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DC Field | Value | Language |
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dc.contributor.author | Amiola, Ruth Ololade | - |
dc.contributor.author | Ademakinwa, Adedeji Nelson | - |
dc.contributor.author | Ayinla, Zainab Adenike | - |
dc.contributor.author | Ezima, Esther Nkechi | - |
dc.contributor.author | Agboola, Femi Kayode | - |
dc.date.accessioned | 2021-02-17T11:55:09Z | - |
dc.date.available | 2021-02-17T11:55:09Z | - |
dc.date.issued | 2018-02-06 | - |
dc.identifier.citation | Amiola, R.O., Ademakinwa, A.N., Ayinla, Z.A., Ezima, E.N., & Agboola, F. (2018). Purification and biochemical characterization of a β-cyanoalanine synthase expressed in germinating seeds of Sorghum bicolor (L.) moench. Turkish Journal of Biochemistry, 43, 638 - 650. https://doi.org/10.1515/tjb-2017-0214 | en_US |
dc.identifier.issn | 1303-829X | - |
dc.identifier.uri | https://doi.org/10.1515/tjb-2017-0214 | - |
dc.identifier.uri | http://repository.elizadeuniversity.edu.ng/jspui/handle/20.500.12398/877 | - |
dc.description | Staff Publication | en_US |
dc.description.abstract | Background: β-Cyanoalanine synthase plays essential roles in germinating seeds, such as in cyanide homeostasis. Methods: β-Cyanoalanine synthase was isolated from sorghum seeds, purified using chromatographic techniques and its biochemical and catalytic properties were determined. Results: The purified enzyme had a yield of 61.74% and specific activity of 577.50 nmol H2S/min/mg of protein. The apparent and subunit molecular weight for purified β-cyanoalanine synthase were 58.26 ± 2.41 kDa and 63.4 kDa, respectively. The kinetic parameters with sodium cyanide as substrate were 0.67 ± 0.08 mM, 17.60 ± 0.50 nmol H2S/mL/min, 2.97 × 10−1 s−1 and 4.43 × 102 M−1 s−1 for KM, Vmax, kcat and kcat/KM, respectively. With L-cysteine as substrate, the kinetic parameters were 2.64 ± 0.37 mM, 63.41 ± 4.04 nmol H2S/mL/min, 10.71 × 10−1 s−1 and 4.06 × 102 M−1 s−1 for KM, Vmax, kcat and kcat/KM, respectively. The optimum temperature and pH for activity were 35°C and 8.5, respectively. The enzyme retained more than half of its activity at 40°C. Inhibitors such as HgCl2, EDTA, glycine and iodoacetamide reduced enzyme activity. Conclusion: The biochemical properties of β-cyanoalanine synthase in germinating sorghum seeds highlights its roles in maintaining cyanide homeostasis | en_US |
dc.language.iso | en | en_US |
dc.publisher | De Gruyter : Turkish Journal of Biochemistry | en_US |
dc.subject | β-Cyanoalanine synthase; | en_US |
dc.subject | Cyanide; | en_US |
dc.subject | Sorghum; | en_US |
dc.subject | Detoxification; | en_US |
dc.subject | Characterization; | en_US |
dc.subject | Purification. | en_US |
dc.title | Purification and biochemical characterization of a β-cyanoalanine synthase expressed in germinating seeds of Sorghum bicolor (L.) moench | en_US |
dc.type | Article | en_US |
Appears in Collections: | Research Articles |
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File | Description | Size | Format | |
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Purification_and_biochemical_characterization_of_a.pdf | 1.1 MB | Adobe PDF | View/Open |
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