and BHb. At pH 6.0, the grafted EVAL membrane surface was positively charged and BSA was negatively charged, while BHb was positively charged. The BSA was adsorbed onto the membrane surface due to electrostatic interaction and the BHb passed through the membrane into the permeate. The charge‐selective behavior resulted in the separation of the similarly sized protein. The maximum separation factors of static adsorption separation for model protein and binary mixture were 32.4 and 37.2, respectively. In the dynamic separation process, the maximum separation factor value was 6.2. © 2018 Wiley Periodicals, Inc. J. Appl. Polym. Sci. 2018, 135, 46374.

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Simultaneous anion and cation exchange chromatography of whey proteins using a customizable mixed matrix membrane

Cited by 31 publications

References 27 publications

Analysis of major milk whey proteins by immunoaffinity capillary electrophoresis coupled with MALDI‐MS

Analysis of major milk whey proteins by immunoaffinity capillary electrophoresis coupled with MALDI‐MS

Preparation of high-capacity strong cation exchange membrane for protein adsorption via surface-initiated atom transfer radical polymerization

Similarly sized protein separation of charge‐selective ethylene‐vinyl alcohol copolymer membrane by grafting dimethylaminoethyl methacrylate

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