Purification and characterization of a psychrophilic catalase from Antarctic Bacillus
Catalase from Bacillus sp. N2a (BNC) isolated from Antarctic seawater was purified to homogeneity. BNC has a molecular mass of about 230 kDa and is composed of four identical subunits of 56 kDa. The catalase showed optimal activity at 25 °C and at a pH range of 6–11. The enzyme could be inhibited by...
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crcansciencepubl:10.1139/w08-066 2024-06-23T07:47:05+00:00 Purification and characterization of a psychrophilic catalase from Antarctic Bacillus Wang, Wei Sun, Mi Liu, Wanshun Zhang, Bin 2008 http://dx.doi.org/10.1139/w08-066 http://www.nrcresearchpress.com/doi/full-xml/10.1139/W08-066 http://www.nrcresearchpress.com/doi/pdf/10.1139/W08-066 en eng Canadian Science Publishing http://www.nrcresearchpress.com/page/about/CorporateTextAndDataMining Canadian Journal of Microbiology volume 54, issue 10, page 823-828 ISSN 0008-4166 1480-3275 journal-article 2008 crcansciencepubl https://doi.org/10.1139/w08-066 2024-06-13T04:10:51Z Catalase from Bacillus sp. N2a (BNC) isolated from Antarctic seawater was purified to homogeneity. BNC has a molecular mass of about 230 kDa and is composed of four identical subunits of 56 kDa. The catalase showed optimal activity at 25 °C and at a pH range of 6–11. The enzyme could be inhibited by azide, hydroxylamine, and mercaptoethanol. These characteristics suggested that BNC is a small-subunit monofunctional catalase. The activation energy of BNC was 13 kJ/mol and the apparent k cat /K m values were 3.6 × 10 6 and 4 × 10 6 L·mol –1 ·s –1 at 4 and 25 °C, respectively. High catalytic efficiency of BNC at low temperatures enables this bacterium to scavenge H 2 O 2 efficiently. BNC exhibited activation energy, catalytic efficiency, and thermostability comparable with some mesophilic homologues. Such similarity of enzymatic characteristics to mesophilic homologues, although uncommon among the cold-adapted enzymes in general, has also been observed in other psychrophilic small-subunit monofunctional catalases. Article in Journal/Newspaper Antarc* Antarctic Canadian Science Publishing Antarctic Canadian Journal of Microbiology 54 10 823 828 |
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Open Polar |
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Canadian Science Publishing |
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crcansciencepubl |
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English |
description |
Catalase from Bacillus sp. N2a (BNC) isolated from Antarctic seawater was purified to homogeneity. BNC has a molecular mass of about 230 kDa and is composed of four identical subunits of 56 kDa. The catalase showed optimal activity at 25 °C and at a pH range of 6–11. The enzyme could be inhibited by azide, hydroxylamine, and mercaptoethanol. These characteristics suggested that BNC is a small-subunit monofunctional catalase. The activation energy of BNC was 13 kJ/mol and the apparent k cat /K m values were 3.6 × 10 6 and 4 × 10 6 L·mol –1 ·s –1 at 4 and 25 °C, respectively. High catalytic efficiency of BNC at low temperatures enables this bacterium to scavenge H 2 O 2 efficiently. BNC exhibited activation energy, catalytic efficiency, and thermostability comparable with some mesophilic homologues. Such similarity of enzymatic characteristics to mesophilic homologues, although uncommon among the cold-adapted enzymes in general, has also been observed in other psychrophilic small-subunit monofunctional catalases. |
format |
Article in Journal/Newspaper |
author |
Wang, Wei Sun, Mi Liu, Wanshun Zhang, Bin |
spellingShingle |
Wang, Wei Sun, Mi Liu, Wanshun Zhang, Bin Purification and characterization of a psychrophilic catalase from Antarctic Bacillus |
author_facet |
Wang, Wei Sun, Mi Liu, Wanshun Zhang, Bin |
author_sort |
Wang, Wei |
title |
Purification and characterization of a psychrophilic catalase from Antarctic Bacillus |
title_short |
Purification and characterization of a psychrophilic catalase from Antarctic Bacillus |
title_full |
Purification and characterization of a psychrophilic catalase from Antarctic Bacillus |
title_fullStr |
Purification and characterization of a psychrophilic catalase from Antarctic Bacillus |
title_full_unstemmed |
Purification and characterization of a psychrophilic catalase from Antarctic Bacillus |
title_sort |
purification and characterization of a psychrophilic catalase from antarctic bacillus |
publisher |
Canadian Science Publishing |
publishDate |
2008 |
url |
http://dx.doi.org/10.1139/w08-066 http://www.nrcresearchpress.com/doi/full-xml/10.1139/W08-066 http://www.nrcresearchpress.com/doi/pdf/10.1139/W08-066 |
geographic |
Antarctic |
geographic_facet |
Antarctic |
genre |
Antarc* Antarctic |
genre_facet |
Antarc* Antarctic |
op_source |
Canadian Journal of Microbiology volume 54, issue 10, page 823-828 ISSN 0008-4166 1480-3275 |
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http://www.nrcresearchpress.com/page/about/CorporateTextAndDataMining |
op_doi |
https://doi.org/10.1139/w08-066 |
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Canadian Journal of Microbiology |
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54 |
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10 |
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823 |
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828 |
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1802650754618490880 |