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Purification and characterization of a hyperthermostable Mn-superoxide dismutase from Thermus thermophilus HB27.

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...

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Publication status:
Published

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Publisher copy:
10.1007/s00792-010-0350-3

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Institution:
University of Oxford
Department:
Oxford, MPLS, Engineering Science
Role:
Author
Journal:
Extremophiles : life under extreme conditions
Volume:
15
Issue:
2
Pages:
221-226
Publication date:
2011-03-05
DOI:
EISSN:
1433-4909
ISSN:
1431-0651
URN:
uuid:023a713f-298e-49db-8f03-00a368d89bb2
Source identifiers:
146588
Local pid:
pubs:146588

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