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- W3005303364 abstract "Abstract The codA gene of Corynebacterium glutamicum PCM 1945 coding for a creatinine deiminase (CDI) (EC 3.5.4.21) has been amplified and cloned. The recombinant strain of Escherichia coli that overproduces the (His) 6 ‐tagged inactive CDI of C. glutamicum as inclusion bodies has been constructed. After solubilization of inclusion bodies in the presence of 0.3% N ‐lauroylsarcosine, the enzyme was renaturated and purified by a single‐step procedure using metal‐affinity chromatography. The yield of the (His) 6 ‐tagged CDI is ~30 mg from 1 L culture. The purified enzyme is sufficiently stable under the conditions designed and possesses an activity of 10–20 U/mg. The main characteristics of the tagged enzyme remained similar to that of the natural enzyme." @default.
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- W3005303364 date "2020-02-19" @default.
- W3005303364 modified "2023-10-18" @default.
- W3005303364 title "Overexpression and one‐step renaturation‐purification of the tagged creatinine deiminase of <i>Corynebacterium glutamicum</i> in <i>Escherichia coli</i> cells" @default.
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- W3005303364 doi "https://doi.org/10.1002/cbin.11320" @default.
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