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|Title:||Stabilization and immobilization of aquaporin reconstituted lipid vesicles for water purification|
|Authors:||Sun, G. |
|Citation:||Sun, G., Chung, T.-S., Jeyaseelan, K., Armugam, A. (2013-02-01). Stabilization and immobilization of aquaporin reconstituted lipid vesicles for water purification. Colloids and Surfaces B: Biointerfaces 102 : 466-471. ScholarBank@NUS Repository. https://doi.org/10.1016/j.colsurfb.2012.08.009|
|Abstract:||Aquaporins are water channel proteins in biological membranes that have extraordinary water permeability and selectivity. In this work, we have demonstrated that one of their family members, AquaporinZ (AqpZ), can be possibly applied in a pressure-driven water purification process. A nanofiltration membrane was designed and fabricated by immobilization of AqpZ-reconstituted liposomes on a polydopamine (PDA) coated microporous membrane. Amine-functionalized proteoliposomes were first deposited via gentle vacuum suction and subsequently conjugated on the PDA layer via an amine-catechol adduct formation. Due to the existence of a polymer network within the lipid bilayers, the membrane could sustain hydraulic pressure of 5bar as well as the strong surface agitation in nanofiltration tests, indicating a relatively stable membrane structure. In comparison with membrane without AqpZ incorporation, the membrane with AqpZ-to-lipid weight ratio of 1:100 increased the water flux by 65% with enhanced NaCl and MgCl2 rejections of 66.2% and 88.1%, respectively. With AqpZ incorporation, the vesicle immobilized membrane exhibits a promising strategy for high productivity water purification. © 2012 Elsevier B.V.|
|Source Title:||Colloids and Surfaces B: Biointerfaces|
|Appears in Collections:||Staff Publications|
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