Nonthermal inactivation of soy (Glycine max Sp.) lipoxygenase by pulsed ultraviolet light.

This study investigated pulsed ultraviolet (PUV) illumination at different distances from the PUV source on soybean lipoxygenase (LOX) (0.4 mg/mL in 0.01 M Tris-HCl buffer, pH 9) activity. Samples (5 mL) were illuminated for 1, 2, 4, 8, and 16 s at 3 distances 6, 8.5, and 11 cm from the PUV lamp's quartz window. The temperature of 33.5 ± 1.8°C was observed for the highest treatment time of 16 s at the shortest distance of 6 cm, and resulted in a 3.5 log reduction (99.95%) in initial LOX activity. Illumination time and distance from the lamp significantly (P ≤ 0.05) affected LOX inactivation. Sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) was performed on treated LOX samples and further protein profile for treated LOX filtrate (≤10 kDa), was analyzed by reverse phase high-performance liquid chromatography (RP-HPLC). The protein profile analysis revealed that LOX protein degradation was influenced significantly (P ≤ 0.05) by PUV illumination time.