Lipase as Biocatalyst- for Synthesis of Phenol by Using Box-Behnken Design

This work highlighted the proficient and naturally safe methodology for the phenol synthesis using biocatalyst lipase. The development of sustainable synthetic protocol for various organic transformations is an important area of research attracts researchers to avoid use of volatile and hazardous or...

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Bibliographic Details
Published in:Polycyclic aromatic compounds 2024-07, Vol.44 (6), p.4261-4272
Main Authors: Kapale, Suraj S., Gaike, Hanuman, Chaudhari, Hemchandra K.
Format: Article
Language:English
Subjects:
arylboronic acid
Biocatalysts
Catalysts
Catalytic activity
Chemical synthesis
Design of experiments
Design optimization
Experimental design
green chemistry
Hazardous areas
ipso hydroxylation
Lipase
Mathematical models
Organic solvents
phenol
Phenols
Purity
Substrates
Sustainable development
Temperature effects
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Summary:This work highlighted the proficient and naturally safe methodology for the phenol synthesis using biocatalyst lipase. The development of sustainable synthetic protocol for various organic transformations is an important area of research attracts researchers to avoid use of volatile and hazardous organic solvents in reaction for greener and eco-friendly protocols. Lipase is subclass of esterase enzymes and acts as biocatalyst with industrial significance. They carry out biochemical transformation in non-aqueous and aqueous phases quickly. To further make the process more specific Design Expert software was used for the optimization of synthesize phenol for maximum % Yield and % Purity. Effect of temperature, Concentration of Catalyst, and Volume of Water was selected as an independent factor to get the maximum % Yield and % Purity of the phenol. The results confirmed the mathematical model robustness and justify experimental design. Therefore, the current protocol for synthesis of phenols from phenylboronic acid is greenest and environmentally benign alternative. The current convention has many benefits, like phenomenal product yields, reduced time of reaction, simple procedure to work up, and extensive substrate scope, cost-effective and also lipase was recuperated and reused multiple times without significant loss of its catalytic activity.
ISSN:1040-6638
1563-5333
DOI:10.1080/10406638.2023.2247123