Enzyme-catalyzed resolution of racemate using enzyme functionalized silica nanoparticles in the presence of surfactants

Yoon Seok Song, Hee Uk Lee, Jong Ho Lee, Chulhwan Park, Seung Wook Kim

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

The enzyme-catalyzed resolution of racemic naproxen 2,2,2-trifluoroethyl thioester was performed by the immobilization of lipase on silica nanoparticles using a covalent bonding method. To increase the conversion and reaction rate of this resolution, we investigated the effect of non-ionic surfactants (M-SA 1025 and SM 20). The optimal reaction conditions such as temperature and loading amount of immobilized lipase were also determined. The addition of M-SA 1025 resulted in the increase in reaction rate (VS), conversion (X S) and enantioselectivity (E value) comparison with SM 20 and the control. The reaction performed in a mixture containing M-SA 1025 at 50 °C with 80 U/mL of immobilized lipase markedly improved the resolution of racemic naproxen 2,2,2-trifluoroethyl thioester compared to other conditions.

Original languageEnglish
Pages (from-to)817-820
Number of pages4
JournalProcess Biochemistry
Volume46
Issue number3
DOIs
Publication statusPublished - 2011 Mar 1

Fingerprint

Lipases
Lipase
Surface-Active Agents
Silicon Dioxide
Nanoparticles
Surface active agents
Enzymes
Silica
Reaction rates
Conversion Disorder
Enantioselectivity
Nonionic surfactants
Immobilization
Temperature
naproxen 2,2,2-trifluoroethyl thioester

Keywords

  • Immobilization
  • Lipase
  • Naproxen
  • Resolution
  • Silica nanoparticle
  • Surfactant

ASJC Scopus subject areas

  • Biochemistry
  • Applied Microbiology and Biotechnology
  • Bioengineering

Cite this

Enzyme-catalyzed resolution of racemate using enzyme functionalized silica nanoparticles in the presence of surfactants. / Song, Yoon Seok; Lee, Hee Uk; Lee, Jong Ho; Park, Chulhwan; Kim, Seung Wook.

In: Process Biochemistry, Vol. 46, No. 3, 01.03.2011, p. 817-820.

Research output: Contribution to journalArticle

Song, Yoon Seok ; Lee, Hee Uk ; Lee, Jong Ho ; Park, Chulhwan ; Kim, Seung Wook. / Enzyme-catalyzed resolution of racemate using enzyme functionalized silica nanoparticles in the presence of surfactants. In: Process Biochemistry. 2011 ; Vol. 46, No. 3. pp. 817-820.
@article{cb313f062fa74f98bb74d37223f13a45,
title = "Enzyme-catalyzed resolution of racemate using enzyme functionalized silica nanoparticles in the presence of surfactants",
abstract = "The enzyme-catalyzed resolution of racemic naproxen 2,2,2-trifluoroethyl thioester was performed by the immobilization of lipase on silica nanoparticles using a covalent bonding method. To increase the conversion and reaction rate of this resolution, we investigated the effect of non-ionic surfactants (M-SA 1025 and SM 20). The optimal reaction conditions such as temperature and loading amount of immobilized lipase were also determined. The addition of M-SA 1025 resulted in the increase in reaction rate (VS), conversion (X S) and enantioselectivity (E value) comparison with SM 20 and the control. The reaction performed in a mixture containing M-SA 1025 at 50 °C with 80 U/mL of immobilized lipase markedly improved the resolution of racemic naproxen 2,2,2-trifluoroethyl thioester compared to other conditions.",
keywords = "Immobilization, Lipase, Naproxen, Resolution, Silica nanoparticle, Surfactant",
author = "Song, {Yoon Seok} and Lee, {Hee Uk} and Lee, {Jong Ho} and Chulhwan Park and Kim, {Seung Wook}",
year = "2011",
month = "3",
day = "1",
doi = "10.1016/j.procbio.2010.12.010",
language = "English",
volume = "46",
pages = "817--820",
journal = "Process Biochemistry",
issn = "1359-5113",
publisher = "Elsevier BV",
number = "3",

}

TY - JOUR

T1 - Enzyme-catalyzed resolution of racemate using enzyme functionalized silica nanoparticles in the presence of surfactants

AU - Song, Yoon Seok

AU - Lee, Hee Uk

AU - Lee, Jong Ho

AU - Park, Chulhwan

AU - Kim, Seung Wook

PY - 2011/3/1

Y1 - 2011/3/1

N2 - The enzyme-catalyzed resolution of racemic naproxen 2,2,2-trifluoroethyl thioester was performed by the immobilization of lipase on silica nanoparticles using a covalent bonding method. To increase the conversion and reaction rate of this resolution, we investigated the effect of non-ionic surfactants (M-SA 1025 and SM 20). The optimal reaction conditions such as temperature and loading amount of immobilized lipase were also determined. The addition of M-SA 1025 resulted in the increase in reaction rate (VS), conversion (X S) and enantioselectivity (E value) comparison with SM 20 and the control. The reaction performed in a mixture containing M-SA 1025 at 50 °C with 80 U/mL of immobilized lipase markedly improved the resolution of racemic naproxen 2,2,2-trifluoroethyl thioester compared to other conditions.

AB - The enzyme-catalyzed resolution of racemic naproxen 2,2,2-trifluoroethyl thioester was performed by the immobilization of lipase on silica nanoparticles using a covalent bonding method. To increase the conversion and reaction rate of this resolution, we investigated the effect of non-ionic surfactants (M-SA 1025 and SM 20). The optimal reaction conditions such as temperature and loading amount of immobilized lipase were also determined. The addition of M-SA 1025 resulted in the increase in reaction rate (VS), conversion (X S) and enantioselectivity (E value) comparison with SM 20 and the control. The reaction performed in a mixture containing M-SA 1025 at 50 °C with 80 U/mL of immobilized lipase markedly improved the resolution of racemic naproxen 2,2,2-trifluoroethyl thioester compared to other conditions.

KW - Immobilization

KW - Lipase

KW - Naproxen

KW - Resolution

KW - Silica nanoparticle

KW - Surfactant

UR - http://www.scopus.com/inward/record.url?scp=79951511778&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=79951511778&partnerID=8YFLogxK

U2 - 10.1016/j.procbio.2010.12.010

DO - 10.1016/j.procbio.2010.12.010

M3 - Article

AN - SCOPUS:79951511778

VL - 46

SP - 817

EP - 820

JO - Process Biochemistry

JF - Process Biochemistry

SN - 1359-5113

IS - 3

ER -