원문정보
초록
영어
Lipoxygenases, enzymes that contain non-heme iron, catalyze the oxidation of unsaturated fatty acids with a (1Z,4Z)-pentadiene moiety leading to conjugated (Z,E)-hydroperoxydienoic acids. These enzymes are widely distributed in plants and animals, and a few microorganisms are reported as well. It was reported that conversion of linoleic hydroperoxide by soybean lipoxygenase generated trihydroxy-, hydroperoxy dihydroxy-, hydroxyepoxy-octadecenoate, and lipid hydroperoxide. These reaction products are also known in many other higher plants. Previously, we reported that Pseudomonas aeruginosa PR3 converted linoleic acid to equimolar mixture of 9,10,13-trihydroxy-11(E)-octadecenoic acid and 9,12,13-trihydroxy-10(E)-octadecenoic acid.
These results augmented us to address identification of new lipoxygenase in P. aeruginosa PR3. As a result, we isolated a protein carrying lipoxygenase activity from P. aeruginosa PR3 with 20.6 purification fold and 3.1% of recovery. The Km and Vmax value of the purified enzyme was 4.923 mM and 0.815 μM· min-1·mg-1, respectively. The optimal pH and temperature was 6.0 and and 60℃, respectively.
Moreover, this enzyme is highly thermostable representing 60% of the initial activity after incubation at 80℃ for 2 hours.