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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).


Daisuke Sugimori, Yu Tomita, Yusaku Matsumoto, Chiaki Ogino. Extracellular production of a sphingomyelinase from Streptomyces griseocarneus using Streptomyces lividans. Biotechnology letters. 2011 Apr;33(4):727-31

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PMID: 21116683

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