Effect of other protein on the solubility of hen egg white lysozyme

Mehta, Chirag M., White, Edward T., Litster, James D., Hardin, Matthew T. and Lenhoff, Abraham (2007). Effect of other protein on the solubility of hen egg white lysozyme. In: AIChE Conference Proceedings. 2007 AIChE Annual Meeting, Salt Lake City, United States, (). 4-9 November 2007.

Attached Files (Some files may be inaccessible until you login with your UQ eSpace credentials)
Name Description MIMEType Size Downloads
UQ231083_other.pdf UQ231083_other.pdf application/pdf 174.09KB 0
Author Mehta, Chirag M.
White, Edward T.
Litster, James D.
Hardin, Matthew T.
Lenhoff, Abraham
Title of paper Effect of other protein on the solubility of hen egg white lysozyme
Conference name 2007 AIChE Annual Meeting
Conference location Salt Lake City, United States
Conference dates 4-9 November 2007
Proceedings title AIChE Conference Proceedings
Journal name AIChE Annual Meeting, Conference Proceedings
Place of Publication New York , NY, United States
Publisher Omnipress
Publication Year 2007
Sub-type Fully published paper
ISBN 978-081691022-9
Total pages 7
Language eng
Formatted Abstract/Summary
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 20°C. 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 [1]. 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 (B 23) with the solubility of lysozyme in a binary mixture.
Q-Index Code E1
Q-Index Status Provisional Code
Institutional Status UQ

Version Filter Type
Citation counts: Scopus Citation Count Cited 0 times in Scopus Article
Google Scholar Search Google Scholar
Created: Thu, 03 Mar 2011, 16:40:02 EST by Mr Chirag Mehta on behalf of Advanced Water Management Centre