Chemiluminescence properties of soybean protein fraction in the hydroperoxide and hydrogen donor system.
Whey fraction, a constituent of soybean protein, produced a photon emission in the presence of gallic acid and hydrogen peroxide. Identification of the chemiluminescence agent from the whey fraction indicated the participation of lipoxygenase in the emission. The reactivity of lipoxygenase with peroxides in the gallic acid solidus hydroperoxide system was in the order of methylethyl hydroperoxide (MEK-OOH, 4800 cps) > tert-butyl hydroperoxide (tert-BuOOH, 607 cps) > hydrogen peroxide (H(2)O(2), 455 cps) > cumene hydroperoxide (cumene-OOH, 261 cps). Emission maxima for H(2)O(2) and cumene-OOH were 670 nm, and emission maxima for MEK-OOH and tert-BuOOH were at 510 nm. The photon intensity from the gallic acid lipoxygenase system corresponded to the linoleic acid hydroperoxide value. A high correlation of photon intensity with hydroperoxide, including linoleic hydroperoxide was useful as a simple and sensitive method for the direct detection of hydroperoxides in biomaterials.
Yoshiki
Y
Y
Department of Environmental Bioremediation, Graduate School of Agricultural Science, Tohoku University, 1-1 Tsutsumidori Amamiyamachi, Aoba-ku, Sendai, Miyagi, 981-8555, Japan.
Yamanaka
T
T
Satake
K
K
Okubo
K
K
D006861:Hydrogen Peroxide / Q000737:chemistry*; D008084:Lipoxygenase / Q000737:chemistry*; D008163:Luminescent Measurements; D013025:Glycine max / Q000737:chemistry / Q000201:enzymology*; D013057:Spectrum Analysis
D006861:Hydrogen Peroxide; D008084:Lipoxygenase