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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 exclusion chromatography and sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The final purified enzyme had an isoelectric point of 6.2 and a high α-helical content of 70%, consistent with the theoretical values. This showed that the purified SOD folded with a reasonable secondary structure.

Original publication

DOI

10.1007/s00792-010-0350-3

Type

Journal article

Journal

Extremophiles

Publication Date

03/2011

Volume

15

Pages

221 - 226

Keywords

Circular Dichroism, Electrophoresis, Polyacrylamide Gel, Ferritins, Hydrogen-Ion Concentration, Ions, Isoelectric Focusing, Isoelectric Point, Kinetics, Metals, Molecular Weight, Protein Structure, Secondary, Superoxide Dismutase, Temperature, Thermus thermophilus