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Lyngby, Denmark

Patent
Aquaporin | Date: 2014-02-24

The present invention relates to a water extraction system comprising a flow cell comprising a membrane; said membrane comprising an active layer comprising immobilized aquaporin water channels and a support layer, and said membrane having a feed side and a non-feed side; and an aqueous source solution in fluid communication with the feed side of the membrane.


Patent
Aquaporin and Nanyang Technological University | Date: 2012-03-02

Present invention relates to a thin film composite membrane wherein a thin selective layer, having incorporated amphiphilic vesicles, is supported by a microporous substrate. A process of preparing the thin film composite membrane and its use are also disclosed.


Patent
Aquaporin | Date: 2011-10-04

A liquid membrane system is disclosed in the form of a biochannel containing bulk liquid membrane (BLM), biochannel containing emulsion liquid membrane (ELM), and biochannel containing supported (immobilised) liquid membrane (SLM), or a combination thereof, wherein said liquid membrane system is based on vesicles formed from amphiphilic compounds such as lipids forming a bilayer wherein biochannels have been incorporated and wherein said vesicles further contain a stabilising oil phase. The uses of the membrane system include water extraction from liquid aqueous media by forward osmosis, e.g. for desalination of salt water.


Grant
Agency: Cordis | Branch: H2020 | Program: IA | Phase: BIOTEC-4-2014 | Award Amount: 7.68M | Year: 2015

In the vaccine industry, downstream processing is of extreme importance. Prophylactic vaccines aim at protecting healthy people, so any contaminant has to be discarded with the most drastic measures. Such negative approach comes at the expense of the recovery of product : yields are poor, thereby inducing a high product cost. Processes are also complex, since they rely on multiple eliminations rather than on recovery of the unique product of interest. Technically, this is mostly due to the lack of specific capture systems that would allow direct, positive separation of the vaccine from its environment.Vaccines know no borders. For developing countries, the pressure on costs is even more acute, and local production is a way to try to reach the 1$ per dose target. In this context, water sustainability is a major issue, as it is a most sensitive ingredient in bioproduction. DiViNe will tackle theses cost and environmental issues with technological answers. The partners will combine two major Nano/biotechnology innovations to develop an integrated purification platform amenable to the different natures of vaccines : glycoconjugates, protein antigens and enveloped viruses. They will implement Nanofitins (novel affinity capture ligands) and Aquaporin-based membranes (energy-saving nano-biomimetics used in the cleantech industry), for a positive purification approach. High yields are expected (data from antibody purification with Nanofitins), at affordable cost of goods and with a sustainable approach of water recycling. Novartis Vaccines brings to the Consortium a broad range of targets, and identical strategies can be applied for biopharmaceuticals in general. The development custom affinity capture processes as a sustainable platform is therefore economically relevant, in a very large market. Beyond the technical partnership, the project is a first run for the partners to structure the platform as a commercial offer for downstream processing of biologics.


Bomholt J.,Aquaporin | Helix-Nielsen C.,Aquaporin | Helix-Nielsen C.,Technical University of Denmark | Scharff-Poulsen P.,Copenhagen University | Pedersen P.A.,Copenhagen University
PLoS ONE | Year: 2013

In the present paper we explored the capacity of yeast Saccharomyces cerevisiae as host for heterologous expression of human Aquaporin-1. Aquaporin-1 cDNA was expressed from a galactose inducible promoter situated on a plasmid with an adjustable copy number. Human Aquaporin-1 was C-terminally tagged with yeast enhanced GFP for quantification of functional expression, determination of sub-cellular localization, estimation of in vivo folding efficiency and establishment of a purification protocol. Aquaporin-1 was found to constitute 8.5 percent of total membrane protein content after expression at 15°C in a yeast host over-producing the Gal4p transcriptional activator and growth in amino acid supplemented minimal medium. In-gel fluorescence combined with western blotting showed that low accumulation of correctly folded recombinant Aquaporin-1 at 30°C was due to in vivo mal-folding. Reduction of the expression temperature to 15°C almost completely prevented Aquaporin-1 mal-folding. Bioimaging of live yeast cells revealed that recombinant Aquaporin-1 accumulated in the yeast plasma membrane. A detergent screen for solubilization revealed that CYMAL-5 was superior in solubilizing recombinant Aquaporin-1 and generated a monodisperse protein preparation. A single Ni-affinity chromatography step was used to obtain almost pure Aquaporin-1. Recombinant Aquaporin-1 produced in S. cerevisiae was not N-glycosylated in contrast to the protein found in human erythrocytes. © 2013 Bomholt et al. Source

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