Enzymes in "Green" Synthetic Chemistry: Laccase and Lipase

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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Bibliographic Details
Published in:Molecules (Basel, Switzerland) Vol. 29; no. 5; p. 989
Main Authors: Scheibel, Dieter M, Gitsov, Ioan Pavel Ivanov, Gitsov, Ivan
Format: Journal Article
Language:English
Published: Switzerland MDPI AG 24-02-2024
MDPI
Subjects:
Amino acids
Biocatalysts
Catalysis
Chemistry
Crosslinked polymers
Economic development
Enzyme kinetics
enzymes
Enzymes, Immobilized - chemistry
immobilization
laccase
Laccase - chemistry
Lipase
Lipase - chemistry
Macromolecular Substances
Metabolism
Oxidases
Protons
Review
wine making
“green” chemistry
polymerization
polyphenols
immobilization
laccase
lipase
enzymes
linear-dendritic copolymers
“green” chemistry
wine making
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Summary: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.
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ISSN:1420-3049
1420-3049
DOI:10.3390/molecules29050989