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| Content Provider | Springer Nature Link |
|---|---|
| Author | Vikramathithan, Jeyaraman Muthuraman, Pandurangan Ravikumar, Sambandam Shayamala, Shivalingam Kumar, Gali Nirmal Srikumar, Kotteazeth |
| Copyright Year | 2012 |
| Abstract | Two thermostable xylanase isoforms T$_{60}$ and T$_{80}$ were purified to homogeneity from the cladodes of the xerophytic Cereus pterogonus plant species. After three consecutive purification steps, the specific activity of T$_{60}$ and T$_{80}$ isoforms were found to be 178.6 and 216.2 U mg$^{−1}$ respectively. The molecular mass of both isoforms was determined to be 80 kDa. The optimum temperature for T$_{60}$ and T$_{80}$ xylanase isoforms were 60 and 80 °C respectively. The pH was 5.0 for both isoforms. The presence of divalent metal ions (10 mM Co$^{2+}$) showed stimulatory effects of both catalytic activities, where as in the presence of Hg$^{2+}$, Cd$^{2+}$, Cu$^{2+}$ showed inhibitory effect on these activities at all concentrations studied. The thermodynamic analysis of xylanase activity using denaturation kinetics and the presence divalent cations at 30–100 °C, showed lower ΔH, ΔS, and ΔG values at all the temperatures investigated. The melting temperature of purified T$_{80}$ xylanase isoform as determined by TG/DTA analysis and it showed the unfolding temperature was 80 °C. The g value and hyperfine (A) value purified xylanase T$_{80}$ isoform was 2.017 and 10.80 respectively. Immunoblot analysis with antiserum raised against the purified T$_{80}$ xylanase isoforms revealed single immunolgically related polypeptides of 80 kDa, identical with the polypeptide band produced on SDS-PAGE. The results of double immunodiffusion against the T$_{80}$ isoforms showed a single precipitin line indicating that the serum used was specific to these xylanase isoforms. The kinetic and thermodynamic properties suggested that xylanase from C. pterogonus may have a potential usage in various industries. |
| Starting Page | 141 |
| Ending Page | 149 |
| Page Count | 9 |
| File Format | |
| ISSN | 15723887 |
| Journal | The Protein Journal |
| Volume Number | 31 |
| Issue Number | 2 |
| e-ISSN | 15734943 |
| Language | English |
| Publisher | Springer US |
| Publisher Date | 2012-01-10 |
| Publisher Place | Boston |
| Access Restriction | One Nation One Subscription (ONOS) |
| Subject Keyword | Xylanase Thermodynamics Enzyme kinetics TG/DTA Immuno diffusion Western blot Organic Chemistry Biochemistry Animal Anatomy / Morphology / Histology Bioorganic Chemistry |
| Content Type | Text |
| Resource Type | Article |
| Subject | Organic Chemistry Analytical Chemistry Biochemistry Bioengineering |
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