American Journal of Chemical Engineering

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Maximizing Stability in Industrial Enzymes: Rational Design Approach – A Review

Received: 13 September 2017    Accepted: 26 September 2017    Published: 13 November 2017
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Abstract

Indigenous enzymes found in nature have found wide application in industries ascribable to their ability to catalyze complex chemical processes under moderate experimental and environmental conditions. However, the use of indigenous enzymes is yet to achieve the needed industrial goal for, indigenous enzymes are readily unstable when subjected to harsh environmental conditions. Since the emergence of recombinant DNA technology and recent developments in protein engineering in recent years, there have been continuous reports regarding enzyme stability – most especially by the introduction of site-directed mutagenesis. With these new developments, scientists have been able to engineer enzymes using a variety of strategies in rational design such as the introduction of disulfide bridges and engineering hydrophobic residues. This review aims to highlight rational design methods and enzyme immobilization from various studies, which may be used to increase stability in industrial enzymes.

DOI 10.11648/j.ajche.20170506.13
Published in American Journal of Chemical Engineering (Volume 5, Issue 6, November 2017)
Page(s) 135-139
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), 2024. Published by Science Publishing Group

Keywords

Protein Engineering, Stability, Rational Design, Immobilization

References
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    Abubakar Muhammad Nazif, Ayuba Yohanna Musa, Muhammad Muawiya Alkali, Ilesanmi Esther. (2017). Maximizing Stability in Industrial Enzymes: Rational Design Approach – A Review. American Journal of Chemical Engineering, 5(6), 135-139. https://doi.org/10.11648/j.ajche.20170506.13

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    ACS Style

    Abubakar Muhammad Nazif; Ayuba Yohanna Musa; Muhammad Muawiya Alkali; Ilesanmi Esther. Maximizing Stability in Industrial Enzymes: Rational Design Approach – A Review. Am. J. Chem. Eng. 2017, 5(6), 135-139. doi: 10.11648/j.ajche.20170506.13

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    AMA Style

    Abubakar Muhammad Nazif, Ayuba Yohanna Musa, Muhammad Muawiya Alkali, Ilesanmi Esther. Maximizing Stability in Industrial Enzymes: Rational Design Approach – A Review. Am J Chem Eng. 2017;5(6):135-139. doi: 10.11648/j.ajche.20170506.13

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  • @article{10.11648/j.ajche.20170506.13,
      author = {Abubakar Muhammad Nazif and Ayuba Yohanna Musa and Muhammad Muawiya Alkali and Ilesanmi Esther},
      title = {Maximizing Stability in Industrial Enzymes: Rational Design Approach – A Review},
      journal = {American Journal of Chemical Engineering},
      volume = {5},
      number = {6},
      pages = {135-139},
      doi = {10.11648/j.ajche.20170506.13},
      url = {https://doi.org/10.11648/j.ajche.20170506.13},
      eprint = {https://article.sciencepublishinggroup.com/pdf/10.11648.j.ajche.20170506.13},
      abstract = {Indigenous enzymes found in nature have found wide application in industries ascribable to their ability to catalyze complex chemical processes under moderate experimental and environmental conditions. However, the use of indigenous enzymes is yet to achieve the needed industrial goal for, indigenous enzymes are readily unstable when subjected to harsh environmental conditions. Since the emergence of recombinant DNA technology and recent developments in protein engineering in recent years, there have been continuous reports regarding enzyme stability – most especially by the introduction of site-directed mutagenesis. With these new developments, scientists have been able to engineer enzymes using a variety of strategies in rational design such as the introduction of disulfide bridges and engineering hydrophobic residues. This review aims to highlight rational design methods and enzyme immobilization from various studies, which may be used to increase stability in industrial enzymes.},
     year = {2017}
    }
    

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    AU  - Ayuba Yohanna Musa
    AU  - Muhammad Muawiya Alkali
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    AB  - Indigenous enzymes found in nature have found wide application in industries ascribable to their ability to catalyze complex chemical processes under moderate experimental and environmental conditions. However, the use of indigenous enzymes is yet to achieve the needed industrial goal for, indigenous enzymes are readily unstable when subjected to harsh environmental conditions. Since the emergence of recombinant DNA technology and recent developments in protein engineering in recent years, there have been continuous reports regarding enzyme stability – most especially by the introduction of site-directed mutagenesis. With these new developments, scientists have been able to engineer enzymes using a variety of strategies in rational design such as the introduction of disulfide bridges and engineering hydrophobic residues. This review aims to highlight rational design methods and enzyme immobilization from various studies, which may be used to increase stability in industrial enzymes.
    VL  - 5
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Author Information
  • Department of Biotechnology, Modibbo Adama University of Technology, Yola, Nigeria

  • Department of Chemistry, Abubakar Tafawa Balewa University, Bauchi, Nigeria

  • Department of Biochemistry, Modibbo Adama University of Technology, Yola, Nigeria

  • Department of Chemistry, University of Benin, Benin, Nigeria

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