Details
| Original language | English |
|---|---|
| Pages (from-to) | 217-225 |
| Number of pages | 9 |
| Journal | Colloids and Surfaces B: Biointerfaces |
| Volume | 87 |
| Issue number | 2 |
| Publication status | Published - 19 May 2011 |
Abstract
In this study, the potential use of a synthetic Mg/Al hydrotalcite (layered double hydroxide) as a novel chromatography material for protein purification was investigated. The hydrotalcite is present in its carbonate form and is characterized by an Al/Mg-ratio of 1.85. Zetapotential measurements confirm a positive surface potential up to pH 10 suggesting applicability as anion exchanger. The binding of model proteins covering a broad range of isoelectric points and molecular weights was performed at different pH-values under batch conditions to evaluate the binding behaviour of the hydrotalcite. Furthermore, static binding capacities were exemplarily determined for hemoglobin and human serum albumin. Additionally, the adsorption and elution of hemoglobin was studied under dynamic conditions. The binding behaviour of the hydrotalcite was compared to commercially available anion exchangers and was found to be a function of pH, depending on the model protein. Variant adsorption behaviour is explained by further interactions like hydrogen bonds and by an unequal charge distribution over the protein surfaces. The hydrotalcite reveals high adsorption capacities under static (260. mg/g) as well as under dynamic conditions (88. mg/g at 34. cm/h; 61. mg/g at 340. cm/h). With appropriate buffers like 500. mM carbonate (pH 10) the adsorbed proteins can be nearly completely desorbed making regeneration possible. Due to the binding and elution properties it is concluded, that the hydrotalcite can serve anion exchange material for chromatographic protein separations.
Keywords
- Chromatography, Hydrotalcite, Layered double hydroxide, Protein adsorption, Separation
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
- Biotechnology
- Physics and Astronomy(all)
- Surfaces and Interfaces
- Chemistry(all)
- Physical and Theoretical Chemistry
- Chemical Engineering(all)
- Colloid and Surface Chemistry
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In: Colloids and Surfaces B: Biointerfaces, Vol. 87, No. 2, 19.05.2011, p. 217-225.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - Adsorption and separation of proteins by a synthetic hydrotalcite
AU - Ralla, Kathrin
AU - Sohling, Ulrich
AU - Suck, Kirstin
AU - Sander, Friederike
AU - Kasper, Cornelia
AU - Ruf, Friedrich
AU - Scheper, Thomas
N1 - Funding information: The data in this work were partly performed in the scope of the BMBF project BIOCATALYSIS 2021 P7/P8. The authors thank the BMBF for financial support as well as Dr. habil. Lars Dähne (Surflay Nanotec GmbH, Berlin, Germany) for kindly performing zeta potential measurements.
PY - 2011/5/19
Y1 - 2011/5/19
N2 - In this study, the potential use of a synthetic Mg/Al hydrotalcite (layered double hydroxide) as a novel chromatography material for protein purification was investigated. The hydrotalcite is present in its carbonate form and is characterized by an Al/Mg-ratio of 1.85. Zetapotential measurements confirm a positive surface potential up to pH 10 suggesting applicability as anion exchanger. The binding of model proteins covering a broad range of isoelectric points and molecular weights was performed at different pH-values under batch conditions to evaluate the binding behaviour of the hydrotalcite. Furthermore, static binding capacities were exemplarily determined for hemoglobin and human serum albumin. Additionally, the adsorption and elution of hemoglobin was studied under dynamic conditions. The binding behaviour of the hydrotalcite was compared to commercially available anion exchangers and was found to be a function of pH, depending on the model protein. Variant adsorption behaviour is explained by further interactions like hydrogen bonds and by an unequal charge distribution over the protein surfaces. The hydrotalcite reveals high adsorption capacities under static (260. mg/g) as well as under dynamic conditions (88. mg/g at 34. cm/h; 61. mg/g at 340. cm/h). With appropriate buffers like 500. mM carbonate (pH 10) the adsorbed proteins can be nearly completely desorbed making regeneration possible. Due to the binding and elution properties it is concluded, that the hydrotalcite can serve anion exchange material for chromatographic protein separations.
AB - In this study, the potential use of a synthetic Mg/Al hydrotalcite (layered double hydroxide) as a novel chromatography material for protein purification was investigated. The hydrotalcite is present in its carbonate form and is characterized by an Al/Mg-ratio of 1.85. Zetapotential measurements confirm a positive surface potential up to pH 10 suggesting applicability as anion exchanger. The binding of model proteins covering a broad range of isoelectric points and molecular weights was performed at different pH-values under batch conditions to evaluate the binding behaviour of the hydrotalcite. Furthermore, static binding capacities were exemplarily determined for hemoglobin and human serum albumin. Additionally, the adsorption and elution of hemoglobin was studied under dynamic conditions. The binding behaviour of the hydrotalcite was compared to commercially available anion exchangers and was found to be a function of pH, depending on the model protein. Variant adsorption behaviour is explained by further interactions like hydrogen bonds and by an unequal charge distribution over the protein surfaces. The hydrotalcite reveals high adsorption capacities under static (260. mg/g) as well as under dynamic conditions (88. mg/g at 34. cm/h; 61. mg/g at 340. cm/h). With appropriate buffers like 500. mM carbonate (pH 10) the adsorbed proteins can be nearly completely desorbed making regeneration possible. Due to the binding and elution properties it is concluded, that the hydrotalcite can serve anion exchange material for chromatographic protein separations.
KW - Chromatography
KW - Hydrotalcite
KW - Layered double hydroxide
KW - Protein adsorption
KW - Separation
UR - http://www.scopus.com/inward/record.url?scp=79960385337&partnerID=8YFLogxK
U2 - 10.1016/j.colsurfb.2011.05.021
DO - 10.1016/j.colsurfb.2011.05.021
M3 - Article
C2 - 21684727
AN - SCOPUS:79960385337
VL - 87
SP - 217
EP - 225
JO - Colloids and Surfaces B: Biointerfaces
JF - Colloids and Surfaces B: Biointerfaces
SN - 0927-7765
IS - 2
ER -