Next Article in Journal
High-Performance Thin-Layer Chromatography Hyphenated with Microchemical and Biochemical Derivatizations in Bioactivity Profiling of Marine Species
Next Article in Special Issue
Protective Effect of Phloroglucinol on Oxidative Stress-Induced DNA Damage and Apoptosis through Activation of the Nrf2/HO-1 Signaling Pathway in HaCaT Human Keratinocytes
Previous Article in Journal
Comparison of the Sulfonamide Inhibition Profiles of the α-Carbonic Anhydrase Isoforms (SpiCA1, SpiCA2 and SpiCA3) Encoded by the Genome of the Scleractinian Coral Stylophora pistillata
Previous Article in Special Issue
Effect of Fermented Fish Oil on Fine Particulate Matter-Induced Skin Aging
Open AccessArticle

Cold-Adapted Glutathione S-Transferases from Antarctic Psychrophilic Bacterium Halomonas sp. ANT108: Heterologous Expression, Characterization, and Oxidative Resistance

School of Marine Science and Technology, Harbin Institute of Technology, Weihai 264209, China
*
Author to whom correspondence should be addressed.
Mar. Drugs 2019, 17(3), 147; https://doi.org/10.3390/md17030147
Received: 22 January 2019 / Revised: 20 February 2019 / Accepted: 25 February 2019 / Published: 1 March 2019
(This article belongs to the Special Issue Marine Antioxidant)
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. View Full-Text
Keywords: glutathione S-transferases; cold-adapted; Antarctic; antioxidant defense; homology modeling glutathione S-transferases; cold-adapted; Antarctic; antioxidant defense; homology modeling
Show Figures

Figure 1

MDPI and ACS Style

Hou, Y.; Qiao, C.; Wang, Y.; Wang, Y.; Ren, X.; Wei, Q.; Wang, Q. Cold-Adapted Glutathione S-Transferases from Antarctic Psychrophilic Bacterium Halomonas sp. ANT108: Heterologous Expression, Characterization, and Oxidative Resistance. Mar. Drugs 2019, 17, 147.

Show more citation formats Show less citations formats
Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Article Access Map by Country/Region

1
Back to TopTop