onr:"swepub:oai:DiVA.org:umu-81875"
Sökning: onr:"swepub:oai:DiVA.org:umu-81875" > Thermus thermophilu...
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| Fältnamn | Indikatorer | Metadata |
|---|---|---|
| 000 | 03968naa a2200361 4500 | |
| 001 | oai:DiVA.org:umu-81875 | |
| 003 | SwePub | |
| 008 | 131022s2004 | |||||||||||000 ||eng| | |
| 024 | 7 | a https://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-818752 URI |
| 024 | 7 | a https://doi.org/10.1128/AEM.70.7.3839-3844.20042 DOI |
| 040 | a (SwePub)umu | |
| 041 | a engb eng | |
| 042 | 9 SwePub | |
| 072 | 7 | a ref2 swepub-contenttype |
| 072 | 7 | a art2 swepub-publicationtype |
| 100 | 1 | a Hidalgo, Aureliou Departamento de Biocatálisis, Instituto de Catálisis y Petroleoquímica-CSIC4 aut |
| 245 | 1 0 | a Thermus thermophilus as a cell factory for the production of a thermophilic Mn-dependent catalase which fails to be synthesized in an active form in Escherichia coli |
| 264 | 1 | c 2004 |
| 338 | a print2 rdacarrier | |
| 520 | a Thermostable Mn-dependent catalases are promising enzymes in biotechnological applications as H(2)O(2)-detoxifying systems. We cloned the genes encoding Mn-dependent catalases from Thermus thermophilus HB27 and HB8 and a less thermostable mutant carrying two amino acid replacements (M129V and E293G). When the wild-type and mutant genes were overexpressed in Escherichia coli, unmodified or six-His-tagged proteins of the expected size were overproduced as inactive proteins. Several attempts to obtain active forms or to activate the overproduced proteins were unsuccessful, even when soluble and thermostable proteins were used. Therefore, a requirement for a Thermus-specific activation factor was suggested. To overcome this problem, the Mn-dependent catalase genes were overexpressed directly in T. thermophilus under the control of the Pnar promoter. This promoter belongs to a respiratory nitrate reductase from of T. thermophilus HB8, whose transcription is activated by the combined action of nitrate and anoxia. Upon induction in T. thermophilus HB8, a 20- to 30-fold increase in catalase specific activity was observed, whereas a 90- to 110-fold increase was detected when the laboratory strain T. thermophilus HB27::nar was used as the host. The thermostability of the overproduced wild-type catalase was identical to that previously reported for the native enzyme, whereas decreased stability was detected for the mutant derivative. Therefore, our results validate the use of T. thermophilus as an alternative cell factory for the overproduction of thermophilic proteins that fail to be expressed in well-known mesophilic hosts. | |
| 650 | 7 | a NATURVETENSKAPx Biologix Mikrobiologi0 (SwePub)106062 hsv//swe |
| 650 | 7 | a NATURAL SCIENCESx Biological Sciencesx Microbiology0 (SwePub)106062 hsv//eng |
| 700 | 1 | a Betancor, Lorenau Departamento de Biocatálisis, Instituto de Catálisis y Petroleoquímica-CSIC4 aut |
| 700 | 1 | a Moreno, Renatau Centro de Biología Molecular 'Severo Ochoa' CSIC-UAM, Campus de Cantoblanco, Madrid, Spain4 aut |
| 700 | 1 | a Zafra, Olgau Centro de Biología Molecular 'Severo Ochoa' CSIC-UAM, Campus de Cantoblanco, Madrid, Spain4 aut |
| 700 | 1 | a Cava, Felipeu Centro de Biología Molecular 'Severo Ochoa' CSIC-UAM, Campus de Cantoblanco, Madrid, Spain4 aut0 (Swepub:umu)feca0003 |
| 700 | 1 | a Fernández-Lafuente, Robertou Departamento de Biocatálisis, Instituto de Catálisis y Petroleoquímica-CSIC4 aut |
| 700 | 1 | a Guisán, José Mu Departamento de Biocatálisis, Instituto de Catálisis y Petroleoquímica-CSIC4 aut |
| 700 | 1 | a Berenguer, Joséu Centro de Biología Molecular 'Severo Ochoa' CSIC-UAM, Campus de Cantoblanco, Madrid, Spain4 aut |
| 710 | 2 | a Departamento de Biocatálisis, Instituto de Catálisis y Petroleoquímica-CSICb Centro de Biología Molecular 'Severo Ochoa' CSIC-UAM, Campus de Cantoblanco, Madrid, Spain4 org |
| 773 | 0 | t Applied and Environmental Microbiologyg 70:7, s. 3839-3844q 70:7<3839-3844x 0099-2240x 1098-5336 |
| 856 | 4 8 | u https://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-81875 |
| 856 | 4 8 | u https://doi.org/10.1128/AEM.70.7.3839-3844.2004 |
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