Dr. Livnat Apriat-Gourno and her laboratory team at the Miguel Applied Scientific Research Institute, aims to apply the knowledge obtained and improve a variety of enzymes such as those that effectively break down communication molecules between bacteria, as a treatment against disease-causing bacteria and enzymes that break down environmental pollutants
Today, much can be learned from the research on the development paths of enzymes over millions of years, by predicting the sequence of the ancient ancestors and characterizing these ancient enzymes. Dr. Livnat Apriat-Journo and her laboratory team at the Miguel Applied Scientific Research Institute, aims to apply the knowledge obtained and improve a variety of enzymes such as those that effectively break down communication molecules between bacteria, as a treatment against disease-causing bacteria and enzymes that break down environmental pollutants.
Dr. Livnat Afriat-Gourno serves as the head of a research group dealing with the use of enzyme evolution for biotechnological and environmental purposes at the Miguel Applied Scientific Research Institute, and teaches at Tel Hai Academic College in the science departments.
During the years of research carried out by Dr. Apriat-Gourno, she identified a new family of enzymes that break down molecules secreted by bacteria, these molecules allow the bacteria to "communicate" with each other. Dr. Apriat-Gourno found that these enzymes, which have existed for millions of years in bacteria, are evolutionarily related to a "new" enzyme that is very effective in breaking down pesticides that man synthesized about fifty years ago. This is how Dr. Giorno-Apriat focused on questions such as "How did the enzymes that exist today in nature undergo evolution and optimal adaptation to break down man-made matter?" What are the mechanisms that enable the development of new enzymes? How can such evolutionary processes be reproduced in the laboratory and what affects them?" In the laboratory of crystallographer Prof. Colin Jackson at the Australian National University ANU, she learned to better observe the relationship between the three-dimensional structure of enzymes, and their role, in an evolutionary context, with the aim of understanding how a change in the sequence of a protein leads to a structural change that manifests itself in a change in function along a certain evolutionary path . The answer to the above questions was obtained by reconstructing the "reverse" evolutionary path - from a contemporary enzyme to an ancient enzyme. This is a research project led by Dr. Giorno-Apriat, which deals with the design of enzymes that will effectively break down insecticides that are still in use in agriculture, to treat residues of harmful insecticides, which are found in vegetables and fruits or that constitute pollution in an aquatic environment or in the soil. A patent was registered on the sequence of the mutants and a provisional on the encapsulation process of the enzymes. This project is funded by the Ministry of Science for 3 years in collaboration with Dr. Lehi Adler-Abramovich from Tel Aviv University.
Enzymes are protein molecules found in every living cell, and are widely used in industry. Their function is to catalyze biochemical reactions. Without enzymes, vital actions in the human body and in nature, would occur spontaneously after an excessively long period of years or months. In her laboratory, Dr. Afriat-Journo focuses on understanding the development of new enzymes and applies the knowledge to the design and production of engineered enzymes for various uses. A main field of research in the laboratory deals with those enzymes that know how to break down molecules secreted by bacteria as part of a "threshold sensing" mechanism. It is known that many bacteria live as populations and not as individual items, and they have the ability to identify and count identical or different items in a population by secreting and absorbing specific molecules. Once the population has reached a certain threshold, the bacteria recognize it thanks to those molecules, and then they begin to express genes, for example genes involved in causing disease to the host-human or plant. This means that a certain bacteria will not "attack" the host if there are too few items from it, but only if it detects that it has a large enough bacterial population.
Today the laboratory is developing methods to improve the use of these enzymes, with the aim of developing an antibacterial treatment in the mechanism of disrupting the communication of the bacteria. By applying these enzymes, the bacteria will no longer be able to count additional items of their type, since the molecules they secreted have undergone a chemical change by those enzymes. The ambition is that as a result, the development of the disease will be delayed!!!. The significant advantage of using these enzymes is the low chance that resistance will develop against the treatment, because unlike antibiotics, this approach does not kill the bacteria. In a joint study by Dr. Livnat Afriat-Gourno, Dr. Lehi Adler-Abramovich from Tel Aviv University and Dr. Mary Dafni-Yelin from North R&D at the Miguel Research Institute, the effectiveness of mutant enzymes that underwent rounds of evolution to improve their heat resistance was tested. and the introduction of these enzymes into nanocapsules that led to the extension of the enzymes' shelf life. Their effectiveness was tested in growing rooms and in the field against a bacterial disease in pear trees. Today, the disease is treated by spraying antibiotics or chemical sprays based on metals. The study showed that the enzymes produced in the laboratory succeed in delaying the development of the disease in a similar way to antibiotics. The research started with initial funding from the YKA-Migal accelerator of one year and then three years of funding was received from the Ministry of Agriculture. The work was published this year in the scientific journal "American Chemical Society - Applied Materials and Interfaces".
(GurevichD., DorS., ErovM., Dan Y., MoyJ.C., Mairesse O., Dafny-YelinM., Adler-Abramovich L., Afriat-Jurnou L. "Directed Enzyme Evolution and Encapsulation of Quorum Quenching Lactonase in Peptide Nano Spheres as an Antibacterial Treatment against Plant Pathogens""
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