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논문 기본 정보

자료유형
학술저널
저자정보
Simkhada, Jaya Ram (Department of Pharmacy, College of Pharmacy, Chosun University) Cho, Seung-Sik (Department of Pharmacy, College of Pharmacy, Chosun University) Lee, Hyo-Jung (Department of Pharmacy, College of Pharmacy, Chosun University) Yoo, Jin-Cheol (Department of Pharmacy, College of Pharmacy, Chosun University)
저널정보
대한약학회 Archives of pharmacal research : a publication of the Pharmaceutical Society of Korea Archives of pharmacal research : a publication of the Pharmaceutical Society of Korea 제30권 제10호
발행연도
2007.1
수록면
1,302 - 1,308 (7page)

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초록· 키워드

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Streptomyces sp. CS-57, which was isolated from Korean soil, was found to produce phospholipase D ($PLD_{57}$) as an extracellular enzyme when cultured in medium containing 2% glucose, 1.5% yeast extract, 0.5% trypton, and 0.1% calcium carbonate at $28^{\circ}C$, and 160-rpm. $PLD_{57}$ was purified using Sepharose CL-6B column chromatography, and DEAE-Sepharose CL-6B ion exchange column chromatography. The specific activity of the purified enzyme increased 6.7 fold with 3% recovery. The purified enzyme was then analyzed using 12% SDS-PAGE, which revealed that the molecular mass of the purified enzyme was 55 kDa. $PLD_{57}$ showed both hydrolytic (H) and transphosphatidylation (T) activity, and the optimum temperatures of these activities were found to be $45^{\circ}C\;and\;35^{\circ}C$, respectively. Similarly, both of these activities were found to be optimal at a pH of 7.5. In addition, even after being heat treated at $45^{\circ}C$ for up to 2 h, the enzyme activity remained at 100%, and the H-activity was found to be stable at a pH of 6 to 8. Further, enzyme activity occurred in the presence of EDTA, indicating that metal ions are not required for their activity, although some metal ions did marginally increase the activity. Enzyme activity also increased by 75% in the presence of Triton-X 100 at a concentration of 0.375 %; however, none of the other detergents evaluated in this study were found to enhance enzyme activity.

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