Polyphenol oxidases are oxido-reductases that catalyses oxidation of phenolic compounds in the presence of oxygen to form corresponding quinone intermediates which spontaneously polymerize to form undesirable pigments. Polyphenol oxidase was isolated and characterized in Irvingia species (gabonensis and wombolu) kernel, a tropical African fruit. Extracts were partially purified with ammonium sulphate. The effects of optimum pH and temperature were investigated while the pH and thermal stability were carried out. The Km, Vmax and the activity on both monophenol and diphenol substrates were determined. The optimum pH and optimum temperature of activity were found out to be 7.0 and 60°C in both species. The enzyme was stable at pH 7.0 and pH 8.0, and also at temperatures of 25, 30, 40, 50 and 60°C, it however loses stability beyond 60°C. Km and Vmax for Irvingia gabonesis were 2.51mM and 0.0411 Unit/min while Km and Vmax for Irvingia wombolu were 2.55mM and 0.0415 Unit/min respectively. Higher activity was observed with diphenol substrate L-DOPA than with monophenol - tyrosine. It can therefore be deduced from this study that the storage of the seeds of African mango at a room temperature above 60°C will prolong its shelf-life.
| Published in | Advances in Biochemistry (Volume 4, Issue 4) |
| DOI | 10.11648/j.ab.20160404.12 |
| Page(s) | 47-52 |
| Creative Commons |
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Copyright © The Author(s), 2016. Published by Science Publishing Group |
Enzyme Activity, African Mango, Polyphenol Oxidase
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APA Style
David Morakinyo Sanni. (2016). Isolation, Partial Purification and Characterization of Polyphenol Oxidase from Two Species of African Mango Seeds (Irvingia gabonensis and Irvingia wombolu). Advances in Biochemistry, 4(4), 47-52. https://doi.org/10.11648/j.ab.20160404.12
ACS Style
David Morakinyo Sanni. Isolation, Partial Purification and Characterization of Polyphenol Oxidase from Two Species of African Mango Seeds (Irvingia gabonensis and Irvingia wombolu). Adv. Biochem. 2016, 4(4), 47-52. doi: 10.11648/j.ab.20160404.12
AMA Style
David Morakinyo Sanni. Isolation, Partial Purification and Characterization of Polyphenol Oxidase from Two Species of African Mango Seeds (Irvingia gabonensis and Irvingia wombolu). Adv Biochem. 2016;4(4):47-52. doi: 10.11648/j.ab.20160404.12
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Download@article{10.11648/j.ab.20160404.12,
author = {David Morakinyo Sanni},
title = {Isolation, Partial Purification and Characterization of Polyphenol Oxidase from Two Species of African Mango Seeds (Irvingia gabonensis and Irvingia wombolu)},
journal = {Advances in Biochemistry},
volume = {4},
number = {4},
pages = {47-52},
doi = {10.11648/j.ab.20160404.12},
url = {https://doi.org/10.11648/j.ab.20160404.12},
eprint = {https://article.sciencepublishinggroup.com/pdf/10.11648.j.ab.20160404.12},
abstract = {Polyphenol oxidases are oxido-reductases that catalyses oxidation of phenolic compounds in the presence of oxygen to form corresponding quinone intermediates which spontaneously polymerize to form undesirable pigments. Polyphenol oxidase was isolated and characterized in Irvingia species (gabonensis and wombolu) kernel, a tropical African fruit. Extracts were partially purified with ammonium sulphate. The effects of optimum pH and temperature were investigated while the pH and thermal stability were carried out. The Km, Vmax and the activity on both monophenol and diphenol substrates were determined. The optimum pH and optimum temperature of activity were found out to be 7.0 and 60°C in both species. The enzyme was stable at pH 7.0 and pH 8.0, and also at temperatures of 25, 30, 40, 50 and 60°C, it however loses stability beyond 60°C. Km and Vmax for Irvingia gabonesis were 2.51mM and 0.0411 Unit/min while Km and Vmax for Irvingia wombolu were 2.55mM and 0.0415 Unit/min respectively. Higher activity was observed with diphenol substrate L-DOPA than with monophenol - tyrosine. It can therefore be deduced from this study that the storage of the seeds of African mango at a room temperature above 60°C will prolong its shelf-life.},
year = {2016}
}
TY - JOUR T1 - Isolation, Partial Purification and Characterization of Polyphenol Oxidase from Two Species of African Mango Seeds (Irvingia gabonensis and Irvingia wombolu) AU - David Morakinyo Sanni Y1 - 2016/06/30 PY - 2016 N1 - https://doi.org/10.11648/j.ab.20160404.12 DO - 10.11648/j.ab.20160404.12 T2 - Advances in Biochemistry JF - Advances in Biochemistry JO - Advances in Biochemistry SP - 47 EP - 52 PB - Science Publishing Group SN - 2329-0862 UR - https://doi.org/10.11648/j.ab.20160404.12 AB - Polyphenol oxidases are oxido-reductases that catalyses oxidation of phenolic compounds in the presence of oxygen to form corresponding quinone intermediates which spontaneously polymerize to form undesirable pigments. Polyphenol oxidase was isolated and characterized in Irvingia species (gabonensis and wombolu) kernel, a tropical African fruit. Extracts were partially purified with ammonium sulphate. The effects of optimum pH and temperature were investigated while the pH and thermal stability were carried out. The Km, Vmax and the activity on both monophenol and diphenol substrates were determined. The optimum pH and optimum temperature of activity were found out to be 7.0 and 60°C in both species. The enzyme was stable at pH 7.0 and pH 8.0, and also at temperatures of 25, 30, 40, 50 and 60°C, it however loses stability beyond 60°C. Km and Vmax for Irvingia gabonesis were 2.51mM and 0.0411 Unit/min while Km and Vmax for Irvingia wombolu were 2.55mM and 0.0415 Unit/min respectively. Higher activity was observed with diphenol substrate L-DOPA than with monophenol - tyrosine. It can therefore be deduced from this study that the storage of the seeds of African mango at a room temperature above 60°C will prolong its shelf-life. VL - 4 IS - 4 ER -
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