Enzymes in “Green” Synthetic Chemistry: Laccase and Lipase
Enzymes play an important role in numerous natural processes and are increasingly being utilized as environmentally friendly substitutes and alternatives to many common catalysts. Their essential advantages are high catalytic efficiency, substrate specificity, minimal formation of byproducts, and lo...
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| Format: | Article |
| Language: | English |
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MDPI AG
2024-02-01
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| Series: | Molecules |
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| Online Access: | https://www.mdpi.com/1420-3049/29/5/989 |
| _version_ | 1797264128521273344 |
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| author | Dieter M. Scheibel Ioan Pavel Ivanov Gitsov Ivan Gitsov |
| author_facet | Dieter M. Scheibel Ioan Pavel Ivanov Gitsov Ivan Gitsov |
| author_sort | Dieter M. Scheibel |
| collection | DOAJ |
| description | Enzymes play an important role in numerous natural processes and are increasingly being utilized as environmentally friendly substitutes and alternatives to many common catalysts. Their essential advantages are high catalytic efficiency, substrate specificity, minimal formation of byproducts, and low energy demand. All of these benefits make enzymes highly desirable targets of academic research and industrial development. This review has the modest aim of briefly overviewing the classification, mechanism of action, basic kinetics and reaction condition effects that are common across all six enzyme classes. Special attention is devoted to immobilization strategies as the main tools to improve the resistance to environmental stress factors (temperature, pH and solvents) and prolong the catalytic lifecycle of these biocatalysts. The advantages and drawbacks of methods such as macromolecular crosslinking, solid scaffold carriers, entrapment, and surface modification (covalent and physical) are discussed and illustrated using numerous examples. Among the hundreds and possibly thousands of known and recently discovered enzymes, hydrolases and oxidoreductases are distinguished by their relative availability, stability, and wide use in synthetic applications, which include pharmaceutics, food and beverage treatments, environmental clean-up, and polymerizations. Two representatives of those groups—laccase (an oxidoreductase) and lipase (a hydrolase)—are discussed at length, including their structure, catalytic mechanism, and diverse usage. Objective representation of the current status and emerging trends are provided in the main conclusions. |
| first_indexed | 2024-04-25T00:23:59Z |
| format | Article |
| id | doaj.art-03e574eb49984c24abf55762cdad15c1 |
| institution | Directory Open Access Journal |
| issn | 1420-3049 |
| language | English |
| last_indexed | 2024-04-25T00:23:59Z |
| publishDate | 2024-02-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Molecules |
| spelling | doaj.art-03e574eb49984c24abf55762cdad15c12024-03-12T16:50:40ZengMDPI AGMolecules1420-30492024-02-0129598910.3390/molecules29050989Enzymes in “Green” Synthetic Chemistry: Laccase and LipaseDieter M. Scheibel0Ioan Pavel Ivanov Gitsov1Ivan Gitsov2Department of Chemistry, State University of New York-ESF, Syracuse, NY 13210, USAScience and Technology, Medtronic Incorporated, 710 Medtronic Parkway, Minneapolis, MN 55432, USADepartment of Chemistry, State University of New York-ESF, Syracuse, NY 13210, USAEnzymes play an important role in numerous natural processes and are increasingly being utilized as environmentally friendly substitutes and alternatives to many common catalysts. Their essential advantages are high catalytic efficiency, substrate specificity, minimal formation of byproducts, and low energy demand. All of these benefits make enzymes highly desirable targets of academic research and industrial development. This review has the modest aim of briefly overviewing the classification, mechanism of action, basic kinetics and reaction condition effects that are common across all six enzyme classes. Special attention is devoted to immobilization strategies as the main tools to improve the resistance to environmental stress factors (temperature, pH and solvents) and prolong the catalytic lifecycle of these biocatalysts. The advantages and drawbacks of methods such as macromolecular crosslinking, solid scaffold carriers, entrapment, and surface modification (covalent and physical) are discussed and illustrated using numerous examples. Among the hundreds and possibly thousands of known and recently discovered enzymes, hydrolases and oxidoreductases are distinguished by their relative availability, stability, and wide use in synthetic applications, which include pharmaceutics, food and beverage treatments, environmental clean-up, and polymerizations. Two representatives of those groups—laccase (an oxidoreductase) and lipase (a hydrolase)—are discussed at length, including their structure, catalytic mechanism, and diverse usage. Objective representation of the current status and emerging trends are provided in the main conclusions.https://www.mdpi.com/1420-3049/29/5/989“green” chemistryenzymesimmobilizationlaccaselipasewine making |
| spellingShingle | Dieter M. Scheibel Ioan Pavel Ivanov Gitsov Ivan Gitsov Enzymes in “Green” Synthetic Chemistry: Laccase and Lipase Molecules “green” chemistry enzymes immobilization laccase lipase wine making |
| title | Enzymes in “Green” Synthetic Chemistry: Laccase and Lipase |
| title_full | Enzymes in “Green” Synthetic Chemistry: Laccase and Lipase |
| title_fullStr | Enzymes in “Green” Synthetic Chemistry: Laccase and Lipase |
| title_full_unstemmed | Enzymes in “Green” Synthetic Chemistry: Laccase and Lipase |
| title_short | Enzymes in “Green” Synthetic Chemistry: Laccase and Lipase |
| title_sort | enzymes in green synthetic chemistry laccase and lipase |
| topic | “green” chemistry enzymes immobilization laccase lipase wine making |
| url | https://www.mdpi.com/1420-3049/29/5/989 |
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