Measuring the interaction forces between protein inclusion bodies and an air bubble using an atomic force microscope


Autoria(s): Wangsa-Wirawan, N. D.; Ikai, A.; ONeill, B. K.; Middelberg, A. P. J.
Data(s)

01/01/2001

Resumo

Interaction forces between protein inclusion bodies and an air bubble have been quantified using an atomic force microscope (AFM). The inclusion bodies were attached to the AFM tip by covalent bonds. Interaction forces measured in various buffer concentrations varied from 9.7 nN to 25.3 nN (+/- 4-11%) depending on pH. Hydrophobic forces provide a stronger contribution to overall interaction force than electrostatic double layer forces. It also appears that the ionic strength affects the interaction force in a complex way that cannot be directly predicted by DLVO theory. The effects of pH are significantly stronger for the inclusion body compared to the air bubble. This study provides fundamental information that will subsequently facilitate the rational design of flotation recovery system for inclusion bodies. It has also demonstrated the potential of AFM to facilitate the design of such processes from a practical viewpoint.

Identificador

http://espace.library.uq.edu.au/view/UQ:37636

Idioma(s)

eng

Publicador

Amer Chemical Soc

Palavras-Chave #Biotechnology & Applied Microbiology #Food Science & Technology #Inorganic Salt-solutions #Surface Interactions #Aqueous-electrolyte #Colloidal Forces #Adhesion #Particle #Silica #Water #Reversal #Friction
Tipo

Journal Article