Dispersion-enhanced chromatography refolding of denatured protein

Ding, Yong; He, Li; Middelberg, Anton P. J.

doi:10.1016/j.ces.2008.05.034

Cited by 7 publications

(4 citation statements)

References 30 publications

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“…Secondly, lateral repulsion within the plane of the interface due to high repulsive charge might be expected to limit the extent of surface coverage. This has been evidenced in our other work using an anionic peptide surfactant Lac21E . The peptide Lac21E (Ac‐MEELADS LEELARQ VEELESA‐NH 2 ) has a high negative charge at neutral pH 7 (−6.9).…”

Section: Resultsmentioning

confidence: 99%

“…Lac21E has shown capable of being reversibly switched by pH change to give rapid and large changes in interfacial tension. At pH 3, Lac21E with a positive charge of +2.3 gave an interfacial tension of 43 m n m −1 , while addition of NaOH to adjust the pH to 7.4 resulted in a rapid increase in interfacial tension to 69 m n m −1 because of the desorption from the interface . The structure of the interfacial Lac21E film was determined using neutron reflectometry, and the corresponding volume fractions at the interface were determined to be 17 and 70 % at pH 7 and pH 3, respectively, indicating the high interfacial tension resulting from the less adsorption of Lac21E peptide at the interface at pH 7 because of its high negative charge.…”

Section: Resultsmentioning

confidence: 99%

See 1 more Smart Citation

From Folding to Function: Design of a New Switchable Biosurfactant Protein

Zhao

Dwyer

et al. 2017

ChemPhysChem

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A new anionic biosurfactant protein (SP16) capable of tuning foaming behaviour by pH or salt has been designed. This biosurfactant exhibits unique foaming behaviour with high sensitivity to pH. A good level of foaming was observed at pH 2 but not at pH 3. A further increase by one pH unit to pH 4 restored good foaming. At pH 5-8, SP16 again showed low foaming propensity, whereas the presence of salt (NaCl) was able to restore foaming again. Interfacial tension and circular dichroism investigations revealed the foaming control mechanism. The high negative charge (-16.6) at pH 6 and above restricted the ability of SP16 to fold into an α-helical conformation and also restricted surface activity. For pH 5 (-13.6), even though SP16 folds in bulk to give α-helical structure, the high charge inhibited adsorption at the air-water interface, resulting in a significant lag time of about 150-200 sec to achieve a decrease in interfacial tension. In contrast to its low foaming behaviour at pH 5-8, the presence of salt (NaCl) was found to effectively screen negative charge, thus leading to its folding and a decrease of interfacial tension. This new design offers a new strategy to control foaming behaviour, and elaborates a clear link between charge, structure and interfacial activity for biosurfactants.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

From Folding to Function: Design of a New Switchable Biosurfactant Protein

Zhao

Dwyer

et al. 2017

ChemPhysChem

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“…During SEC refolding this dilution factor has been estimated to be on the area of 40-120 fold (Gu et al, 2001;Park et al, 2005). Furthermore, high dilution has been linked to an increase on the SEC batch refolding yield (Ding et al, 2008). In contrast, during the SMBSECR operation such large dilution does not occur.…”

Section: Comparison Between Sec Batch Refolding and Smbsec Refoldingmentioning

confidence: 97%

Size-exclusion simulated moving bed chromatographic protein refolding

Freydell¹,

Bulsink²,

Hateren³

et al. 2010

Chemical Engineering Science

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“…When target proteins are obtained from E. coli , a protein renaturing step is typically required before subjecting the target proteins to several LC steps for further purification. Protein folding liquid chromatography (PFLC) is well known as a powerful tool for renaturation with the simultaneous purification of these recombinant proteins, which has greatly accelerated the purification processes of recombinant proteins and protein drugs .…”

Section: Introductionmentioning

confidence: 99%

Fast separations of intact proteins by liquid chromatography

Wang

Min

Geng

2012

J of Separation Science

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Scientists working in many fields require fast separations of intact proteins using liquid chromatography. The fast separations here concern not only the separation step alone but also the complete chromatographic process, including column regeneration, system equilibration, and buffer exchange, in one- and two-dimensional liquid chromatography in addition to fast purification technologies predominantly on the analytical scale with some unique examples on the preparative and industrial scales. This comprehensive review discusses recent developments in methodologies, packing materials, column techniques, and purification technologies in the field of rapid liquid chromatography of intact proteins. Some typical examples are summarized in the tables.

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Dispersion-enhanced chromatography refolding of denatured protein

Cited by 7 publications

References 30 publications

From Folding to Function: Design of a New Switchable Biosurfactant Protein

From Folding to Function: Design of a New Switchable Biosurfactant Protein

Size-exclusion simulated moving bed chromatographic protein refolding

Fast separations of intact proteins by liquid chromatography

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