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| Content Provider | Springer Nature Link |
|---|---|
| Author | Večerek, B. Marešová, H. Kočavá, M. Kyslík, P. |
| Copyright Year | 2003 |
| Abstract | A cDNA of a structural gene encoding pyranose 2-oxidase (P2O) from Trametes ochracea strain MB49 was cloned into Escherichia coli strain BL21(DE3) on a multicopy plasmid under the control of the trc promoter. Synthesis of P2O was studied in batch cultures in LB or M9-based mineral medium at 28°C. While there was a low specific activity of P2O in LB medium, the enzyme was synthesised constitutively in mineral medium and represented 3% of the cell soluble protein (0.3 U mg−1). The effect of isopropyl β-d-thiogalactoside on the expression of P2O was studied in mineral medium at 25 and 28°C. The synthesis of P2O at 28°C corresponded to 39% of the cell soluble protein but the major portion of P2O (93%) was in the form of non-active inclusion bodies (activity of P2O equalled 0.19 U mg−1). At 25°C, the amount of P2O represented 14% of the cell soluble protein and the activity of P2O was 1.1 U mg−1. The soluble enzyme represented 70% of the total amount of P2O. |
| Starting Page | 525 |
| Ending Page | 530 |
| Page Count | 6 |
| File Format | |
| ISSN | 01757598 |
| Journal | Applied Microbiology and Biotechnology |
| Volume Number | 64 |
| Issue Number | 4 |
| e-ISSN | 14320614 |
| Language | English |
| Publisher | Springer-Verlag |
| Publisher Date | 2003-12-20 |
| Publisher Place | Berlin, Heidelberg |
| Access Restriction | Subscribed |
| Content Type | Text |
| Resource Type | Article |
| Subject | Medicine Applied Microbiology and Biotechnology Biotechnology |
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