A glutathione peroxidase from Antarctic psychrotrophic bacterium<i>Pseudoalteromonas</i>sp. ANT506: Cloning and heterologous expression of the gene and characterization of recombinant enzyme

Wang, Yatong; Han, Han; Cui, Bingqing; Hou, Yanhua; Wang, Yifan; Wang, Quanfu

doi:10.1080/21655979.2017.1373534

Cited by 15 publications

(12 citation statements)

References 26 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Antarctic sea ice microorganisms would be a novel source of antioxidant enzymes. Based on our recent studies, several cold-active antioxidant proteins were separated from Antarctic sea ice microorganisms and widely used in industrial sectors due to their excellent biochemical properties [16,17]. Halomonas is the type genus of the family Halomonadaceae belonging to the class Gammaproteobacteria.…”

Section: Introductionmentioning

confidence: 99%

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

et al. 2019

Self Cite

View full text Add to dashboard Cite

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.

show abstract

Section: Introductionmentioning

confidence: 99%

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

et al. 2019

Self Cite

View full text Add to dashboard Cite

show abstract

“…The residual activity in the treated and control samples were plotted against the time of exposure for treatment as relative activity. The control samples were considered as 100% activity (Shi et al, 2014;Wang et al, 2017). Each measurement represented the mean of three repeated experiments.…”

Section: Purification and Characterization Of Gst And Gpx Enzymesmentioning

confidence: 99%

Stress-Based Production, and Characterization of Glutathione Peroxidase and Glutathione S-Transferase Enzymes From Lactobacillus plantarum

Al-Madboly

Ali

Fakharany

et al. 2020

Front. Bioeng. Biotechnol.

View full text Add to dashboard Cite

More attention has been recently directed toward glutathione peroxidase and s-transferase enzymes because of the great importance they hold with respect to their applications in the pharmaceutical field. This work was conducted to optimize the production and characterize glutathione peroxidase and glutathione s-transferase produced by Lactobacillus plantarum KU720558 using Plackett-Burman and Box-Behnken statistical designs. To assess the impact of the culture conditions on the microbial production of the enzymes, colorimetric methods were used. Following data analysis, the optimum conditions that enhanced the s-transferase yield were the De Man-Rogosa-Sharp (MRS) broth as a basal medium supplemented with 0.1% urea, 0.075% H 2 O 2 , 0.5% 1-butanol, 0.0125% amino acids, and 0.05% SDS at pH 6.0 and anaerobically incubated for 24 h at 40 • C. The optimum s-transferase specific activity was 1789.5 U/mg of protein, which was ∼12 times the activity of the basal medium. For peroxidase, the best medium composition was 0.17% urea, 0.025% bile salt, 7.5% Na Cl, 0.05% H 2 O 2 , 0.05% SDS, and 2% ethanol added to the MRS broth at pH 6.0 and anaerobically incubated for 24 h at 40 • C. Furthermore, the optimum peroxidase specific activity was 612.5 U/mg of protein, indicating that its activity was 22 times higher than the activity recorded in the basal medium. After SDS-PAGE analysis, GST and GPx showed a single protein band of 25 and 18 kDa, respectively. They were able to retain their activities at an optimal temperature of 40 • C for an hour and pH range 4-7. The 3D model of both enzymes was constructed showing helical structures, sheet and loops. Protein cavities were also detected to define druggable sites. GST model had two large pockets; 185Å3 and 71 Å3 with druggability score 0.5-0.8. For GPx, the pockets were relatively Al-Madboly et al.Enzymes Production From Lactobacillus plantarum smaller, 71 Å3 and 32 Å3 with druggability score (0.65-0.66). Therefore, the present study showed that the consortium components as well as the stress-based conditions used could express both enzymes with enhanced productivity, recommending their application based on the obtained results.

show abstract

“…The crystal structure of a Fe-superoxide dismutase, Fe-SOD (EC 1.15.1.1) isolated from the marine P. haloplanktis , revelead that cold-adapted enzyme displays high catalysis at low temperature increasing the flexibility of its active site without modifying the overall structure [161]. SODs have been used in the pharmaceutical and cosmetic industries, food, agricultural, and chemical industries [169]. Antioxidant defense is an important component of evolutionary adaptations in the cold to face increased levels of reactive oxygen species (ROS).…”

Section: Cold-adapted Enzymes and Their Biotechnological Applicationsmentioning

confidence: 99%

Enzymes from Marine Polar Regions and Their Biotechnological Applications

et al. 2019

View full text Add to dashboard Cite

The microorganisms that evolved at low temperatures express cold-adapted enzymes endowed with unique catalytic properties in comparison to their mesophilic homologues, i.e., higher catalytic efficiency, improved flexibility, and lower thermal stability. Cold environments are therefore an attractive research area for the discovery of enzymes to be used for investigational and industrial applications in which such properties are desirable. In this work, we will review the literature on cold-adapted enzymes specifically focusing on those discovered in the bioprospecting of polar marine environments, so far largely neglected because of their limited accessibility. We will discuss their existing or proposed biotechnological applications within the framework of the more general applications of cold-adapted enzymes.

show abstract

A glutathione peroxidase from Antarctic psychrotrophic bacteriumPseudoalteromonassp. ANT506: Cloning and heterologous expression of the gene and characterization of recombinant enzyme

Cited by 15 publications

References 26 publications

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

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

Stress-Based Production, and Characterization of Glutathione Peroxidase and Glutathione S-Transferase Enzymes From Lactobacillus plantarum

Enzymes from Marine Polar Regions and Their Biotechnological Applications

Contact Info

Product

Resources

About