Improving the inactivation effect of lipoxygenase through a novel catalytic infrared system and exploring its inactivation mechanism

To achieve efficient lipoxygenase (LOX) inactivation, this study developed an innovative catalytic infrared (IR) method using natural gas as an alternative to conventional electric heating. The activity, deactivation kinetics, structure, and catalytic kinetics of LOX were evaluated following IR treatment. Molecular dynamics and docking simulations were employed to assess the inactivation effects of both thermal and radiation components. Both temperature and wavelength effects contributed significantly to LOX denaturation, with an inactivation rate of 95.83% after 9 min at 130 °C. This was evidenced by the disruption of hydrogen bonds and various interactions, the disordering of LOX's secondary structure, and a reduction in LOX-substrate binding energies. The deactivation kinetics followed a Weibull distribution. The catalytic reaction efficiency of LOX decreased 177-fold. The temperature effect was stronger than the wavelength effect. This study provides a quantified mechanism for LOX inactivation by IR, highlighting IR as a promising alternative to conventional methods, offering both energy savings and efficient enzyme deactivation.