Strategy to enhance catalytic activity and stability of sol–gel oxidoreductases
Oxidoreductases are widely recognized for their capability to degrade phenolic pollutants and versatile. However, the lack of enzyme stability makes this technique unrealistic for industrial applications. In order to enhance their catalytic activity, stability and reusability, oxidoreductases namely...
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my.utm.979632022-11-10T01:33:02Z http://eprints.utm.my/id/eprint/97963/ Strategy to enhance catalytic activity and stability of sol–gel oxidoreductases Mohidem, Nur Atikah Mat, Hanapi Mohamad, Mardawani Hamzah, Fazlena Rashid, Muhammad Usman TP Chemical technology Oxidoreductases are widely recognized for their capability to degrade phenolic pollutants and versatile. However, the lack of enzyme stability makes this technique unrealistic for industrial applications. In order to enhance their catalytic activity, stability and reusability, oxidoreductases namely laccases and peroxidases were entrapped in sol–gel silica and their catalytic activities were measured by an enzymatic assay using 2,6-dimethoxyphenol and guaiacol as substrates, respectively. The sol–gel silica matrices acted as a polymeric framework around the enzyme is a promising tool for improving enzyme stability. After entrapment, the catalytic activity and stability of sol–gel laccase and peroxidase toward pH, temperature and storage duration remarkably enhanced. Springer 2021 Article PeerReviewed Mohidem, Nur Atikah and Mat, Hanapi and Mohamad, Mardawani and Hamzah, Fazlena and Rashid, Muhammad Usman (2021) Strategy to enhance catalytic activity and stability of sol–gel oxidoreductases. Journal of Sol-Gel Science and Technology, 98 (3). pp. 462-469. ISSN 0928-0707 http://dx.doi.org/10.1007/s10971-021-05522-0 DOI : 10.1007/s10971-021-05522-0 |
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TP Chemical technology Mohidem, Nur Atikah Mat, Hanapi Mohamad, Mardawani Hamzah, Fazlena Rashid, Muhammad Usman Strategy to enhance catalytic activity and stability of sol–gel oxidoreductases |
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Oxidoreductases are widely recognized for their capability to degrade phenolic pollutants and versatile. However, the lack of enzyme stability makes this technique unrealistic for industrial applications. In order to enhance their catalytic activity, stability and reusability, oxidoreductases namely laccases and peroxidases were entrapped in sol–gel silica and their catalytic activities were measured by an enzymatic assay using 2,6-dimethoxyphenol and guaiacol as substrates, respectively. The sol–gel silica matrices acted as a polymeric framework around the enzyme is a promising tool for improving enzyme stability. After entrapment, the catalytic activity and stability of sol–gel laccase and peroxidase toward pH, temperature and storage duration remarkably enhanced. |
format |
Article |
author |
Mohidem, Nur Atikah Mat, Hanapi Mohamad, Mardawani Hamzah, Fazlena Rashid, Muhammad Usman |
author_facet |
Mohidem, Nur Atikah Mat, Hanapi Mohamad, Mardawani Hamzah, Fazlena Rashid, Muhammad Usman |
author_sort |
Mohidem, Nur Atikah |
title |
Strategy to enhance catalytic activity and stability of sol–gel oxidoreductases |
title_short |
Strategy to enhance catalytic activity and stability of sol–gel oxidoreductases |
title_full |
Strategy to enhance catalytic activity and stability of sol–gel oxidoreductases |
title_fullStr |
Strategy to enhance catalytic activity and stability of sol–gel oxidoreductases |
title_full_unstemmed |
Strategy to enhance catalytic activity and stability of sol–gel oxidoreductases |
title_sort |
strategy to enhance catalytic activity and stability of sol–gel oxidoreductases |
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Springer |
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2021 |
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http://eprints.utm.my/id/eprint/97963/ http://dx.doi.org/10.1007/s10971-021-05522-0 |
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