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A novel alkalo- and thermostable phospholipase D from Streptomyces olivochromogenes

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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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Acknowledgements

This work was supported by a grant RT104-03-03 from the Regional Technology Innovation Program of Ministry of Commerce, Industry, and Energy (MOCIE), Republic of Korea.

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Authors and Affiliations

  1. Department of Pharmacy, College of Pharmacy, Chosun University, Gwangju, 501-759, South Korea

    Jaya Ram Simkhada, So Young Jang, Seung Sik Cho, Eun Jung Park & Jin Cheol Yoo

  2. Department of Complementary and Alternative Therapy, College of Management, Commerce and Social Welfare, Gwangju University, Gwangju, 503-703, South Korea

    Hyo Jeong Lee

  3. Institute of Biomolecule Reconstruction, Sun Moon University, Asansi, Chungnam, 336-708, South Korea

    Jae Kyung Sohng

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  1. Jaya Ram Simkhada
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Correspondence to Jin Cheol Yoo.

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Simkhada, J.R., Lee, H.J., Jang, S.Y. et al. A novel alkalo- and thermostable phospholipase D from Streptomyces olivochromogenes . Biotechnol Lett 31, 429–435 (2009). https://doi.org/10.1007/s10529-008-9890-3

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  • DOI: https://doi.org/10.1007/s10529-008-9890-3

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