(506e) Effect of Other Protein on the Solubility of Hen Egg White Lysozyme | AIChE

(506e) Effect of Other Protein on the Solubility of Hen Egg White Lysozyme

Authors 

Mehta, C. M. - Presenter, The University of Queensland
White, E. T. - Presenter, The University of Queensland
Lenhoff, A. - Presenter, Department of Chemical Engineering
Hardin, M. T. - Presenter, University of Queensland

Protein
separation and characterisation are crucial challenges faced by industrial
biologists and engineers working with proteins. The key aim is to extract the
valuable protein from a broth containing a mixture of proteins in the most
efficient and economic way. In
this work salt precipitation (crystallisation) has been investigated as a
purification technique for a binary protein mixture. For the bulk recovery of a
valuable protein, a thorough understanding of the interactive effect of another
protein on the solubility of the desired protein in a mixture is essential for
successful crystallisation.

 

Tetragonal crystals of lysozyme
were used to estimate the solubilities in the pH range 4.0 to 5.4 in salt
concentrations from 0.2 to 0.5 M at 20oC. To estimate the effect of
other protein, lysozyme solubilities were also measured in presence of
ovalbumin. A steep drop in solubility was observed in presence of ovalbumin in
pH range 4 to 4.5 at low salt concentration (< 0.3 M). Formation of
ovalbumin-lysozyme complexes were also observed at pH 4 in low salt
concentration. Minimum effect on lysozyme solubility was observed at high pH
(> 5.0) and salt concentration (> 0.3 M). To estimate the interaction
between lysozyme and ovalbumin in salt solutions cross interaction
chromatography (CIC) was used. Strong cross interaction was observed at low
salt concentration (< 0.3 M). This work shows the effect of ovalbumin on
lysozyme solubility and correlates the second virial cross coefficient (B23)
with the solubility of lysozyme in a binary mixture.

 

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