Extracellular production of a sphingomyelinase from <Emphasis Type="Italic">Streptomyces griseocarneus</Emphasis> using <Emphasis Type="Italic">Streptomyces lividans</Emphasis> |
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| Authors: | Daisuke Sugimori Yu Tomita Yusaku Matsumoto Chiaki Ogino |
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| Institution: | (1) Department of Symbiotic Systems Science and Technology, Graduate School of Symbiotic Systems Science and Technology, Fukushima University, 1 Kanayagawa, Fukushima 960-1296, Japan;(2) Department of Chemical Science and Engineering, Graduate School of Technology, Kobe University, 1–1 Rokkodaicho, Nada, Kobe 657-8501, Japan |
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| 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 MgCl2 which was about 50-fold more than that with 10 mM MgCl2. |
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