caa a22 4500 445818743 CHVBK 20180317145237.0 cr unu---uuuuu 170323e20110301xx s 000 0 eng 10.1007/s00792-010-0350-3 doi (NATIONALLICENCE)springer-10.1007/s00792-010-0350-3 Purification and characterization of a hyperthermostable Mn-superoxide dismutase from Thermus thermophilus HB27 [Elektronische Daten] [Jianguo Liu, Mengmeng Yin, Hu Zhu, Jianren Lu, Zhanfeng Cui] 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 1h. 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. Springer, 2010 Superoxide dismutase nationallicence Thermus thermophilus nationallicence Purification nationallicence Enzyme characterization nationallicence Mn-SOD : Manganese superoxide dismutase nationallicence CD : Circular dichroism nationallicence IEF : Isoelectric focusing nationallicence SDS-PAGE : Sodium dodecyl sulfate-polyacrylamide gel electrophoresis nationallicence IgG : Immunoglobulin G nationallicence BSA : Bovine serum albumin nationallicence PES : Polyethersulfone nationallicence MWCO : Molecular weight cut-off nationallicence RC : Regenerated cellulose nationallicence PCR : Polymerase chain reaction nationallicence p I : Isoelectric point nationallicence E. coli : Escherichia coli nationallicence Liu Jianguo Center for Bioengineering and Biotechnology, China University of Petroleum (East China), 266555, Qingdao, People's Republic of China aut Yin Mengmeng Center for Bioengineering and Biotechnology, China University of Petroleum (East China), 266555, Qingdao, People's Republic of China aut Zhu Hu Center for Bioengineering and Biotechnology, China University of Petroleum (East China), 266555, Qingdao, People's Republic of China aut Lu Jianren School of Physics, Manchester University, M60 1QD, Manchester, UK aut Cui Zhanfeng Department of Engineering Science, University of Oxford, OX1 3PJ, Oxford, UK aut Extremophiles Springer Japan 15/2(2011-03-01), 221-226 1431-0651 15:2<221 2011 15 792 https://doi.org/10.1007/s00792-010-0350-3 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s00792-010-0350-3 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Liu Jianguo Center for Bioengineering and Biotechnology, China University of Petroleum (East China), 266555, Qingdao, People's Republic of China aut NATIONALLICENCE 700 1- Yin Mengmeng Center for Bioengineering and Biotechnology, China University of Petroleum (East China), 266555, Qingdao, People's Republic of China aut NATIONALLICENCE 700 1- Zhu Hu Center for Bioengineering and Biotechnology, China University of Petroleum (East China), 266555, Qingdao, People's Republic of China aut NATIONALLICENCE 700 1- Lu Jianren School of Physics, Manchester University, M60 1QD, Manchester, UK aut NATIONALLICENCE 700 1- Cui Zhanfeng Department of Engineering Science, University of Oxford, OX1 3PJ, Oxford, UK aut NATIONALLICENCE 773 0- Extremophiles Springer Japan 15/2(2011-03-01), 221-226 1431-0651 15:2<221 2011 15 792 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer