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.
Published in | American Journal of Chemical Engineering (Volume 5, Issue 6) |
DOI | 10.11648/j.ajche.20170506.13 |
Page(s) | 135-139 |
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Copyright © The Author(s), 2017. Published by Science Publishing Group |
Protein Engineering, Stability, Rational Design, Immobilization
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APA Style
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
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
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
@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} }
TY - JOUR T1 - Maximizing Stability in Industrial Enzymes: Rational Design Approach – A Review AU - Abubakar Muhammad Nazif AU - Ayuba Yohanna Musa AU - Muhammad Muawiya Alkali AU - Ilesanmi Esther Y1 - 2017/11/13 PY - 2017 N1 - https://doi.org/10.11648/j.ajche.20170506.13 DO - 10.11648/j.ajche.20170506.13 T2 - American Journal of Chemical Engineering JF - American Journal of Chemical Engineering JO - American Journal of Chemical Engineering SP - 135 EP - 139 PB - Science Publishing Group SN - 2330-8613 UR - https://doi.org/10.11648/j.ajche.20170506.13 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 IS - 6 ER -