Highly stabilized lipase in polyaniline nanofibers for surfactant-mediated esterification of ibuprofen

Sung Gil Hong, Han Sol Kim, Jungbae Kim

Research output: Contribution to journalArticle

17 Citations (Scopus)

Abstract

Lipase (LP) from Candida rugosa was immobilized and stabilized in polyaniline nanofibers (PANFs) via a three-step process of enzyme adsorption, precipitation, and cross-linking, which generates the final immobilization called "EAPC". The activity of EAPC was 5.1 and 5.9 times higher than those of LP immobilizations via enzyme adsorption (EA) and enzyme adsorption/cross-linking (EAC), respectively. After incubation in an aqueous buffer under shaking (200 rpm) for 84 days, EAPC maintained 74% of its initial activity, while EA and EAC retained 11 and 24% of their initial activities, respectively. Highly stable and active EAPC was employed for the resolution of racemic ibuprofen via esterification of S-(+)-ibuprofen with 1-propanol in isooctane. The addition of 100 mM dioctyl sulfosuccinate (AOT) into the reaction medium increased the esterification activity by 61-fold, which can be explained by the better dispersion of EAPC in isooctane. EAPC showed 42% conversion in the esterification of racemic ibuprofen after 102 h, whereas EA and EAC showed only 1.2 and 1.4% conversion in the same condition, respectively. The EAPC approach increases both loading and stability of LP, and the combination of EAPC with the surfactant addition can be employed for efficient enzymatic reactions in organic solvents.

Original languageEnglish
Pages (from-to)911-915
Number of pages5
JournalLangmuir
Volume30
Issue number3
DOIs
Publication statusPublished - 2014 Jan 28

Fingerprint

Nanofibers
Esterification
Ibuprofen
Lipases
Polyaniline
Lipase
Surface-Active Agents
Adsorption
Surface active agents
enzymes
surfactants
Enzymes
adsorption
immobilization
Immobilization
Dioctyl Sulfosuccinic Acid
1-Propanol
enzyme activity
shaking
Candida

ASJC Scopus subject areas

  • Electrochemistry
  • Condensed Matter Physics
  • Surfaces and Interfaces
  • Materials Science(all)
  • Spectroscopy

Cite this

Highly stabilized lipase in polyaniline nanofibers for surfactant-mediated esterification of ibuprofen. / Hong, Sung Gil; Kim, Han Sol; Kim, Jungbae.

In: Langmuir, Vol. 30, No. 3, 28.01.2014, p. 911-915.

Research output: Contribution to journalArticle

@article{367918c03cac4ec0a877bc679ac57dba,
title = "Highly stabilized lipase in polyaniline nanofibers for surfactant-mediated esterification of ibuprofen",
abstract = "Lipase (LP) from Candida rugosa was immobilized and stabilized in polyaniline nanofibers (PANFs) via a three-step process of enzyme adsorption, precipitation, and cross-linking, which generates the final immobilization called {"}EAPC{"}. The activity of EAPC was 5.1 and 5.9 times higher than those of LP immobilizations via enzyme adsorption (EA) and enzyme adsorption/cross-linking (EAC), respectively. After incubation in an aqueous buffer under shaking (200 rpm) for 84 days, EAPC maintained 74{\%} of its initial activity, while EA and EAC retained 11 and 24{\%} of their initial activities, respectively. Highly stable and active EAPC was employed for the resolution of racemic ibuprofen via esterification of S-(+)-ibuprofen with 1-propanol in isooctane. The addition of 100 mM dioctyl sulfosuccinate (AOT) into the reaction medium increased the esterification activity by 61-fold, which can be explained by the better dispersion of EAPC in isooctane. EAPC showed 42{\%} conversion in the esterification of racemic ibuprofen after 102 h, whereas EA and EAC showed only 1.2 and 1.4{\%} conversion in the same condition, respectively. The EAPC approach increases both loading and stability of LP, and the combination of EAPC with the surfactant addition can be employed for efficient enzymatic reactions in organic solvents.",
author = "Hong, {Sung Gil} and Kim, {Han Sol} and Jungbae Kim",
year = "2014",
month = "1",
day = "28",
doi = "10.1021/la404189e",
language = "English",
volume = "30",
pages = "911--915",
journal = "Langmuir",
issn = "0743-7463",
publisher = "American Chemical Society",
number = "3",

}

TY - JOUR

T1 - Highly stabilized lipase in polyaniline nanofibers for surfactant-mediated esterification of ibuprofen

AU - Hong, Sung Gil

AU - Kim, Han Sol

AU - Kim, Jungbae

PY - 2014/1/28

Y1 - 2014/1/28

N2 - Lipase (LP) from Candida rugosa was immobilized and stabilized in polyaniline nanofibers (PANFs) via a three-step process of enzyme adsorption, precipitation, and cross-linking, which generates the final immobilization called "EAPC". The activity of EAPC was 5.1 and 5.9 times higher than those of LP immobilizations via enzyme adsorption (EA) and enzyme adsorption/cross-linking (EAC), respectively. After incubation in an aqueous buffer under shaking (200 rpm) for 84 days, EAPC maintained 74% of its initial activity, while EA and EAC retained 11 and 24% of their initial activities, respectively. Highly stable and active EAPC was employed for the resolution of racemic ibuprofen via esterification of S-(+)-ibuprofen with 1-propanol in isooctane. The addition of 100 mM dioctyl sulfosuccinate (AOT) into the reaction medium increased the esterification activity by 61-fold, which can be explained by the better dispersion of EAPC in isooctane. EAPC showed 42% conversion in the esterification of racemic ibuprofen after 102 h, whereas EA and EAC showed only 1.2 and 1.4% conversion in the same condition, respectively. The EAPC approach increases both loading and stability of LP, and the combination of EAPC with the surfactant addition can be employed for efficient enzymatic reactions in organic solvents.

AB - Lipase (LP) from Candida rugosa was immobilized and stabilized in polyaniline nanofibers (PANFs) via a three-step process of enzyme adsorption, precipitation, and cross-linking, which generates the final immobilization called "EAPC". The activity of EAPC was 5.1 and 5.9 times higher than those of LP immobilizations via enzyme adsorption (EA) and enzyme adsorption/cross-linking (EAC), respectively. After incubation in an aqueous buffer under shaking (200 rpm) for 84 days, EAPC maintained 74% of its initial activity, while EA and EAC retained 11 and 24% of their initial activities, respectively. Highly stable and active EAPC was employed for the resolution of racemic ibuprofen via esterification of S-(+)-ibuprofen with 1-propanol in isooctane. The addition of 100 mM dioctyl sulfosuccinate (AOT) into the reaction medium increased the esterification activity by 61-fold, which can be explained by the better dispersion of EAPC in isooctane. EAPC showed 42% conversion in the esterification of racemic ibuprofen after 102 h, whereas EA and EAC showed only 1.2 and 1.4% conversion in the same condition, respectively. The EAPC approach increases both loading and stability of LP, and the combination of EAPC with the surfactant addition can be employed for efficient enzymatic reactions in organic solvents.

UR - http://www.scopus.com/inward/record.url?scp=84893514240&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84893514240&partnerID=8YFLogxK

U2 - 10.1021/la404189e

DO - 10.1021/la404189e

M3 - Article

C2 - 24417226

AN - SCOPUS:84893514240

VL - 30

SP - 911

EP - 915

JO - Langmuir

JF - Langmuir

SN - 0743-7463

IS - 3

ER -