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

Journal article

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.

Authors: Liu, J; Yin, M; Zhu, H; Lu, J; Cui, Z

• Publication status: Published
• Journal: Extremophiles : life under extreme conditions
• Volume: 15
• Issue: 2
• Pages: 221-226
• Publication date: 2011-03-01
• DOI: 10.1007/s00792-010-0350-3
• EISSN: 1433-4909
• ISSN: 1431-0651
• Language: English
• Keywords: Superoxide Dismutase; Molecular Weight; Ferritins; Circular Dichroism; Metals; Protein Structure, Secondary; Temperature; Ions; Isoelectric Point; Electrophoresis, Polyacrylamide Gel; Isoelectric Focusing; Thermus thermophilus; Kinetics; Hydrogen-Ion Concentration