Thermostable lipoxygenase is a key enzyme in the conversion of linoleic acid to trihydroxy-octadecenoic acid by <Emphasis Type="Italic">Pseudomonas aeruginosa</Emphasis> PR3 |
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Authors: | Jae-Han Bae Ching T Hou Hak-Ryul Kim |
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Institution: | (1) Department of Animal Science and Biotechnology, Kyungpook National University, 702-701 Daegu, South Korea;(2) Department of Food and Nutrition, College of Health Science, Korea University, Seoul, South Korea;(3) Department of Biotechnology, College of Engineering, Daegu University, Gyungsan, South Korea;(4) Microbial Genomic and Bioprocessing Research Unit, National Center for Agricultural Utilization Research, ARS, USDA, Peoria, IL 61604, USA; |
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Abstract: | Lipoxygenases (LOXs) constitute a family of lipid-peroxidizing enzymes that catalyze the oxidation of unsaturated fatty acid
containing a (1Z,4Z)-pentadiene structural unit, leading to formation of conjugated (Z,E)-hydroperoxydienoic acid. LOXs are known to be widely distributed in plants and animals. Recently, several microbial LOXs
were reported to be involved in the production of hydroperoxy fatty acids. Among the microorganisms that produce hydroxy fatty
acids, Pseudomonas aeruginosa PR3 is known to convert linoleic acid to trihydroxy fatty acid, which suggests the involvement of a LOX enzyme. Based on
these reports, we identified a novel thermostable LOX from P. aeruginosa PR3 strain. The protein was purified 34.3-fold with a recovery rate of 5.14%. The Km and Vmax values of the purified enzyme were 3.57 mM and 0.73 μmol/min//mg, respectively. Heat stability of the purified enzyme was
unexpectedly high with an LD50 of 90 min at 80°C, although P. aeruginosa PR3 is known as a mesophilic bacterium. Substrate specificity of the purified enzyme was restricted only to unsaturated fatty
acids carrying a (1Z,4Z)-pentadiene unit. |
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