Russian researchers reconstructed the evolution process of the oxidoreductase (LuxG) family of bioluminescent bacteria and determined the conditions necessary for the efficient functioning of this enzyme.

The findings by researchers from the Siberian Federal University (SFU) who worked along with colleagues from the Institute of Cell Biophysics of the Russian Academy of Sciences, State Institute of Information Technologies and Telecommunications ("Informika") and Institute of Biophysics of the Siberian Branch of the Russian Academy of Sciences were published in the journal Proteins and can be used for efficient bioassays to estimate the toxicity of food, soil, and water.

SFU researchers studied the evolution process of the enzyme called LuxG oxidoreductase of bio-luminous bacteria, which is synthesized with luciferase – a bioluminescent protein produced by fireflies, jellyfish and mushrooms. Having compared the data on the evolution of oxidoreductase with the data on this protein’s 3D structure, scientists have determined the number of important factors that contribute to the efficient functioning of this enzyme.

"We believe that understanding how LuxG oxidoreductase functions, where it came from and how it evolved will bring scientists closer to carrying out more accurate bioassays than the ones we have today", said Anna Deyeva, from SFU Laboratory of Bioluminescent Biotechnologies. "Proteins that are synthesized simultaneously, that evolve together, will probably work together far better than the proteins in hybrid systems, where luciferase has to team up with unfamiliar reductases".

Bioassay is a technique used for assessing the level of toxicity in water, soil and food. This method relies on using living organisms, cells and enzymes.

Luciferase is present in every bacterial bioluminescent enzyme test system. It requires two substrates: one is abundant, while the other is highly unstable; this is why it is supplied by an oxidoreductase. Despite the use of luciferase and oxidoreductase in bioassay development, little is known about this enzyme so far.

Further research will enable the development of a system of express monitoring that will allow scientists to evaluate the level of contamination in a sample in just 15 minutes.