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Published: October 27, 2011 r 2011 American Chemical Society 4849 dx.doi.org/10.1021/je200807y |J. Chem. Eng. Data 2011, 56, 48494852
 

Summary: Published: October 27, 2011
r 2011 American Chemical Society 4849 dx.doi.org/10.1021/je200807y |J. Chem. Eng. Data 2011, 56, 4849­4852
ARTICLE
pubs.acs.org/jced
Effect of Lysozyme Proteins on the Mutual-Diffusion Coefficient of
Sodium Chloride in Water
Onofrio Annunziata,* Daniela Buzatu,
and John G. Albright
Department of Chemistry, Texas Christian University, Fort Worth, Texas 76129, United States
ABSTRACT: We measured accurate NaCl main-term diffusion coefficients in aqueous lysozyme solutions at 25 °C and pH 4.5
using the Gosting diffusiometer operated in its Rayleigh interferometric optical mode. The dependence of this diffusion coefficient
on lysozyme concentration was examined using the obstruction-effect theory. Agreement between experimental results and theory is
achieved if lysozyme proteins are treated as hydrated spheres with a hydration number of 240, a value that is comparable with those
reported in literature for this protein. Electrostatic interactions and common-ion effects due to lysozyme net charge at pH 4.5 do
not contribute significantly to the behavior of the NaCl diffusion coefficient within our experimental range of salt concentrations
[(0.25 to 0.90) mol 3 dmĀ3
].
' INTRODUCTION
In a binary liquid mixture, mutual diffusion coefficients
characterize the motion of solute and solvent molecules relative

  

Source: Annunziata, Onofrio - Department of Chemistry, Texas Christian University

 

Collections: Chemistry