Splitting water into its constituents hydrogen and oxygen remains an enviable task in the field of science, given the scope’s huge potential for running future vehicles on H2O. Well researchers from the Indiana University have brought such an ambit one step closer to reality, with their creation of a special biomaterial that catalyzes the formation of hydrogen. This biometerial in question entails a modified enzyme that is rather strengthened by the protein housing (capsid) of a bacterial virus. And this fascinating composition (entailing the combination of the enzyme and the virus) makes for a highly efficient biomaterial that is 150 times more effective in catalyzing hydrogen than its regular enzyme counterpart.

As Trevor Douglas, the Earl Blough Professor of Chemistry in the IU Bloomington College of Arts and Sciences’ Department of Chemistry, and leader of the study, made it clear –

Essentially, we’ve taken a virus’s ability to self-assemble myriad genetic building blocks and incorporated a very fragile and sensitive enzyme with the remarkable property of taking in protons and spitting out hydrogen gas. The end result is a virus-like particle that behaves the same as a highly sophisticated material that catalyzes the production of hydrogen.

As for the contrivance of the modified enzyme, the scientists utilized the genetic material known as hydrogenase. It is produced by two genes (hyaA and hyaB) derived from the common bacteria Escherichia coli that were then integrated inside the aforementioned protective capsid – by some indigenous processes perfected by the team. This protein capsid was salvaged from bacteriophage P22, a known bacterial virus. As as result, the newly concocted biomaterial is called the P22-Hyd, and it can be simply ‘harvested’ by an easy fermentation procedure that takes place at room temperature.

Interestingly, the researchers chose nickel-iron (NiFe)-hydrogenase, which in its conventional form is highly vulnerable to exposed chemicals in the environment. But the scientists solved the issue by incorporating it inside the capsid, which endowed the genetic material the capacity to catalyze at room temperature while showcasing high resistance to external elements. Moreover, NiFe-hydrogenase has the intrinsic ability to easily integrate into biomaterials – the very reason why it was chosen in the first place.

Now as for the incredible advantages of the P22-Hyd biomaterial, the scientists have already touted its environmentally friendly and low cost attributes. For comparison’s sake, one of the common technologies that catalyzes hydrogen as fuel in futuristic automobiles, utilizes platinum – which is unfortunately expensive and pretty rare. Furthermore, the P22-Hyd can both split water and also recombine hydrogen and oxygen to generate power. So basically, the biodegradable ‘green’ material can be used as a catalyst for both hydrogen production and fuel cells.

But its greatest advantage arguably relates to the practicality of the scope. As Douglas said –

No one’s ever had a way to create a large enough amount of this hydrogenase despite its incredible potential for biofuel production. But now we’ve got a method to stabilize and produce high quantities of the material—and enormous increases in efficiency.

And at last but not the least, the research team is not stopping at just the concoction of this potentially valuable biomaterial. They are also looking forth to processes that could aid in the catalytic reactions between the material and incoming sunlight. Simply put, the P22-Hyd biomaterial can be possibly incorporated in the burgeoning scope of solar-powered systems.

The study was originally published in Nature Chemistry.

Rendering showcasing the release of NiFe-hydrogenase from inside the capsid shell.

Source: Indiana University