Bioluminescence: Siberian experts simulate intracellular habitat of luminescent bacteria
A team of researchers have simulated an intracellular environment of luminescent bacteria using glycerol and sucrose
MOSCOW, October 30. /TASS/. A team of researchers from Russia’s Siberian Federal University (SFU) have simulated an intracellular environment of luminescent bacteria using glycerol and sucrose, the SFU press service said in a statement, adding that the achievement would make it possible to study enzymatic reactions, when one substance is affected by an enzyme and turned into another.
Enzymes are the major regulators of all vitally important processes in the human body and in other living things. Thousands of chemical reactions involving enzymes take place in cells every single second. In particular, metabolic processes, synthesis, digestion, the breakdown of fats, blood circulation and many other processes are impossible without enzymes. In order to study enzymatic reactions thoroughly, scientists throughout the world seek to simulate an intracellular environment that would be as similar as possible to a natural one.
"Researchers from the Institute of Fundamental Biology and Biotechnology at Siberian Federal University (SFU) simulated luminescent bacteria’s intracellular environment using glycerol and sucrose, and conducted some enzymatic reactions inside it," the statement reads.
Bioluminescence - or a living thing’s ability to emit light - is based on an enzyme called luciferase, which converts light during oxidation. Fireflies and marine bacteria are among those who have such an ability. SFU researchers tried to figure out what effect the viscosity of the environment where this reaction takes place has on the speed of enzymatic processes within the cells of such living things. During the first stage, they created several artificial systems using glycerol and sucrose in various concentrations, while the viscosity indicator remained unchanged.
During the second stage, the researchers found out how viscosity affects the speed of an enzymatic reaction in a system containing three enzymes bound together. At the third stage of the experiment, the scientists assessed the three-enzyme system’s resistance to high temperatures ranging from 15 to 80 degrees Celsius. As a result, they established that sucrose was more effective than glycerol in limiting the mobility of enzyme molecules, which may change the reaction’s speed and even its mechanism.
"The unique feature of our research is that we use natural substances - glycerol and sucrose - that every living cell contains instead of crowding agents used in similar experiments," Junior Researcher at the SFU Laboratory of Bioluminescence Technology Oleg Sutormin said, commenting on the outcome of the research.