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

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 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.

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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Author Information
  • Department of Biochemistry, Federal University of Technology, Akure, Nigeria

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