Aquaporin A/S

Aquaporin A/S is a global cleantech company located in Kongens Lyngby, Denmark. Aquaporin is dedicated to revolutionizing water purification through the use of industrial biotechnological techniques and thinking. The main goal of Aquaporin is to develop the Aquaporin Inside technology – capable of separating and purifying water from all other compounds. The Aquaporin Inside platform uses biotechnological principles in a technological context which is a novel upcoming field with large commercial perspectives. This is a field where Denmark has taken an early global lead. Aquaporin is currently building its global distribution network within all segments.

Company details

Nymøllevej 78 , Kongens Lyngby , DK-2800 Denmark

Locations Served

Business Type:
Manufacturer
Industry Type:
Water and Wastewater - Water Filtration and Separation
Market Focus:
Globally (various continents)

Aquaporin is dedicated to revolutionising water purification and desalination of seawater through the use of industrial biotechnological techniques and thinking. The main goal of Aquaporin is to develop the Aquaporin Inside™ technology. Commercial success will be reached through completion of the three main phases in which the development of Aquaporin is structured are:

  • Development and proof of the technological concept
  • Development of a prototype and further development thereof into a final membrane technology
  • Marketing, sales and out licensing of the final membrane technology expected in 2013

The technological platform of Aquaporin is the use of biotechnological principles in a technological context which is a novel upcoming field with large commercial perspectives. This is a field where Denmark has taken an early global lead.

Today Aquaporin's shareholders are:

Aquaporin is a subsidiary in the M. Goldschmidt Holding A/S group.

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The IP strategy of Aquaporin includes aggressive patenting of all new technologies following proof of concept and reproducibility studies. Having a skilled and committed team of scientists/engineers, the company is well positioned to contribute in this emerging area of biomimetic materials and has established a selected portfolio of patent applications covering core developments in the field of water purification/filtration and other applications.

In addition, Aquaporin seeks to in-license complementary technologies that can contribute to reaching its goal of creating a reliable and cost efficient filtration membrane for ultra pure water production and numerous other water purifications markets.

Aquaporin envisages the proprietary technologies of the company to be useful in a wide range of applications and is willing to discuss non-exclusive licenses with other companies.

An essential building block in the water membrane technology of Aquaporin A/S is the aquaporin molecule. The aquaporin molecule is described in the following.

Living cells are enclosed by a lipid bilayer membrane, separating the cells from other cells and their extra cellular medium. Lipid bilayer membranes are essentially impermeable to water, ions, and other polar molecules; yet, in many instances, such entities need to be rapidly and selectively transported across a membrane, often in response to an extra- or intracellular signal. The water-transporting task is accomplished by aquaporin water channel proteins (Preston et al., 1992).

Academic version of the scientific animation movie on the aquaporin membrane technology Aquaporins are crucial for life in any form and they are found in all organisms, from bacteria via plants to man. Aquaporins facilitate rapid, highly selective water transport, thus allowing the cell to regulate its volume and internal osmotic pressure according to hydrostatic and/or osmotic pressure differences across the cell membrane. The physiological importance of the aquaporin in human is perhaps most conspicuous in the kidney, where ~150-200 litres of water need to be reabsorbed from the primary urine each day, that is, aquaporin facilitated water transport is invoked when water rapidly must be retrieved from a body fluid.

In kidneys, this is made possible mainly by two aquaporins denoted AQP1 and AQP2 (11 different aquaporins are known in humans). In plants, aquaporins are also critical for water absorption in the root and for maintaining the water balance throughout the plant (Agre et al., 1998, Borgnia et al., 1999).

Studies of water transport in various organisms and tissues suggested that aquaporins have a narrow pore preventing any large molecule, ions (salts) and even proton (H3O+) and hydroxyl ion (OH-) flow while maintaining an extremely high water permeation rate; ~ 109molecules H2O per channel per second (Agre et al., 1998, Borgnia et al., 1999).

Until 2000 and 2001 where the first high-resolution 3D structure of AQP1 and that of the related glycerol-conducting bacterial channel protein aquaglyceroporin GlpF were reported (Fu et al., 2000; Murata et al., 2000; Ren et al., 2001; Sui et al., 2001) little was known about the origin of water selectivity.

However, based on the experimental structures, detailed computer models were put forward explaining not only the high permeation rate and the strict water selectivity but also the ability of aquaporins to prevent proton leakage (de Groot and Grubmüller, 2001; Tajkhorshid et al., 2002, Jensen et al., 2003, Zhu et al. 2003, de Groot et al., 2003, Burykin and Warshel 2003, Ilan et al., 2004, Chakrabarti at al., 2004). In essence, the architecture of the aquaporin channel allows water molecules to pass only in single file while electrostatic tuning of the channel interior controls aquaporin selectivity against any charged species, that is, transport of any salt (ion) as well as protons and hydroxyl ions is abrogated (de Groot and Grubmüller, 2001; Tajkhorshid et al., 2002, Jensen et al., 2003, Zhu et al. 2003, de Groot et al., 2003, Burykin and Warshel 2003, Ilan et al., 2004, Chakrabarti at al., 2004). In short, this implies that only water molecules pass through the aquaporin water pore, nothing else.

In the short span of just over ten years from the discovery of aquaporins in 1992 (Preston et al., 1992) to now an almost complete atomic-level understanding of aquaporin water channel function has been reached as recently underscored by awarding the Nobel Prize in chemistry to Professor Peter Agre in 2003 for his discovery of the aquaporin water channel.

The physiological roles of water channels in both eukaryotic and prokaryotic organisms have been elucidated and their roles in living cells are becoming increasingly well documented. The understanding of aquaporins and their role in life has opened the possibility of using aquaporins in an industrial context. Aquaporin's goal is to use aquaporins as cornerstones in water filtering devices to be employed in industrial and household water filtration and purification.

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Nature provides an excellent palette of highly effective membranes capable of highly selective vectorial transport of a large number of molecular species. It is therefore striking that the membrane industry has developed synthetic separation membrane processes in a very different way [1].

Traditional separation membranes are mostly dense polymeric films where advanced chemistry is used to control the surface properties of the films produced [2]. A wide range of polymers and production techniques are been used resulting in a great diversity in structure and function of separation membranes tailored to a wide variety of applications. Separation is usually described in terms of pore/solute size, pore/solute charge and dielectric effects, coupled with diffusion or convective flow. Occasionally, more complex partitioning and transport mechanisms are used, however, most synthetic membranes may be broadly described as polymer sheets containing micron to nanometre sized holes.

This is in stark contrast to the bewildering complexity of biological membranes. 30 % of the human genome codes for membrane proteins [3], and a typical mammalian cell membrane hosts several hundred lipid types [4]. Despite dramatic progress over the last decades in our understanding of the molecular basis for biological membrane transport (e.g. [5-7]), this complexity remains a major obstacle in our molecular understanding of how living cells maintain their integrity and perform their function [8].
One way leading to a better understanding of membranes and membrane transport is to focus on a few of its components and features. This understanding is crucial if we want to exploit – or mimic – nature’s tremendous capability for selective membrane transport. The term Biomimetic Membranes denotes the common denominator for such endeavours [9]. Recent examples of membrane biomimetics include low noise recording devices for ion channel research [10], free-standing triblock copolymer membranes [11, 12], enzyme-immobilization [13], and gas-extraction membranes [14].

In the development of biomimetic membranes it is important to know the morphological descriptors such as the amount and intrinsic properties of amphiphiles (lipidic or block coplymeric types) forming the membrane, the equilibrium thickness, and the coverage. Also important are the properties of interaction: the stability against mechanical perturbations (e.g. viscoelastic responses to changes in hydrostatic or osmotic pressure differences) [15, 16], the rate of regeneration (self healing) [17], the ease with which functional peptides or proteins can be adsorbed/incorporated [18] and, once incorporated, how proteins interact with the amphiphilic matrix [19]; and surface (e.g. electrostatic) energetics [20].

Perhaps the most challenging part of biomimetic membrane development is to understand the interaction between the membrane and its support – in particular when this support also is porous and thus can support mass transport across the membrane [21]. In Aquaporin's case the biomimetic membrane with embedded aquaporins must support pressures up to 10 bar and allow a water flux > 100 l /m3 h. Therefore the development of the Aquaporin Inside™ membrane is closely linked to the simultaneous development of suitable porous support materials.