Cold-Adapted Glutathione S-Transferases from Antarctic Psychrophilic Bacterium Halomonas sp. ANT108: Heterologous Expression, Characterization, and Oxidative Resistance
Glutathione S-transferases are one of the most important antioxidant enzymes to protect against oxidative damage induced by reactive oxygen species. In this study, a novel gst gene, designated as hsgst, was derived from Antarctic sea ice bacterium Halomonas sp. ANT108 and expressed in Escherichia co...
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ftdoajarticles:oai:doaj.org/article:fdd5e9d76b94414384e54cab72414a9e 2023-05-15T14:02:16+02:00 Cold-Adapted Glutathione S-Transferases from Antarctic Psychrophilic Bacterium Halomonas sp. ANT108: Heterologous Expression, Characterization, and Oxidative Resistance Yanhua Hou Chenhui Qiao Yifan Wang Yatong Wang Xiulian Ren Qifeng Wei Quanfu Wang 2019-03-01T00:00:00Z https://doi.org/10.3390/md17030147 https://doaj.org/article/fdd5e9d76b94414384e54cab72414a9e EN eng MDPI AG http://www.mdpi.com/1660-3397/17/3/147 https://doaj.org/toc/1660-3397 1660-3397 doi:10.3390/md17030147 https://doaj.org/article/fdd5e9d76b94414384e54cab72414a9e Marine Drugs, Vol 17, Iss 3, p 147 (2019) glutathione S-transferases cold-adapted Antarctic antioxidant defense homology modeling Biology (General) QH301-705.5 article 2019 ftdoajarticles https://doi.org/10.3390/md17030147 2022-12-30T20:09:41Z Glutathione S-transferases are one of the most important antioxidant enzymes to protect against oxidative damage induced by reactive oxygen species. In this study, a novel gst gene, designated as hsgst, was derived from Antarctic sea ice bacterium Halomonas sp. ANT108 and expressed in Escherichia coli (E. coli) BL21. The hsgst gene was 603 bp in length and encoded a protein of 200 amino acids. Compared with the mesophilic EcGST, homology modeling indicated HsGST had some structural characteristics of cold-adapted enzymes, such as higher frequency of glycine residues, lower frequency of proline and arginine residues, and reduced electrostatic interactions, which might be in relation to the high catalytic efficiency at low temperature. The recombinant HsGST (rHsGST) was purified to apparent homogeneity with Ni-affinity chromatography and its biochemical properties were investigated. The specific activity of the purified rHsGST was 254.20 nmol/min/mg. The optimum temperature and pH of enzyme were 25 °C and 7.5, respectively. Most importantly, rHsGST retained 41.67% of its maximal activity at 0 °C. 2.0 M NaCl and 0.2% H2O2 had no effect on the enzyme activity. Moreover, rHsGST exhibited its protective effects against oxidative stresses in E. coli cells. Due to its high catalytic efficiency and oxidative resistance at low temperature, rHsGST may be a potential candidate as antioxidant in low temperature health foods. Article in Journal/Newspaper Antarc* Antarctic Sea ice Directory of Open Access Journals: DOAJ Articles Antarctic Marine Drugs 17 3 147 |
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Open Polar |
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Directory of Open Access Journals: DOAJ Articles |
op_collection_id |
ftdoajarticles |
language |
English |
topic |
glutathione S-transferases cold-adapted Antarctic antioxidant defense homology modeling Biology (General) QH301-705.5 |
spellingShingle |
glutathione S-transferases cold-adapted Antarctic antioxidant defense homology modeling Biology (General) QH301-705.5 Yanhua Hou Chenhui Qiao Yifan Wang Yatong Wang Xiulian Ren Qifeng Wei Quanfu Wang Cold-Adapted Glutathione S-Transferases from Antarctic Psychrophilic Bacterium Halomonas sp. ANT108: Heterologous Expression, Characterization, and Oxidative Resistance |
topic_facet |
glutathione S-transferases cold-adapted Antarctic antioxidant defense homology modeling Biology (General) QH301-705.5 |
description |
Glutathione S-transferases are one of the most important antioxidant enzymes to protect against oxidative damage induced by reactive oxygen species. In this study, a novel gst gene, designated as hsgst, was derived from Antarctic sea ice bacterium Halomonas sp. ANT108 and expressed in Escherichia coli (E. coli) BL21. The hsgst gene was 603 bp in length and encoded a protein of 200 amino acids. Compared with the mesophilic EcGST, homology modeling indicated HsGST had some structural characteristics of cold-adapted enzymes, such as higher frequency of glycine residues, lower frequency of proline and arginine residues, and reduced electrostatic interactions, which might be in relation to the high catalytic efficiency at low temperature. The recombinant HsGST (rHsGST) was purified to apparent homogeneity with Ni-affinity chromatography and its biochemical properties were investigated. The specific activity of the purified rHsGST was 254.20 nmol/min/mg. The optimum temperature and pH of enzyme were 25 °C and 7.5, respectively. Most importantly, rHsGST retained 41.67% of its maximal activity at 0 °C. 2.0 M NaCl and 0.2% H2O2 had no effect on the enzyme activity. Moreover, rHsGST exhibited its protective effects against oxidative stresses in E. coli cells. Due to its high catalytic efficiency and oxidative resistance at low temperature, rHsGST may be a potential candidate as antioxidant in low temperature health foods. |
format |
Article in Journal/Newspaper |
author |
Yanhua Hou Chenhui Qiao Yifan Wang Yatong Wang Xiulian Ren Qifeng Wei Quanfu Wang |
author_facet |
Yanhua Hou Chenhui Qiao Yifan Wang Yatong Wang Xiulian Ren Qifeng Wei Quanfu Wang |
author_sort |
Yanhua Hou |
title |
Cold-Adapted Glutathione S-Transferases from Antarctic Psychrophilic Bacterium Halomonas sp. ANT108: Heterologous Expression, Characterization, and Oxidative Resistance |
title_short |
Cold-Adapted Glutathione S-Transferases from Antarctic Psychrophilic Bacterium Halomonas sp. ANT108: Heterologous Expression, Characterization, and Oxidative Resistance |
title_full |
Cold-Adapted Glutathione S-Transferases from Antarctic Psychrophilic Bacterium Halomonas sp. ANT108: Heterologous Expression, Characterization, and Oxidative Resistance |
title_fullStr |
Cold-Adapted Glutathione S-Transferases from Antarctic Psychrophilic Bacterium Halomonas sp. ANT108: Heterologous Expression, Characterization, and Oxidative Resistance |
title_full_unstemmed |
Cold-Adapted Glutathione S-Transferases from Antarctic Psychrophilic Bacterium Halomonas sp. ANT108: Heterologous Expression, Characterization, and Oxidative Resistance |
title_sort |
cold-adapted glutathione s-transferases from antarctic psychrophilic bacterium halomonas sp. ant108: heterologous expression, characterization, and oxidative resistance |
publisher |
MDPI AG |
publishDate |
2019 |
url |
https://doi.org/10.3390/md17030147 https://doaj.org/article/fdd5e9d76b94414384e54cab72414a9e |
geographic |
Antarctic |
geographic_facet |
Antarctic |
genre |
Antarc* Antarctic Sea ice |
genre_facet |
Antarc* Antarctic Sea ice |
op_source |
Marine Drugs, Vol 17, Iss 3, p 147 (2019) |
op_relation |
http://www.mdpi.com/1660-3397/17/3/147 https://doaj.org/toc/1660-3397 1660-3397 doi:10.3390/md17030147 https://doaj.org/article/fdd5e9d76b94414384e54cab72414a9e |
op_doi |
https://doi.org/10.3390/md17030147 |
container_title |
Marine Drugs |
container_volume |
17 |
container_issue |
3 |
container_start_page |
147 |
_version_ |
1766272427622400000 |