Substrate specificity and enzyme recycling using chitosan immobilized laccase
Skoronski, E; Fernandes, M; Magalhães, M; da Silva, GF; João, JJ; Soares, CH; Júnior, AF
HERO ID
2862045
Reference Type
Journal Article
Year
2014
Language
English
PMID
| HERO ID | 2862045 |
|---|---|
| In Press | No |
| Year | 2014 |
| Title | Substrate specificity and enzyme recycling using chitosan immobilized laccase |
| Authors | Skoronski, E; Fernandes, M; Magalhães, M; da Silva, GF; João, JJ; Soares, CH; Júnior, AF |
| Journal | Molecules |
| Volume | 19 |
| Issue | 10 |
| Page Numbers | 16794-16809 |
| Abstract | The immobilization of laccase (Aspergillus sp.) on chitosan by cross-linking and its application in bioconversion of phenolic compounds in batch reactors were studied. Investigation was performed using laccase immobilized via chemical cross-linking due to the higher enzymatic operational stability of this method as compared to immobilization via physical adsorption. To assess the influence of different substrate functional groups on the enzyme's catalytic efficiency, substrate specificity was investigated using chitosan-immobilized laccase and eighteen different phenol derivatives. It was observed that 4-nitrophenol was not oxidized, while 2,5-xylenol, 2,6-xylenol, 2,3,5-trimethylphenol, syringaldazine, 2,6-dimetoxyphenol and ethylphenol showed reaction yields up 90% at 40 °C. The kinetic of process, enzyme recyclability and operational stability were studied. In batch reactors, it was not possible to reuse the enzyme when it was applied to syringaldazne bioconversion. However, when the enzyme was applied to bioconversion of 2,6-DMP, the activity was stable for eight reaction batches. |
| Doi | 10.3390/molecules191016794 |
| Pmid | 25329872 |
| Wosid | WOS:000344456100083 |
| Is Certified Translation | No |
| Dupe Override | No |
| Is Public | Yes |
| Language Text | English |
| Keyword | laccase; Aspergillus sp.; chitosan; enzyme immobilization; phenolic compounds; bioremediation |