Partial Purification and Characterisation of Polyphenol oxidase from Two Species of Bitter Yam (<i>Discorea dumentorum</i>)

David Morakinyo Sanni

doi:doi:10.11648/j.bmb.20160102.11

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Partial Purification and Characterisation of Polyphenol oxidase from Two Species of Bitter Yam (Discorea dumentorum)

David Morakinyo Sanni

Published in Biochemistry and Molecular Biology (Volume 1, Issue 2)

Received: 1 June 2016 Accepted: 12 June 2016 Published: 6 July 2016

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Abstract

Polyphenol oxidases (PPO) are group of copper proteins, widely distributed phylogenetically from bacteria to mammals that catalyze the oxidation of phenolics to quinones which produces brown pigments in wounded tissues. PPO was isolated and partially characterized in white and yellow bitter yam (Discorea dumentorum). Extracts were partially purified using ammonium sulphate. The effects of optimum pH and temperature were investigated, while thermal and pH stability was also determined. The substrate specificity, kinetic and inhibition studies were also carried out. The optimal pH in the absence and presence of SDS were found to be 5.0 and 6.0, and 6.0 and 8.0 for white and yellow bitter yam respectively, while the optimum temperature for both white and yellow bitter yam was at 30°C. The enzyme was stable with over 90% activity after 3 hours incubation time at pH of 4.0 and 5.0, and 4.0 for yellow and white bitter yam respectively. The enzyme revealed over 70% remaining activities at all temperature investigated for yellow and at 30, 40 and 50°C for white bitter yam after 1 hour incubation. The K_m values of 6.8 x 10^-2mM and 8.0 x 10^-2mM, and 3.3 x 10^-1mM and 4.0 x 10^-1mM with L-DOPA and tyrosine as substrates for PPO from white and yellow bitter yam respectively. Higher activity was observed with L-DOPA than with tyrosine.

Published in	Biochemistry and Molecular Biology (Volume 1, Issue 2)
DOI	10.11648/j.bmb.20160102.11
Page(s)	11-16
Creative Commons	This is an Open Access article, distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution and reproduction in any medium or format, provided the original work is properly cited.
Copyright	Copyright © The Author(s), 2016. Published by Science Publishing Group

Keywords

Activity, Bitter Yam, Polyphenol oxidase, Partial Purification

References

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David Morakinyo Sanni. (2016). Partial Purification and Characterisation of Polyphenol oxidase from Two Species of Bitter Yam (Discorea dumentorum). Biochemistry and Molecular Biology, 1(2), 11-16. https://doi.org/10.11648/j.bmb.20160102.11

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ACS Style

David Morakinyo Sanni. Partial Purification and Characterisation of Polyphenol oxidase from Two Species of Bitter Yam (Discorea dumentorum). Biochem. Mol. Biol. 2016, 1(2), 11-16. doi: 10.11648/j.bmb.20160102.11

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AMA Style

David Morakinyo Sanni. Partial Purification and Characterisation of Polyphenol oxidase from Two Species of Bitter Yam (Discorea dumentorum). Biochem Mol Biol. 2016;1(2):11-16. doi: 10.11648/j.bmb.20160102.11

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@article{10.11648/j.bmb.20160102.11,
  author = {David Morakinyo Sanni},
  title = {Partial Purification and Characterisation of Polyphenol oxidase from Two Species of Bitter Yam (Discorea dumentorum)},
  journal = {Biochemistry and Molecular Biology},
  volume = {1},
  number = {2},
  pages = {11-16},
  doi = {10.11648/j.bmb.20160102.11},
  url = {https://doi.org/10.11648/j.bmb.20160102.11},
  eprint = {https://article.sciencepublishinggroup.com/pdf/10.11648.j.bmb.20160102.11},
  abstract = {Polyphenol oxidases (PPO) are group of copper proteins, widely distributed phylogenetically from bacteria to mammals that catalyze the oxidation of phenolics to quinones which produces brown pigments in wounded tissues. PPO was isolated and partially characterized in white and yellow bitter yam (Discorea dumentorum). Extracts were partially purified using ammonium sulphate. The effects of optimum pH and temperature were investigated, while thermal and pH stability was also determined. The substrate specificity, kinetic and inhibition studies were also carried out. The optimal pH in the absence and presence of SDS were found to be 5.0 and 6.0, and 6.0 and 8.0 for white and yellow bitter yam respectively, while the optimum temperature for both white and yellow bitter yam was at 30°C. The enzyme was stable with over 90% activity after 3 hours incubation time at pH of 4.0 and 5.0, and 4.0 for yellow and white bitter yam respectively. The enzyme revealed over 70% remaining activities at all temperature investigated for yellow and at 30, 40 and 50°C for white bitter yam after 1 hour incubation. The Km values of 6.8 x 10-2mM and 8.0 x 10-2mM, and 3.3 x 10-1mM and 4.0 x 10-1mM with L-DOPA and tyrosine as substrates for PPO from white and yellow bitter yam respectively. Higher activity was observed with L-DOPA than with tyrosine.},
 year = {2016}
}

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TY - JOUR
T1 - Partial Purification and Characterisation of Polyphenol oxidase from Two Species of Bitter Yam (Discorea dumentorum)
AU - David Morakinyo Sanni
Y1 - 2016/07/06
PY - 2016
N1 - https://doi.org/10.11648/j.bmb.20160102.11
DO - 10.11648/j.bmb.20160102.11
T2 - Biochemistry and Molecular Biology
JF - Biochemistry and Molecular Biology
JO - Biochemistry and Molecular Biology
SP - 11
EP - 16
PB - Science Publishing Group
SN - 2575-5048
UR - https://doi.org/10.11648/j.bmb.20160102.11
AB - Polyphenol oxidases (PPO) are group of copper proteins, widely distributed phylogenetically from bacteria to mammals that catalyze the oxidation of phenolics to quinones which produces brown pigments in wounded tissues. PPO was isolated and partially characterized in white and yellow bitter yam (Discorea dumentorum). Extracts were partially purified using ammonium sulphate. The effects of optimum pH and temperature were investigated, while thermal and pH stability was also determined. The substrate specificity, kinetic and inhibition studies were also carried out. The optimal pH in the absence and presence of SDS were found to be 5.0 and 6.0, and 6.0 and 8.0 for white and yellow bitter yam respectively, while the optimum temperature for both white and yellow bitter yam was at 30°C. The enzyme was stable with over 90% activity after 3 hours incubation time at pH of 4.0 and 5.0, and 4.0 for yellow and white bitter yam respectively. The enzyme revealed over 70% remaining activities at all temperature investigated for yellow and at 30, 40 and 50°C for white bitter yam after 1 hour incubation. The Km values of 6.8 x 10-2mM and 8.0 x 10-2mM, and 3.3 x 10-1mM and 4.0 x 10-1mM with L-DOPA and tyrosine as substrates for PPO from white and yellow bitter yam respectively. Higher activity was observed with L-DOPA than with tyrosine.
VL - 1
IS - 2
ER -

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David Morakinyo Sanni

Department of Biochemistry, Federal University of Technology, Akure, Nigeria

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David Morakinyo Sanni. (2016). Partial Purification and Characterisation of Polyphenol oxidase from Two Species of Bitter Yam (Discorea dumentorum). Biochemistry and Molecular Biology, 1(2), 11-16. https://doi.org/10.11648/j.bmb.20160102.11

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David Morakinyo Sanni. Partial Purification and Characterisation of Polyphenol oxidase from Two Species of Bitter Yam (Discorea dumentorum). Biochem. Mol. Biol. 2016, 1(2), 11-16. doi: 10.11648/j.bmb.20160102.11

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AMA Style

David Morakinyo Sanni. Partial Purification and Characterisation of Polyphenol oxidase from Two Species of Bitter Yam (Discorea dumentorum). Biochem Mol Biol. 2016;1(2):11-16. doi: 10.11648/j.bmb.20160102.11

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@article{10.11648/j.bmb.20160102.11,
  author = {David Morakinyo Sanni},
  title = {Partial Purification and Characterisation of Polyphenol oxidase from Two Species of Bitter Yam (Discorea dumentorum)},
  journal = {Biochemistry and Molecular Biology},
  volume = {1},
  number = {2},
  pages = {11-16},
  doi = {10.11648/j.bmb.20160102.11},
  url = {https://doi.org/10.11648/j.bmb.20160102.11},
  eprint = {https://article.sciencepublishinggroup.com/pdf/10.11648.j.bmb.20160102.11},
  abstract = {Polyphenol oxidases (PPO) are group of copper proteins, widely distributed phylogenetically from bacteria to mammals that catalyze the oxidation of phenolics to quinones which produces brown pigments in wounded tissues. PPO was isolated and partially characterized in white and yellow bitter yam (Discorea dumentorum). Extracts were partially purified using ammonium sulphate. The effects of optimum pH and temperature were investigated, while thermal and pH stability was also determined. The substrate specificity, kinetic and inhibition studies were also carried out. The optimal pH in the absence and presence of SDS were found to be 5.0 and 6.0, and 6.0 and 8.0 for white and yellow bitter yam respectively, while the optimum temperature for both white and yellow bitter yam was at 30°C. The enzyme was stable with over 90% activity after 3 hours incubation time at pH of 4.0 and 5.0, and 4.0 for yellow and white bitter yam respectively. The enzyme revealed over 70% remaining activities at all temperature investigated for yellow and at 30, 40 and 50°C for white bitter yam after 1 hour incubation. The Km values of 6.8 x 10-2mM and 8.0 x 10-2mM, and 3.3 x 10-1mM and 4.0 x 10-1mM with L-DOPA and tyrosine as substrates for PPO from white and yellow bitter yam respectively. Higher activity was observed with L-DOPA than with tyrosine.},
 year = {2016}
}

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