- Abstract:
-
Thermostable Mn-dependent catalases are promising enzymes in biotechnological applications. In the present study, a Mn-containing superoxide dismutase of the hyperthermophilic Thermus thermophilus HB27 had been purified and characterized by a two-stage ultrafiltration process after being expressed in E. coli. The enzyme was highly stable at 90°C and retained 57% activity after heat treatment at 100°C for 1 h. The native form of the enzyme was determined as a homotetramer by analytical size ex...
Expand abstract - Publication status:
- Published
- Publisher copy:
- 10.1007/s00792-010-0350-3
-
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- Journal:
- Extremophiles : life under extreme conditions
- Volume:
- 15
- Issue:
- 2
- Pages:
- 221-226
- Publication date:
- 2011-03-05
- DOI:
- EISSN:
-
1433-4909
- ISSN:
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1431-0651
- URN:
-
uuid:023a713f-298e-49db-8f03-00a368d89bb2
- Source identifiers:
-
146588
- Local pid:
- pubs:146588
- Copyright date:
- 2011
Journal article
Purification and characterization of a hyperthermostable Mn-superoxide dismutase from Thermus thermophilus HB27.
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