Purification and partial characterization of recombinant Cu, Zn containing superoxide dismutase of Cordyceps militaris in E. coli

Wang, Zunsheng; He, Zhimin; Shen, Qiong; Gu, Yun; Li, Suxia; Qin-sheng, Yuan

doi:10.1016/j.jchromb.2005.08.010

Cited by 11 publications

(10 citation statements)

References 37 publications

(54 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…This value of pH was selected because it proved to give a stable environment for the enzyme activity preservation; at pH >8 the activity started to decrease significantly. This is consistent with other publications; generally pH values are set between 7 and 8 for SOD adsorption onto anion exchange resins . The adsorption results obtained for the seven anion exchange resins are shown in Table , high binding capacities were observed for four resins: Q Sepharose™ XL, Streamline™ Q XL, Streamline™ DEAE and Amberlite™ IRA‐96, but only two resins were selected for further analysis: Amberlite™ IRA‐96 (weak anion exchange) because of its inexpensiveness; and Q Sepharose™ XL (strong anion exchange), since it showed the highest SOD binding capacity (Fig.…”

Section: Resultssupporting

confidence: 88%

“…In the case of the recombinant enzyme, the authors achieved a global 85% yield, which is very similar to our recovery (84%), but they attained a 6.1‐fold purification, eleven times lower, compared with the result from the present study. When purifying the native enzyme, the yield was much lower (17.6%), but with greater purification (264.9) . The difference in the purification factors from the latter two processes relies on the mass ratio of SOD/contaminants, as the recombinant SOD is overexpressed, the mentioned ratio is higher, so there are less contaminants to remove per milligram of enzyme compared with the case in which the native SOD is purified, that is why the purification attained in the second case is so high.…”

Section: Resultsmentioning

confidence: 99%

“…Wang et al . used anion exchange chromatography, cation exchange chromatography and size exclusion chromatography . Finally, Kim et al .…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

A novel process for the recovery of superoxide dismutase from yeast exploiting electroextraction coupled to direct sorption

Simental-Martínez

Vennapusa

Benavides

et al. 2013

J of Chemical Tech & Biotech

View full text Add to dashboard Cite

show abstract

Section: Resultssupporting

confidence: 88%

Section: Resultsmentioning

confidence: 99%

See 1 more Smart Citation

A novel process for the recovery of superoxide dismutase from yeast exploiting electroextraction coupled to direct sorption

Simental-Martínez

Vennapusa

Benavides

et al. 2013

J of Chemical Tech & Biotech

View full text Add to dashboard Cite

show abstract

“…Lesser than pH 4.0 or greater than pH 9.0, the activity declined rapidly. Ideally pH range of SOD from garlic is about in the range of pH 4.0–9.0 is much better than that of Cu–Zn–SOD from entomogenous fungal species Cordyceps militaris range from pH 8.2 to 8.8 (Wang et al, ).…”

Section: Resultsmentioning

confidence: 99%

Juglans regia and Ribes nigrum as potential nutraceuticals: Source of thermostable superoxide dismutase enzyme

et al. 2019

View full text Add to dashboard Cite

In the present study, superoxide dismutase (SOD) extracted from dry fruits; Juglans regia (Walnut; W) and Ribes nigrum (Munakka; M) was partially purified into 0%–40% and 40%–80% fractions based on ammonium sulfate saturation levels. The partially purified fractions (0%–40%) exhibited purification level of 3.09‐ (W) and 3.22‐ (M) fold with specific activity 79.32 Umg−1 (W) and 125.23 Umg−1 (M). SOD from both the sources was found to be thermally stable, that is, 80°C (W) and 70°C (M). Kinetic studies showed Km values to be 3.33 mM (W) and 2.86 mM (M), whereas the activation energy (Ea) calculated as 24.52 KJ mol−1 (W) and 26.25 KJ mol−1 (M). Na+, Mn2+, and Ba2+ ions acted as potential inhibitors, whereas Fe2+ stimulated SOD from both the sources. Among these metal ions, Na+ exhibited uncompetitive inhibition in both cases; with Ki values of 0.7 mM (W) and 0.9 mM (M), suggesting the more prominent binding affinity and effectiveness. Practical applications Awareness need to be created among people for multifactorial health benefits of nutraceuticals in day‐to‐day life. Nutritional consumption from fruits, nuts, and vegetables safeguard against various maladies like cardiovascular diseases, diabetes, and cancers. Superoxide dismutase (EC 1.15.1.1) is a standout among the most critical metal‐containing enzymes that act as a main line of defense against oxidative stress. Antioxidant‐based drugs and formulations have been developed in the recent years and research is emphasized on its impact on oxidative stress levels. In this study, Juglans regia (W) and Ribes nigrum (M) were found to have thermostable SOD enzyme with excellent antioxidant properties. Thermal stability of an enzyme improves its significance making it industry friendly with therapeutically vital products, alongside their utilization as supplement in numerous therapeutic formulations.

show abstract

“…C. miliatris is one of the most representative and widely-used species of Cordyceps. Some conserved or functional genes of C. miliatris have been studied for phylogenetic analysis or probable enzyme application (Sung et al 2007;Ujita et al 2006;Wang et al 2005). In previous research, the cox1 introns of Cordyceps were only found in Beauveria bassiana and B. brongniartii (teleomorph: Cordyceps bassiana and C. brongniartii) when the complete mitochondrial genomes were reported (Ghikas et al 2010).…”

Section: Introductionmentioning

confidence: 99%

Cordyceps militaris (Hypocreales: Cordycipitaceae): transcriptional analysis and molecular characterization of cox1 and group I intron with putative LAGLIDADG endonuclease

Zheng

Jiang

Huang

et al. 2011

World J Microbiol Biotechnol

View full text Add to dashboard Cite

The full-length cytochrome c oxidase subunit I gene (cox1) containing a group I intron was isolated from an important medical fungus Cordyceps militaris (Cordycipitaceae). The open reading frame (ORF) of 1,593 nucleotides encoded a predicted protein COX1 of 530 amino acids. The group I intron encoded a putative homing endonuclease (HE) with two LAGLIDADG motifs. RT-PCR and Northern analysis showed a mature transcript of spliced cox1. Both 5'exon-intron and intron-3'exon junctions were also found by RT-PCR, suggesting the possible presence of unspliced cox1 RNA in total RNA. Sequence comparison by BLASTn showed that the coding region of cox1 (CRcox1) of C. militaris had significant similarities to those of related species (such as Cordyceps bassiana and C. brongniartii), while the intron had no significant homologous sequences of Cordycipitaceae fungi in NCBI database. The phylogenetic tree based on the CRcox1 confirmed the present taxonomic status of related species, but the cox1 introns were phylogenetically distinct. Compared to C. bassiana and C. brongniartii, the cox1 intron of C. militaris exhibited specific splicing site and different intronic ORF. The analysis of the folding RNA structures of the known cox1 introns from Cordyceps species showed different base pairs and conserved regions (P1-P10) in their structures. The present results provide useful information on the studies of cox1 intron splicing and Cordyceps evolution.

show abstract

Purification and partial characterization of recombinant Cu, Zn containing superoxide dismutase of Cordyceps militaris in E. coli

Cited by 11 publications

References 37 publications

A novel process for the recovery of superoxide dismutase from yeast exploiting electroextraction coupled to direct sorption

A novel process for the recovery of superoxide dismutase from yeast exploiting electroextraction coupled to direct sorption

Juglans regia and Ribes nigrum as potential nutraceuticals: Source of thermostable superoxide dismutase enzyme

Cordyceps militaris (Hypocreales: Cordycipitaceae): transcriptional analysis and molecular characterization of cox1 and group I intron with putative LAGLIDADG endonuclease

Contact Info

Product

Resources

About