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https://hdl.handle.net/2440/793
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Type: | Journal article |
Title: | Measuring the interaction forces between protein inclusion bodies and an air bubble using an atomic force microscope |
Author: | WangsaWirawan, N. Ikai, A. O'Neill, B. Middelberg, A. |
Citation: | Biotechnology Progress, 2001; 17(5):963-969 |
Publisher: | Amer Chemical Soc |
Issue Date: | 2001 |
ISSN: | 8756-7938 1520-6033 |
Statement of Responsibility: | N. D. Wangsa-Wirawan, A. Ikai, B. K. O’Neill and A. P. J. Middelberg |
Abstract: | 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. |
Keywords: | Inclusion Bodies Humans Escherichia coli Insulin-Like Growth Factor I Recombinant Proteins Buffers Microscopy, Atomic Force Specimen Handling Air Hydrogen-Ion Concentration Osmolar Concentration Static Electricity |
Description: | Copyright © 2001 American Chemical Society and American Institute of Chemical Engineers |
DOI: | 10.1021/bp010072 |
Published version: | http://www3.interscience.wiley.com/cgi-bin/fulltext/121399876/PDFSTART |
Appears in Collections: | Aurora harvest 6 Chemical Engineering publications |
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