Over-expression system for secretory phospholipase D by<Emphasis Type="Italic"> Streptomyces lividans</Emphasis> |
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| Authors: | C?Ogino M?Kanemasu Y?Hayashi A?Kondo N?Shimizu S?Tokuyama Y?Tahara S?Kuroda K?Tanizawa Email author" target="_blank">H?FukudaEmail author |
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| Institution: | (1) Division of Molecular Science, Graduate School of Science and Technology, Kobe University, 1–1 Rokkodai, Nada, 657–8501 Kobe, Japan;(2) Department of Chemistry and Chemical Engineering, Faculty of Engineering, Kanazawa University, 2–40–20 Kodatsuno, 920–8667 Kanazawa, Japan;(3) Department of Chemical Science and Engineering, Faculty of Engineering, Kobe University, 1–1 Rokkodai, Nada, 657–8501 Kobe, Japan;(4) Department of Applied Biological Chemistry, Faculty of Agriculture, Shizuoka University, 836 Ohya, 422–8529 Shizuoka, Japan;(5) Department of Structural Molecular Biology, Institute of Scientific and Industrial Research, Osaka University, 8–1 Mihogaoka, 567–0047 Ibaraki, Japan |
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| Abstract: | The structural gene for phospholipase D (PLD) of an actinomycete, Streptoverticillium cinnamoneum, together with its promoter region was introduced into Streptomyces lividans using a shuttle vector—pUC702—for Escherichia coli and S. lividans. The transformant was found to secrete a large amount of PLD (about 2.0×104 U/l, 42 mg/l) when cultured in a jar fermentor. Both an initial glucose concentration of 17.5 g/l and the feeding of carbon and nitrogen sources are effective for efficient secretion of PLD; under these culture conditions, the amount of PLD secreted reached a maximum level (about 5.5×104 U/l, 118 mg/l) after about 60 h. In contrast to the original producer, Stv. cinnamoneum, which secretes only a small amount of PLD (about 1.1×103 U/l, 2 mg/l) along with other extracellular proteins, this heterologous expression system is markedly more efficient in production of secretory PLD. |
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