2. Academic Validation
  3. Extracellular production of a sphingomyelinase from Streptomyces griseocarneus using Streptomyces lividans

Extracellular production of a sphingomyelinase from Streptomyces griseocarneus using Streptomyces lividans

  • Biotechnol Lett. 2011 Apr;33(4):727-31. doi: 10.1007/s10529-010-0480-9.
Daisuke Sugimori 1,  Yu Tomita,  Yusaku Matsumoto,  Chiaki Ogino
Affiliations

Affiliation

  • 1 Department of Symbiotic Systems Science and Technology, Graduate School of Symbiotic Systems Science and Technology, Fukushima University, Kanayagawa, Fukushima, Japan. [email protected]
PMID: 21116683 DOI: 10.1007/s10529-010-0480-9
Abstract

The structural gene for sphingomyelinase (SMase) from Streptomyces griseocarneus, was introduced into Streptomyces lividans using a shuttle vector, pUC702, for Escherichia coli/S. lividans. High-level secretory production of SMase was achieved using the promoter, signal sequence and terminator regions of Phospholipase D from Streptoverticillium cinnamoneum. The transformant constitutively expressed a high specific activity of SMase extracellularly during batch culture. Maximum SMase activity (555 ± 114 U/mg protein) was with 1.75 M MgCl(2) which was about 50-fold more than that with 10 mM MgCl(2).

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