Affordable Access

Access to the full text

Enzymatic Synthesis of Formate Ester through Immobilized Lipase and Its Reuse

Authors
  • Baek, Yesol1
  • Lee, Jonghwa1
  • Son, Jemin1
  • Lee, Taek1
  • Sobhan, Abdus
  • Lee, Jinyoung
  • Koo, Sang-Mo2
  • Shin, Weon Ho2
  • Oh, Jong-Min2
  • Park, Chulhwan1
  • 1 (J.S.)
  • 2 (J.-M.O.)
Type
Published Article
Journal
Polymers
Publisher
MDPI AG
Publication Date
Aug 11, 2020
Volume
12
Issue
8
Identifiers
DOI: 10.3390/polym12081802
PMID: 32796735
PMCID: PMC7465053
Source
PubMed Central
Keywords
License
Green

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.

Report this publication

Statistics

Seen <100 times