Electrostatic effects on protein adsorption were investigated using differential scanning calorimetry (DSC) and adsorption isotherms. The thermal denaturation of lysozyme, ribonuclease A (RNase), and Ξ±-lactalbumin in solution and adsorbed onto silica nanoparticles was examined at three concentration
Electrostatic Effect on the Hydration Layer of Colloidal Silica Particles
β Scribed by Shigeo Sasaki; Hiroshi Maeda
- Publisher
- Elsevier Science
- Year
- 1994
- Tongue
- English
- Weight
- 192 KB
- Volume
- 167
- Category
- Article
- ISSN
- 0021-9797
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β¦ Synopsis
The hydrodynamic radii of colloidal silica particles in the aqueous solutions were measured under various conditions of (\mathrm{pH}) and salt concentration by means of the dynamic light scattering technique. In the salt free solutions the observed hydrodynamic radius increased by (1 \mathrm{~nm}) from (13 \mathrm{~nm}) at (\mathrm{pH}) below 8 to (14 \mathrm{~nm}) at (\mathrm{pH}) above 9 according to the ionization of silanol groups. At pH above 9 , the radius decreased from (14 \mathrm{~nm}) in salt free solutions to (13 \mathrm{~nm}) at the salt concentration of (10^{-2} M). These results suggest that the strong electrostatic electric field makes the hydration layer on the surface of a silica particle thicker. 1994 Academic Press, Inc.
π SIMILAR VOLUMES
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