パルス電場処理によるトリプシン活性化メカニズムの化学実験と分子動力学シミュレーションによる解明
This study investigated how pulsed electric field (PEF) treatment modulates trypsin activity using a combination of chemical assays and molecular dynamics simulations. At 20 kV/cm relative to 0 kV/cm, enzyme activity, Vmax, and Kcat rose by 9.30%, 4.74%, and 4.30%, respectively, while Km declined by 11.14%, reflecting enhanced enzyme-substrate interaction. Simulation analyses showed increases in intramolecular hydrogen bond count and solvent-accessible surface area, alongside reductions in rotation radius and random coil content by 5.00% and 3.37%, respectively. Molecular docking further revealed alterations in the active center that elevated substrate affinity. These computational findings were corroborated by spectroscopic measurements, collectively clarifying the molecular basis of PEF-induced trypsin activation.
PEF treatment increases intramolecular hydrogen bond formation and solvent-accessible surface area in trypsin, inducing structural changes at the active center that enhance enzyme-substrate affinity and thereby elevate catalytic activity.
This is basic research at the cellular or molecular level. For human application, inhalation is the most promising delivery route, but inhalation carries explosion risk and concentration matters (empirical LFL of 10%; high-concentration devices are not recommended).
See also:
https://h2-papers.org/en/papers/35728469