Purification and biochemical characterization of a novel carbonic anhydrase II from erythrocytes of camel (Camelusdromedarius)
Copyright © 2023 Elsevier Inc. All rights reserved..
A novel carbonic anhydrase II (CA II) from erythrocytes of camel (Camelus dromedarius) was purified to homogeneity using affinity chromatography and biochemically characterized. Specific activity of 140.88 U/mg was obtained with 745.17-fold purification and 25.37% yield. The enzyme was a monomer with a lower molecular weight (25 kDa) and lower Zn content (0.50 mol of Zn per mol of protein). The enzyme showed higher optimum temperature (70 °C) and pH (pH 9.0), moreover, it was stable at higher temperatures and strongly alkaline pH as judged by thermodynamic parameters (Ea, kd, Ed, t1/2, D-value, Z-value, ΔH, ΔG and ΔS). The enzyme was inhibited by cations (Al3+, Ca2+, Cd2+, Co2+, Cr3+, Cu2+, Fe3+, Ni2+, Mg2+ and Zn2+) as well as by anions (Br‾, CH3COO‾, ClO4‾, CN‾, F‾, HCO3‾, I‾, N3‾, NO3‾ and SCN‾), some anions (C6H5O73-, CO32-, SeO3‾ and SO42-) does not affect enzyme activity. Effect of various chemicals on enzyme activity was also investigated. Km, Vmax, kcat and kcat/Km values for 4-NPA were found to be 1.74 mM, 0.0093 U/mL, 0,0039 s-1 and 0,0023 s-1 mM-1, respectively. With these interesting biochemical properties, camel CA II represents promising candidate for harsh industrial applications, in particular, for a successful biomimetic CO2 sequestration process.
| Medienart: |
E-Artikel |
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| Erscheinungsjahr: |
2023 |
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| Erschienen: |
2023 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:676 |
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| Enthalten in: |
Biochemical and biophysical research communications - 676(2023) vom: 08. Okt., Seite 171-181 |
| Sprache: |
Englisch |
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| Beteiligte Personen: |
Chafik, Abdelbasset [VerfasserIn] |
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| Links: |
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| Themen: |
Biochemical characterization |
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| Anmerkungen: |
Date Revised 01.09.2023 published: Print-Electronic Citation Status Publisher |
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| doi: |
10.1016/j.bbrc.2023.07.055 |
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| funding: |
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| Förderinstitution / Projekttitel: |
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| 245 | 1 | 0 | |a Purification and biochemical characterization of a novel carbonic anhydrase II from erythrocytes of camel (Camelusdromedarius) |
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| 520 | |a Copyright © 2023 Elsevier Inc. All rights reserved. | ||
| 520 | |a A novel carbonic anhydrase II (CA II) from erythrocytes of camel (Camelus dromedarius) was purified to homogeneity using affinity chromatography and biochemically characterized. Specific activity of 140.88 U/mg was obtained with 745.17-fold purification and 25.37% yield. The enzyme was a monomer with a lower molecular weight (25 kDa) and lower Zn content (0.50 mol of Zn per mol of protein). The enzyme showed higher optimum temperature (70 °C) and pH (pH 9.0), moreover, it was stable at higher temperatures and strongly alkaline pH as judged by thermodynamic parameters (Ea, kd, Ed, t1/2, D-value, Z-value, ΔH, ΔG and ΔS). The enzyme was inhibited by cations (Al3+, Ca2+, Cd2+, Co2+, Cr3+, Cu2+, Fe3+, Ni2+, Mg2+ and Zn2+) as well as by anions (Br‾, CH3COO‾, ClO4‾, CN‾, F‾, HCO3‾, I‾, N3‾, NO3‾ and SCN‾), some anions (C6H5O73-, CO32-, SeO3‾ and SO42-) does not affect enzyme activity. Effect of various chemicals on enzyme activity was also investigated. Km, Vmax, kcat and kcat/Km values for 4-NPA were found to be 1.74 mM, 0.0093 U/mL, 0,0039 s-1 and 0,0023 s-1 mM-1, respectively. With these interesting biochemical properties, camel CA II represents promising candidate for harsh industrial applications, in particular, for a successful biomimetic CO2 sequestration process | ||
| 650 | 4 | |a Journal Article | |
| 650 | 4 | |a Biochemical characterization | |
| 650 | 4 | |a Camel | |
| 650 | 4 | |a Camelus dromedarius | |
| 650 | 4 | |a Carbonic anhydrase II | |
| 650 | 4 | |a Purification | |
| 700 | 1 | |a Essamadi, Abdelkhalid |e verfasserin |4 aut | |
| 700 | 1 | |a Çelik, Safinur Yildirim |e verfasserin |4 aut | |
| 700 | 1 | |a Mavi, Ahmet |e verfasserin |4 aut | |
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