Earticle

초록

영어

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. 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 80oC, 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.

키워드

저자

• Jinhee JANG [ Department of Biological Engineering, Inha University, Incheon 402-751. ]
• Jae-Han BAE [ Department of Biological Engineering, Inha University, Incheon 402-751. ]
• Choul-Gyun LEE [ Department of Biological Engineering, Inha University, Incheon 402-751. ]
• Hak-Ryul KIM [ Department of Animal Science and Biotechnology, Kyungpook National University, Daegu 702-701. ]

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간행물

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• 간행물명

  한국생물공학회 학술대회

• 간기

  반년간

• 수록기간

  1985~2013

• 십진분류

  KDC 476 DDC 576