Adsorption equilibrium of proteins on a dye-ligand adsorbent

“…It has been well known that aqueous phase ionic strength strongly affects the adsorption equilibrium of proteins to Ž . Cibacron Blue 3GA CB modified agarose gel, leading to Ž the decrease of protein adsorption Boyer and Hsu, 1990;He . et al, 1997 .…”

Section: Introductionmentioning

confidence: 99%

Ionic strength dependence of protein adsorption to dye‐ligand adsorbents

Zhang

Sun

2002

AIChE Journal

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“…It has been shown that proteins have no The albumin-adsorption capacities of the Cibanet charge at their isoelectric points, and, therecron Blue F3GA-Zn(II)-attached poly(HEMA) fore, the maximum adsorption from aqueous solumembranes containing different amounts of tions is usually observed at their isolectric Zn(II) [between 0.65 and 1.44 g Zn(II)/m 2 ] were point. 26,27 The maximum adsorption was observed investigated at pH 5.0. The initial concentration of BSA in the incubation solution was 3.0 mg/mL.…”

Section: Resultsmentioning

confidence: 97%

New metal chelate sorbent for albumin adsorption: Cibacron Blue F3GA-Zn(II) attached microporous poly(HEMA) membranes

Deni̇zli̇

Salih

Şenel

et al. 1998

J. Appl. Polym. Sci.

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Poly(2-hydroxyethyl methacrylate) [poly(HEMA)] membranes were prepared by UV-initiated photopolymerization of HEMA in the presence of an initiator (a-a-azobis-isobutyronitrile, AIBN). The triazine dye Cibacron Blue F3GA was attached as an affinity ligand to poly(HEMA) membranes, covalently. These affinity membranes with a swelling ratio of 58% and containing 10.7 mmol Cibacron Blue F3GA/m 2 were used in the albumin adsorption studies. After dye-attachment, Zn(II) ions were chelated within the membranes via attached-dye molecules. Different amounts of Zn(II) ions [650-1440 mg Zn(II)/m 2 ] were loaded on the membranes by changing the initial concentration of Zn(II) ions and pH. Bovine serum albumin (BSA) adsorption on these membranes from aqueous solutions containing different amounts of BSA at different pH was investigated in batch reactors. The nonspecific adsorption of BSA on the poly(HEMA) membranes was negligible. Cibacron Blue F3GA attachment significantly increased the BSA adsorption up to 92.1 mg BSA/m 2 . Adsorption capacity was further increased when Zn(II) ions were attached (up to 144.8 mg BSA m 2 ). More than 90% of the adsorbed BSA was desorbed in 1 h in the desorption medium containing 0.5M NaSCN at pH 8.0 and 0.025M EDTA at pH 4.9.

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“…Many publications have demonstrated that the affinity of CB or other reactive dyes to proteins would decrease by increasing ionic strength (Boyer and Hsu, 1990;Herak and Merrill, 1989;He et al, 1997). Thus we investigated the effect of ionic strength on lysozyme extraction to find a proper ionic strength for back extraction.…”

Section: Effect Of Ionic Strengthmentioning

confidence: 97%

“…In both cases with and without CB, the extraction yield increased with increasing pH at pH <10 for lysozyme or pH <9.15 for cytochrome c. Because CB had no binding ability to cytochrome c and pH had little effect on CB-lysozyme binding (Boyer and Hsu, 1990), it was considered that the change of lysozyme or cytochrome c extraction with pH was primarily attributed to the electrostatic interactions between the proteins and the reversed micelles. As stated above, the crude lecithin consisted of many other lipids besides phosphatidylcholine and phosphatidylethanolamine.…”

Section: Effect Of Ph and Temperaturementioning

confidence: 98%

Affinity extraction of proteins with a reversed micellar system composed of Cibacron Blue-modified lecithin

Sun

Ichikawa

Sugiura

et al. 1998

Biotechnol. Bioeng.

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Crude soybean lecithin was used as a novel surfactant to form reversed micelles in n‐hexane. Cibacron Blue F‐3GA (CB) was directly immobilized to the reversed micelles by a two‐phase reaction. The reversed micellar system without CB showed low solubilizing capacity for low molecular weight proteins, lysozyme, and cytochrome c due to the weak electrostatic interactions. The introduction of CB significantly increased the solubilization of lysozyme because of its affinity binding to CB but showed no effect on the solubilization of cytochrome c since it did not bind to CB. Although bovine serum albumin had an affinity for CB, it was not extracted to the reversed micelles containing CB because its high molecular weight resulted in a significant steric hindrance effect. Thus the reversed micellar system had a high selectivity resulting from both biospecific and steric hindrance effects. The extraction yield of lysozyme decreased significantly with increasing ionic strength. Therefore, the back extraction of lysozyme was carried out using a stripping solution with an ionic strength of 0.865 mol/L. The overall recovery yield of lysozyme after back extraction could be increased to 87% by stripping for 2 h. The recovered lysozyme exhibited an activity equivalent to native lysozyme, and its secondary structure was also unchanged. © 1998 John Wiley & Sons, Inc. Biotechnol Bioeng 58:58–64, 1998.

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Adsorption equilibrium of proteins on a dye-ligand adsorbent

Cited by 34 publications

References 8 publications

Ionic strength dependence of protein adsorption to dye‐ligand adsorbents

Ionic strength dependence of protein adsorption to dye‐ligand adsorbents

New metal chelate sorbent for albumin adsorption: Cibacron Blue F3GA-Zn(II) attached microporous poly(HEMA) membranes

Affinity extraction of proteins with a reversed micellar system composed of Cibacron Blue-modified lecithin

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