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The interaction of bovine serum albumin (BSA) with sulfated, carboxylated, and pyridinium-grafted cellulose nanocrystals (CNCs) was studied as a function of the degree of substitution by determining the adsorption isotherm and by directly measuring the thermodynamics of interaction. The adsorption of BSA onto positively charged pyridinium-grafted cellulose nanocrystals followed Langmuirian adsorption with the maximum amount of adsorbed protein increasing linearly with increasing degree of substitution. The binding mechanism between the positively charged pyridinum-grafted cellulose nanocrystals and BSA was found to be endothermic and based on charge neutralization. A positive entropy of adsorption associated with an increase of the degree of disorder upon addition of BSA compensated for the unfavorable endothermic enthalpy and enabled formation of pyridinium–g–CNC–BSA complexes. The …
American Chemical Society
Publication date: 
6 Jun 2017

Salvatore Lombardo, Samuel Eyley, Christina Schütz, Hans Van Gorp, Sabine Rosenfeldt, Guy Van den Mooter, Wim Thielemans

Biblio References: 
Volume: 33 Issue: 22 Pages: 5473-5481