A novel alkalo- and thermostable phospholipase D from <Emphasis Type="Italic">Streptomyces olivochromogenes</Emphasis> |
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| Authors: | Jaya Ram Simkhada Hyo Jeong Lee So Young Jang Seung Sik Cho Eun Jung Park Jae Kyung Sohng Jin Cheol Yoo |
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| Institution: | (1) Department of Pharmacy, College of Pharmacy, Chosun University, Gwangju, 501-759, South Korea;(2) Department of Complementary and Alternative Therapy, College of Management, Commerce and Social Welfare, Gwangju University, Gwangju, 503-703, South Korea;(3) Institute of Biomolecule Reconstruction, Sun Moon University, Asansi, Chungnam, 336-708, South Korea |
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| Abstract: | A 60 kDa phospholipase D (PLD) was obtained from Streptomyces olivochromogenes by one-step chromatography on Sepharose CL-6B. Maximal activity was at pH 8 and 75°C and the enzyme was stable from pH 7
to 13 and from 55 to 75°C. Thermal and pH stability with temperature optimum of the enzyme were highest among Streptomyces PLDs reported so far. The activity was Ca2+-dependent and enhanced by detergents. The Km and Vmax values for phosphatidylcholine were 0.6 mM and 650 μmol min−1 mg−1, respectively. In addition, the enzyme also revealed transphosphatidylation activity, which was optimum at pH 8 and 50°C.
The first 15 amino acid residues of the N terminal sequence were ADYTPGAPGIGDPYY, which are significantly different from the
other known PLDs. The enzyme may therefore be a novel PLD with potential application in the lipid industry. |
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| Keywords: | Alkalo- and thermostable One-step purification Phospholipase D Streptomyces olivochromogenes |
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