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...
| 發表在: | Journal of Sol-Gel Science and Technology |
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| 格式: | Article |
| 語言: | English |
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Springer
2021
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| 在線閱讀: | https://www.scopus.com/inward/record.uri?eid=2-s2.0-85103535613&doi=10.1007%2fs10971-021-05522-0&partnerID=40&md5=c4a078b5bea7940337f5c856393b07ec |
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Mohidem N.A.; Bin Mat H.; Mohamad M.; Hamzah F.; Rashid M.U. |
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Mohidem N.A.; Bin Mat H.; Mohamad M.; Hamzah F.; Rashid M.U. 2-s2.0-85103535613 Strategy to enhance catalytic activity and stability of sol–gel oxidoreductases 2021 Journal of Sol-Gel Science and Technology 98 3 10.1007/s10971-021-05522-0 https://www.scopus.com/inward/record.uri?eid=2-s2.0-85103535613&doi=10.1007%2fs10971-021-05522-0&partnerID=40&md5=c4a078b5bea7940337f5c856393b07ec 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. [Figure not available: see fulltext.] © 2021, The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature. Springer 9280707 English Article |
| author |
2-s2.0-85103535613 |
| spellingShingle |
2-s2.0-85103535613 Strategy to enhance catalytic activity and stability of sol–gel oxidoreductases |
| author_facet |
2-s2.0-85103535613 |
| author_sort |
2-s2.0-85103535613 |
| 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 |
| publishDate |
2021 |
| container_title |
Journal of Sol-Gel Science and Technology |
| container_volume |
98 |
| container_issue |
3 |
| doi_str_mv |
10.1007/s10971-021-05522-0 |
| url |
https://www.scopus.com/inward/record.uri?eid=2-s2.0-85103535613&doi=10.1007%2fs10971-021-05522-0&partnerID=40&md5=c4a078b5bea7940337f5c856393b07ec |
| description |
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. [Figure not available: see fulltext.] © 2021, The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature. |
| publisher |
Springer |
| issn |
9280707 |
| language |
English |
| format |
Article |
| accesstype |
|
| record_format |
scopus |
| collection |
Scopus |
| _version_ |
1828987870402052096 |