Osmotic second virial cross-coefficient measurements for binary combination of lysozyme, ovalbumin, and alpha-amylase in salt solutions

Mehta, Chirag M., White, Edward T. and Litster, James D. (2013) Osmotic second virial cross-coefficient measurements for binary combination of lysozyme, ovalbumin, and alpha-amylase in salt solutions. Biotechnology Progress, 29 5: 1203-1211. doi:10.1002/btpr.1760

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Author Mehta, Chirag M.
White, Edward T.
Litster, James D.
Title Osmotic second virial cross-coefficient measurements for binary combination of lysozyme, ovalbumin, and alpha-amylase in salt solutions
Formatted title
Osmotic second virial cross-coefficient measurements for binary combination of lysozyme, ovalbumin, and α-amylase in salt solutions
Journal name Biotechnology Progress   Check publisher's open access policy
ISSN 8756-7938
1520-6033
Publication date 2013-09
Sub-type Article (original research)
DOI 10.1002/btpr.1760
Volume 29
Issue 5
Start page 1203
End page 1211
Total pages 9
Place of publication Hoboken, NJ, United States
Publisher Wiley-Blackwell Publishing
Collection year 2014
Language eng
Formatted abstract
Interactions measurement is a valuable tool to predict equilibrium phase separation of a desired protein in the presence of unwanted macromolecules. In this study, cross-interactions were measured as the osmotic second virial cross-coefficients (B23) for the three binary protein systems involving lysozyme, ovalbumin, and α-amylase in salt solutions (sodium chloride and ammonium sulfate). They were correlated with solubility for the binary protein mixtures. The cross-interaction behavior at different salt concentrations was interpreted by either electrostatic or hydrophobic interaction forces. At low salt concentrations, the protein surface charge dominates cross-interaction behavior as a function of pH. With added ovalbumin, the lysozyme solubility decreased linearly at low salt concentration in sodium chloride and increased at high salt concentration in ammonium sulfate. The B23 value was found to be proportional to the slope of the lysozyme solubility against ovalbumin concentration and the correlation was explained by preferential interaction theory.
Keyword Osmotic second virial cross-coefficient
Cross-interactions
Binary protein mixtures
Protein solubility in mixture
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: School of Chemical Engineering Publications
Official 2014 Collection
Advanced Water Management Centre Publications
 
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Created: Tue, 10 Dec 2013, 12:06:55 EST by Mr Chirag Mehta on behalf of Advanced Water Management Centre