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KMID : 0545119960060060407
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Journal of Microbiology and Biotechnology
1996 Volume.6 No. 6 p.407 ~ p.413
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Purification and Biochemical Properties of Extracellular Phospholipase A_1 from Serratia sp. MK1
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KIM MYUNG-KEE
RHEE JOON-SHICK
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Abstract
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A novel type of extracellular phospholipase A_1 was isolated from Serratia sp. MK1 and purified to homogeneity by ammonium sulfate precipitatoin, anion exchange and gel filteration chromatography. The purified enzyme was a monomer with a molecular mass of about 43,000 Da. This enzyme showed the highest lipolitic activity toward phosphatidylserin among the phosphoglycerides tested, and preferentially catalyzed the hydrolysis of the ester bond in phosphatidic acid to lyso-phosphatidic acid. Enzyme activity was fully recovered by the presence of Ca^2+. This implise that the enzyme requires Ca^2+ for activity. The enzyme was stable up to 70℃ when incubated for 1 h at pH 8.5, and the optimal pH and temperature were 8.5 and 50℃, respectively.
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