scholarly journals A comparison of the activation energy of viscous flow for hen egg-white lysozyme obtained on the basis of different models of viscosity for glass-forming liquids

2011 ◽  
Vol 34 (1) ◽  
pp. 1-9 ◽  
Author(s):  
Karol Monkos

A comparison of the activation energy of viscous flow for hen egg-white lysozyme obtained on the basis of different models of viscosity for glass-forming liquids The paper presents the results of viscosity determinations on aqueous solutions of hen egg-white lysozyme at a wide range of concentrations and at temperatures ranging from 5°C to 55°C. On the basis of these measurements and different models of viscosity for glass-forming liquids, the activation energy of viscous flow for solutions and the studied protein, at different temperatures, was calculated. The analysis of the results obtained shows that the activation energy monotonically decreases with increasing temperature both for solutions and the studied protein. The numerical values of the activation energy for lysozyme, calculated on the basis of discussed models, are very similar in the range of temperatures from 5°C to 35°C.

2015 ◽  
Vol 37 (1) ◽  
pp. 63-70
Author(s):  
Karol Monkos

The paper presents the results of viscosity determinations on aqueous solutions of hen egg-white lysozyme, bovine ß-lactoglobulin, human and porcine immunoglobulin IgG at a wide range of concentrations and at temperatures ranging from 5oC to 55oC. Viscosity-temperature dependence of the proteins solutions is analyzed based on a formula resulting from the Avramov's model. One of the parameters in the Avramov's equation is the glass transition temperature Tg. It turns out that for all studied proteins, the Tg of the solution increases with increasing concentration. To determine the glass transition temperature of the dry protein Tg,p, a modified form of the Gordon-Taylor equation is used. This equation gives the relationship between Tg and the concentration of the solution, and Tg,p and a parameter dependent on the strength of protein-solvent interaction are fitting parameters. Thus determined the glass transition temperature for the studied dry proteins is in the range from 227.3 K (for bovine ß-lactoglobulin) to 260.6 K (for hen egg-white lysozyme).


1997 ◽  
Vol 94 ◽  
pp. 356-364 ◽  
Author(s):  
M Faraggi ◽  
E Bettelheim ◽  
M Weinstein

2021 ◽  
pp. 138830
Author(s):  
Baoliang Ma ◽  
Haohao Wang ◽  
Yujie Liu ◽  
Fang Wu ◽  
Xudong Zhu

2015 ◽  
Vol 44 (22) ◽  
pp. 10392-10398 ◽  
Author(s):  
Daniela Marasco ◽  
Luigi Messori ◽  
Tiziano Marzo ◽  
Antonello Merlino

The model protein hen egg white lysozyme was challenged with oxaliplatin and cisplatin.


Sign in / Sign up

Export Citation Format

Share Document