Enolase is a conservative
protein. Its cellular enzymatic activity
catalyzes the conversion of 2-phospho-d-glycerate (2-PGA)
to a phosphoenolpyruvate (PEP) product in the glycolysis pathway.
This enzyme also has a multifunctional nature participating in several
biological processes. This work aims to determine the effect of water
polarization on the catalytic activity of enolase. The experiments
have been set based on the concept that water, a polar dielectric,
may undergo the phenomenon of electric polarization, decreasing its
configurational and vibrational entropy. Prior to the reaction, the
2-PGA substrate was incubated for 5 h in the glass cuvette with an
attached chip-inductor. The latter device was designed to transfer
quantum information about a given quantum state from the quantum state
generator to water by a phonon resonance. Then, such substrate samples
preincubated with the chip-inductor were removed every hour in a separate
quartz cuvette with the enzyme to determine its catalytic activity.
The influence of the chip-inductor on the preincubated substrate resulted
in an increase in the catalytic activity of enolase by 30% compared
to the control substrate, not preincubated with the chip-inductor.
This suggests that the catalytic activity of the enzyme is augmented
when the substrate was primed by chip-inductors. In another kind of
experiment, wherein enolase was exposed to methylglyoxal modification,
the catalytic activity of the enzyme dropped to 71.7%, while the same
enzyme glycated with methylglyoxal primed by chip-inductors restored
its activity by 8.4%. This shows the protective effect of chip-inductors
on enolase activity despite the harmful effect of methylglyoxal on
the protein.