- The science of enzymes, enzymology, goes forward rapidly, and enzymes market is one of the fastest growing ones. What is the reason for such a rapid branch development?
 
- All biochemical processes in living organisms occur involving enzymes. Therefore it is not surprising that scientists want to use that power for their own purposes. Science learned to reproduce enzymes found in the body artificially by growing them out of bacteria. Now they are involved in the processes not only inside but also outside us: in the manufacture of paper, pharmaceuticals, soap powder, and many other products.
 
These molecules representing a tangle of different chemical bonds are the most effective catalysts which could be used in industry. In particular, the immobilized enzymes, those that are physically or chemically bound to an insoluble carrier, a so-called matrix. They have a number of advantages: these enzymes can be separated and re-used, they are more stable.
 
But despite all of the above, the enzymes yield solid inorganic catalysts in the struggle for the widespread use in the industry
 
- Why?
 
- For the same reason that a body temperature above 40 degrees is critical for human beings. At high temperatures enzymes denature, lose their activity. The same is happening in the industry: the molecule tangle unfolds, denaturation happens, it becomes inactive. In the body, everything is foreseen: special proteins (molecular chaperones) are involved in the preservation of the structure of enzymes. But what we can do with the manufacture?
 
Scientists have long puzzled over how to stabilize enzymes, so they do not lose their activity in the harsh heat, radiation, chemical exposure conditions. Enzymes immobilization in inorganic matrices became a solution; amorphous silica became the most popular among them. This method allows increasing the stability of biomolecules close to 100 degrees, but does not solve all problems.
 
- What solution do you propose?
 
- We set out to break the stereotype that the maximum temperature that the enzymes can withstand is 100 degrees. We wanted to prove that a special immobilization will expand the range of applications of enzymes to high-temperature processes such as oil refining and organic synthesis.
 
Our solution is a process of enzyme molecules entropy into the aluminum oxide nanoparticles which results in the "capture" of an enzyme into a porous crystalline matrix. We have experimented with the most common industrial enzymes such as proteinase and xylanase. Our enzyme is movable in its nanocrystalline "shell", but can't unfold and cannot be released.
 
- How your structure is different from that used in the industry now?
 
- In the industry, the entropy method is also used but there is a significant drawback: amorphous structures tend to change over time. The matrix made of such a substance begins to deform, which often leads to the destruction of the content. Our crystal matrix is not affected by these transformations: it provides constant enzyme activity in the catalytic reaction.
 
We compared the resistance to temperatures, following an interesting regularity. When heated up to 90 Celsius degrees, our immobilized proteinase and xylanase enzymes activity was growing significantly. This suggests that the biomolecules continue to function actively as if still in the comfort temperature conditions for themselves.
 
It was established experimentally that our method of stabilizing the enzyme continues to work with unimaginable for these systems 200 degrees. We heated enzymes to the critical point, then we cooled them and checked the level of activity preserved. Enzymes in the matrix based on aluminum oxide withstood four such cycles with a small decrease in activity index, and the solution used in the industry today, was unable to cope with even one.
 
- You have a clear evidence of the effectiveness of your solution and an article published on the results of the work. Now what?
 
- The results of our research are already interesting for the scientists abroad. Together with David Avnir, the co-director of our laboratory, professor at the Hebrew University, we maintain a dialogue with John Brennan, Ph.D., the director of the Biointerface Institute at McMaster University in Canada. It is a well-known scientist, a leading world expert in the field of bioprinting, deposition of the bioactive layer on virtually any surface.
 
One of the points of our cooperation could be the creation of highly stable sensors for medicine and industry. From this collaboration we want to get the most, beginning from joint educational programs, ending with the possibility of commercialization of our developments. Some subsequent publications on the results of our research are already planned. Now we are actively searching for masters and volunteers who would like to join our research.