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Cyanobacterium Oscillatoria sp. peroxidase active at alkaline pH and high stability under chemical stresses |
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| รหัสดีโอไอ | |
| Creator | Surasak Laloknam and Chaiyasard Kachensuwan |
| Title | Cyanobacterium Oscillatoria sp. peroxidase active at alkaline pH and high stability under chemical stresses |
| Publisher | Mahasarakham University |
| Publication Year | 2559 |
| Journal Title | Research & Knowledge |
| Journal Vol. | 2 |
| Journal No. | 2 |
| Page no. | 36-45 |
| Keyword | Purification, characterization, peroxidase, cyanobacterium Oscillatoria sp. |
| ISSN | 2408-204x |
| Abstract | Cyanobacterial peroxidase enzyme extracted from Oscillatoria sp. SWU121 was purifiedfrom crude extract by 20-80% ammonium sulfate precipitation, DEAE cellulose ion-exchangechromatography, and Sephadex G-100 size exclusion chromatography. The purified Oscillatoria sp.peroxidase (OsPOX) exhibited a specific activity of 6106.63 mmol.min-1.mg.protein-1, whilepurification fold and yield were 17.45 and 34.70%, respectively. The OsPOX showed single band ofprotein on native and sodium dodecyl sulfate (SDS) polyacrylamide gel electrophoresis (PAGE). Themolecular weight was 45 kD similarly determined by gel filtration and SDS-PAGE suggesting that theOsPOX contained only one subunit. The apparent Km and Vmax values of the enzyme against phenolwere 930 mM and 8078.25 mmol.min-1.mg protein-1, respectively. The temperature and pH optimumfor OsPOX were 30?C and pH 9.0, respectively. However, it was stable at 10 70?C and pH 7.0 - 11.0.The presence of metal ions such as Na+, Mn2+and Fe3+ enhanced peroxidase activity. On the other hand,Zn+, Cd2+ and Hg2+ strongly inhibited the enzyme activity. SDS and EDTA reduced the peroxidaseactivity at 10 mM (20%). The OsPOX was found to be stable in the presence of urea. The affinity ofthe enzyme was highest for gallic acid, followed by ascorbic acid, phenol and cafeic acid. This findingshowed that OsPOX was active at alkaline pH and stable in presence of urea. |
