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Inactivation of tea leaf hydroperoxide lyase by fatty acid hydroperoxide

Inactivation of tea leaf hydroperoxide lyase by fatty acid hydroperoxide

Journal of Agricultural & Food Chemistry 40(2): 175-178

Tea leaf hydroperoxide lyase (HPO lyase) was rapidly and irreversibly inactivated by linoleic acid 13-hydroperoxide [13(S)-hydroperoxy-9(Z),11(E)-octadecadienoic acid (LA 13-HPO]. The rate of the inactivation was directly dependent upon the concentration of hydroperoxide, and its second-order rate constant at pH 5.5 and 25.degree. C was 265 M-1 s-1. Linoleic acid 9-hydroperoxide [9(R)-hydroperoxy-10(E), 12(Z)-octadecadienoic acid], which is little catalyzed by tea leaf HPO lyase, also inactivated the enzyme, but the other organic hydroperoxides such as cumene, tert-butyl hydroperoxide, and H2O2 did not. Inactivation by LA 13-YHPO was protected either by dithiothreitol or by LA 13-hydroxide, which suggests that the inactivation is caused by destruction of an essential SH group near the reaction center of the enzyme. Hydrophobic radical scavengers such as .alpha.-tocopherol and nordihydroguaiaretic acid effectively protected HPO lyase from the inactivation, but mannitol and diethylenetriaminepentaacetic acid showed no effect.

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Accession: 007443243

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DOI: 10.1021/jf00014a002

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