Laccases: Versatile Biocatalysts for the Synthesis of Heterocyclic Cores
Laccases are multicopper oxidases that have shown a great potential in various biotechnological and green chemistry processes mainly due to their high relative non-specific oxidation of phenols, arylamines and some inorganic metals, and their high redox potentials that can span from 500 to 800 mV vs...
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| Format: | Article |
| Language: | English |
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MDPI AG
2021-06-01
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| Series: | Molecules |
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| Online Access: | https://www.mdpi.com/1420-3049/26/12/3719 |
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| author | Ana Catarina Sousa Lígia O. Martins M. Paula Robalo |
| author_facet | Ana Catarina Sousa Lígia O. Martins M. Paula Robalo |
| author_sort | Ana Catarina Sousa |
| collection | DOAJ |
| description | Laccases are multicopper oxidases that have shown a great potential in various biotechnological and green chemistry processes mainly due to their high relative non-specific oxidation of phenols, arylamines and some inorganic metals, and their high redox potentials that can span from 500 to 800 mV vs. SHE. Other advantages of laccases include the use of readily available oxygen as a second substrate, the formation of water as a side-product and no requirement for cofactors. Importantly, addition of low-molecular-weight redox mediators that act as electron shuttles, promoting the oxidation of complex bulky substrates and/or of higher redox potential than the enzymes themselves, can further expand their substrate scope, in the so-called laccase-mediated systems (LMS). Laccase bioprocesses can be designed for efficiency at both acidic and basic conditions since it is known that fungal and bacterial laccases exhibit distinct optimal pH values for the similar phenolic and aromatic amines. This review covers studies on the synthesis of five- and six-membered ring heterocyclic cores, such as benzimidazoles, benzofurans, benzothiazoles, quinazoline and quinazolinone, phenazine, phenoxazine, phenoxazinone and phenothiazine derivatives. The enzymes used and the reaction protocols are briefly outlined, and the mechanistic pathways described. |
| first_indexed | 2024-03-10T10:18:10Z |
| format | Article |
| id | doaj.art-0fb201ae3f2d4004bd206ddd0cb0e45e |
| institution | Directory Open Access Journal |
| issn | 1420-3049 |
| language | English |
| last_indexed | 2024-03-10T10:18:10Z |
| publishDate | 2021-06-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Molecules |
| spelling | doaj.art-0fb201ae3f2d4004bd206ddd0cb0e45e2023-11-22T00:37:53ZengMDPI AGMolecules1420-30492021-06-012612371910.3390/molecules26123719Laccases: Versatile Biocatalysts for the Synthesis of Heterocyclic CoresAna Catarina Sousa0Lígia O. Martins1M. Paula Robalo2Área Departamental de Engenharia Química, Instituto Superior de Engenharia de Lisboa, Instituto Politécnico de Lisboa, R. Conselheiro Emídio Navarro 1, 1959-007 Lisboa, PortugalInstituto de Tecnologia Química e Biológica António Xavier, Universidade Nova de Lisboa, Av. da República, 2780-157 Oeiras, PortugalÁrea Departamental de Engenharia Química, Instituto Superior de Engenharia de Lisboa, Instituto Politécnico de Lisboa, R. Conselheiro Emídio Navarro 1, 1959-007 Lisboa, PortugalLaccases are multicopper oxidases that have shown a great potential in various biotechnological and green chemistry processes mainly due to their high relative non-specific oxidation of phenols, arylamines and some inorganic metals, and their high redox potentials that can span from 500 to 800 mV vs. SHE. Other advantages of laccases include the use of readily available oxygen as a second substrate, the formation of water as a side-product and no requirement for cofactors. Importantly, addition of low-molecular-weight redox mediators that act as electron shuttles, promoting the oxidation of complex bulky substrates and/or of higher redox potential than the enzymes themselves, can further expand their substrate scope, in the so-called laccase-mediated systems (LMS). Laccase bioprocesses can be designed for efficiency at both acidic and basic conditions since it is known that fungal and bacterial laccases exhibit distinct optimal pH values for the similar phenolic and aromatic amines. This review covers studies on the synthesis of five- and six-membered ring heterocyclic cores, such as benzimidazoles, benzofurans, benzothiazoles, quinazoline and quinazolinone, phenazine, phenoxazine, phenoxazinone and phenothiazine derivatives. The enzymes used and the reaction protocols are briefly outlined, and the mechanistic pathways described.https://www.mdpi.com/1420-3049/26/12/3719biocatalysisheterocyclesoxidoreductasesbioprocessescross-coupling reactionsgreen methods |
| spellingShingle | Ana Catarina Sousa Lígia O. Martins M. Paula Robalo Laccases: Versatile Biocatalysts for the Synthesis of Heterocyclic Cores Molecules biocatalysis heterocycles oxidoreductases bioprocesses cross-coupling reactions green methods |
| title | Laccases: Versatile Biocatalysts for the Synthesis of Heterocyclic Cores |
| title_full | Laccases: Versatile Biocatalysts for the Synthesis of Heterocyclic Cores |
| title_fullStr | Laccases: Versatile Biocatalysts for the Synthesis of Heterocyclic Cores |
| title_full_unstemmed | Laccases: Versatile Biocatalysts for the Synthesis of Heterocyclic Cores |
| title_short | Laccases: Versatile Biocatalysts for the Synthesis of Heterocyclic Cores |
| title_sort | laccases versatile biocatalysts for the synthesis of heterocyclic cores |
| topic | biocatalysis heterocycles oxidoreductases bioprocesses cross-coupling reactions green methods |
| url | https://www.mdpi.com/1420-3049/26/12/3719 |
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