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. 2020 Aug 11;12(8):1802.
doi: 10.3390/polym12081802.

Enzymatic Synthesis of Formate Ester through Immobilized Lipase and Its Reuse

Affiliations

Enzymatic Synthesis of Formate Ester through Immobilized Lipase and Its Reuse

Yesol Baek et al. Polymers (Basel). .

Abstract

Octyl formate is an important substance used in the perfume industry in products such as cosmetics, perfumes, and flavoring. Octyl formate is mostly produced by chemical catalysts. However, using enzymes as catalysts has gathered increasing interest due to their environment-friendly proprieties. In the present study, we aimed to identify the optimal conditions for the synthesis of octyl formate through immobilized enzyme-mediated esterification. We investigated the effects of enzymatic reaction parameters including the type of immobilized enzyme, enzyme concentration, molar ratio of reactants, reaction temperature, and type of solvent using the optimization method of one factor at a time (OFAT). The maximum conversion achieved was 96.51% with Novozym 435 (15 g/L), a 1:7 formic acid to octanol ratio, a reaction temperature of 40 °C, and with 1,2-dichloroethane as solvent. Moreover, we demonstrated that the Novozym 435 can be reused under the optimal conditions without affecting the octyl formate yield, which could help reduce the economic burden associated with enzymatic synthesis.

Keywords: conversion; immobilized enzyme; lipase; octyl formate; reusability.

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Conflict of interest statement

The authors declare no conflicts of interest.

Figures

Figure 1
Figure 1
Lipase-catalyzed reactions.
Figure 2
Figure 2
Conversion of octyl formate using commercial lipases.
Figure 3
Figure 3
Effect of the selected lipase concentrations on the octyl formate conversion.
Figure 4
Figure 4
Effect of molar ratio of octyl formic acid and octanol on the octyl formate conversion.
Figure 5
Figure 5
Effect of reaction temperature on the octyl formate conversion.
Figure 6
Figure 6
Conversion of octyl formate using various solvents.
Figure 7
Figure 7
Reusability of selected lipase for high conversion of octyl formate.

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