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Dergiler / Hacettepe Journal of Biology and Chemistry / 2021 / Cilt: 49 - Sayı: 3

Cloning, Over-Expression, and Purification of β–Carbonic Anhydrase from an Extremophilic Bacterium: Deinococcus radiodurans

Ayşe Hümeyra TAŞKIN KAFA
Arzu CİHAN
Mehmet KUZUCU
Murat ÇANKAYA
Sayfa
219–231
Yayın Tarihi
2021-05-17
DOI
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The CO2 hydration assay demonstrated that the specific activity of purified recombinant enzymes (DrCA) was significantly high.

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Amaç & Hipotez:Öz In this study, the cloning, purification and initial characterization of carbonic anhydrase (DrCA) enzyme which we consider to be important in the resistance physiology from extremely radioresistant bacteria Deinococcus radiodurans is performed.
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Temel Bulgular & Veri:In addition, the effect of increased gamma irradiation doses on pH-related DrCA enzyme activity was determined.
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Sonuç & Katkı:The CO2 hydration assay demonstrated that the specific activity of purified recombinant enzymes (DrCA) was significantly high.
🔬Tür:Araştırma Makalesi
📍Kapsam:Genişletilmiş Akademik Örneklem
⚙️Değişkenler:Anahtar Kelimeler Deinococcus radiodurans · carbonic anhydrase · ionizing radiation

Özet

Öz In this study, the cloning, purification and initial characterization of carbonic anhydrase (DrCA) enzyme which we consider to be important in the resistance physiology from extremely radioresistant bacteria Deinococcus radiodurans is performed. In addition, the effect of increased gamma irradiation doses on pH-related DrCA enzyme activity was determined. DrCA activity after radiation treatment showed that the activity continuously increased by 6 fold, up to the first 800 Gy, which a decrease in activity was observed thereafter. The maximum CO2 hydration activity for DrCA enzyme was observed at pH 7.0 and 40°C. DrCA enzyme, homo-dimer complex, is slightly thermostable. The activity of DrCA was significantly enhanced by several metal ions, especially Zn2+, which resulted in 5-fold increases of CO2 hydration activity. Also sulfonamide showed inhibitory effect on the pure enzyme. The apparent Km and Vmax for CO2 as substrate were 8.4 mM and 637 WAU/mg for DrCA respectively. The CO2 hydration assay demonstrated that the specific activity of purified recombinant enzymes (DrCA) was significantly high.

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Bu Makaleye Atıf Yap

KAFA, A. H. T., CİHAN, A., KUZUCU, M., ÇANKAYA, M. (2021). Cloning, Over-Expression, and Purification of β–Carbonic Anhydrase from an Extremophilic Bacterium: Deinococcus radiodurans. Hacettepe Journal of Biology and Chemistry, Cilt: 49 - Sayı: 3, 219–231. https://ajindex.com/articles/255632

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Kaynakça (15)

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