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...

Full description

Bibliographic Details
Published in:Marine Drugs
Main Authors: Yanhua Hou, Chenhui Qiao, Yifan Wang, Yatong Wang, Xiulian Ren, Qifeng Wei, Quanfu Wang
Format: Article in Journal/Newspaper
Language:English
Published: MDPI AG 2019
Subjects:
Online Access:https://doi.org/10.3390/md17030147
https://doaj.org/article/fdd5e9d76b94414384e54cab72414a9e
id ftdoajarticles:oai:doaj.org/article:fdd5e9d76b94414384e54cab72414a9e
record_format openpolar
spelling 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
institution Open Polar
collection 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