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ABSTRACT
Aquaporin biomimetic membrane can only transfer water molecules in and out of the membrane while preventing the passage of other smaller ions and solutes. AquaporinZ (AqpZ), widely spread in Escherichia coli cell membrane, has shown higher water permeability than conventional membranes. Application of those exceptional properties as water purification membrane material is promising. The objective of this study was to assess protein expression conditions for AqpZ mass production. Recombinant AqpZ was successfully synthesized and identified via sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and western blot analysis. The highest level of expression of his-tagged AqpZ (12.2 mg/L) was achieved using E. coli BL21(DE3) host strain by the addition of 0.1 mM isopropyl-b-D-thiogalactoside and 5 h postinduction time. Subsequently, solubilization and purification of his-tagged AqpZ were carried out.
Acknowledgement
This research was supported by a grant (07SeaHeroA01-01) from the Plant Technology Advancement Program funded by the Ministry of Land, Transport.
Notes
Presented at The Fifth Desalination Workshop (IDW 2012), October 28–31, 2012, Jeju, Korea