Proteomic analysis of a thermostable superoxide dismutase from Bacillus stearothermophilus TLS33
Thermophilic bacterium Bacillus stearothermophilus TLS33 isolated from a hot spring in Chiang Mai, Thailand produces an extracellular superoxide dismutase (SOD). SOD is a free radical metabolizing enzyme that protects the cell membrane from damage by the highly reactive superoxide free radicals. To...
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2014
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th-cmuir.6653943832-55202014-08-30T02:56:38Z Proteomic analysis of a thermostable superoxide dismutase from Bacillus stearothermophilus TLS33 Sookkheo B. Sinchaikul S. Thannan H. Thongprasong O. Phutrakul S. Chen S.-T. Thermophilic bacterium Bacillus stearothermophilus TLS33 isolated from a hot spring in Chiang Mai, Thailand produces an extracellular superoxide dismutase (SOD). SOD is a free radical metabolizing enzyme that protects the cell membrane from damage by the highly reactive superoxide free radicals. To identify the secreted SOD, we used the systematically proteomic approaches of two-dimensional polyacrylamide gel electrophoresis (2-D PAGE) analysis and database searching. The bacterium was grown in a medium containing 0.1% w/v yeast extract and 0.1% w/v tryptone in 100% v/v base mixture at 65°C for 72 h, by assessing their growth by protein and SOD activity. The bacterium produced the highest SOD activity at 65°C for 48 h and the extracellular SOD was run on 2-D PAGE using broad range pH 3-10 immobilized pH gradients (IPGs) and narrow range pH 4-7 IPGs. The isoelectric point and molecular mass of the extracellular SOD were approximately 5.8 and 28 kDa, respectively. In addition, the NH2-terminal amino acid sequence was found to be P-F-E-L-P-A-L-P-Y-P-Y-D-A-L-E-P-P-I-I-D, which had a homology of approximately 85% to the Mn-SOD family and 65% to the Fe-SOD family. 2014-08-30T02:56:38Z 2014-08-30T02:56:38Z 2002 Conference Paper 16159853 10.1002/1615-9861(200209)2:9<1311::AID-PROT1311>3.0.CO;2-U 12362349 PROTC http://www.scopus.com/inward/record.url?eid=2-s2.0-0036744433&partnerID=40&md5=92a76ee7cbddc6a362e9d3d56997727b http://cmuir.cmu.ac.th/handle/6653943832/5520 English |
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Thermophilic bacterium Bacillus stearothermophilus TLS33 isolated from a hot spring in Chiang Mai, Thailand produces an extracellular superoxide dismutase (SOD). SOD is a free radical metabolizing enzyme that protects the cell membrane from damage by the highly reactive superoxide free radicals. To identify the secreted SOD, we used the systematically proteomic approaches of two-dimensional polyacrylamide gel electrophoresis (2-D PAGE) analysis and database searching. The bacterium was grown in a medium containing 0.1% w/v yeast extract and 0.1% w/v tryptone in 100% v/v base mixture at 65°C for 72 h, by assessing their growth by protein and SOD activity. The bacterium produced the highest SOD activity at 65°C for 48 h and the extracellular SOD was run on 2-D PAGE using broad range pH 3-10 immobilized pH gradients (IPGs) and narrow range pH 4-7 IPGs. The isoelectric point and molecular mass of the extracellular SOD were approximately 5.8 and 28 kDa, respectively. In addition, the NH2-terminal amino acid sequence was found to be P-F-E-L-P-A-L-P-Y-P-Y-D-A-L-E-P-P-I-I-D, which had a homology of approximately 85% to the Mn-SOD family and 65% to the Fe-SOD family. |
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Conference or Workshop Item |
author |
Sookkheo B. Sinchaikul S. Thannan H. Thongprasong O. Phutrakul S. Chen S.-T. |
spellingShingle |
Sookkheo B. Sinchaikul S. Thannan H. Thongprasong O. Phutrakul S. Chen S.-T. Proteomic analysis of a thermostable superoxide dismutase from Bacillus stearothermophilus TLS33 |
author_facet |
Sookkheo B. Sinchaikul S. Thannan H. Thongprasong O. Phutrakul S. Chen S.-T. |
author_sort |
Sookkheo B. |
title |
Proteomic analysis of a thermostable superoxide dismutase from Bacillus stearothermophilus TLS33 |
title_short |
Proteomic analysis of a thermostable superoxide dismutase from Bacillus stearothermophilus TLS33 |
title_full |
Proteomic analysis of a thermostable superoxide dismutase from Bacillus stearothermophilus TLS33 |
title_fullStr |
Proteomic analysis of a thermostable superoxide dismutase from Bacillus stearothermophilus TLS33 |
title_full_unstemmed |
Proteomic analysis of a thermostable superoxide dismutase from Bacillus stearothermophilus TLS33 |
title_sort |
proteomic analysis of a thermostable superoxide dismutase from bacillus stearothermophilus tls33 |
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2014 |
url |
http://www.scopus.com/inward/record.url?eid=2-s2.0-0036744433&partnerID=40&md5=92a76ee7cbddc6a362e9d3d56997727b http://cmuir.cmu.ac.th/handle/6653943832/5520 |
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1681420441145573376 |