Immobilization of lipase on hydrophobic nano-sized magnetite particles

Dong Geun Lee, Kanagasabai M. Ponvel, Mir Kim, Sangpill Hwang, Ik Sung Ahn, Chang Ha Lee

Research output: Contribution to journalArticle

130 Citations (Scopus)

Abstract

As a tool for the stable enzyme reuse, enzyme immobilization has been studied for several decades. Surface-modified nano-sized magnetite (S-NSM) particles have been suggested as a support for the immobilization of enzyme in this study. Based on the finding that a lipase is strongly adsorbed onto a hydrophobic surface, NSM particles (8-12 nm) were made hydrophobic by binding of sodium dodecyl sulfate via a sulfate ester bond. Various types of measurements, such as transmission electron microscopy, X-ray diffraction, infrared spectroscopy, vibration sample magnetometer, and thermo gravimetric analysis, were conducted in characterizing S-NSM nanoparticles. S-NSM particles were used for the adsorption of porcine pancreas lipase (PPL). A dodecyl carbon chain is expected to form a spacer between the surface of the NSM and the lipase adsorbed. The immobilized PPL showed the higher specific activity of oil hydrolysis than that of free one. Immobilized PPL could be recovered by magnetic separation, and showed the constant activity during the recycles.

Original languageEnglish
Pages (from-to)62-66
Number of pages5
JournalJournal of Molecular Catalysis B: Enzymatic
Volume57
Issue number1-4
DOIs
Publication statusPublished - 2009 May 1

Fingerprint

Ferrosoferric Oxide
Lipases
Magnetite
Lipase
Immobilization
Pancreas
Swine
Magnetite Nanoparticles
Enzymes
Enzyme immobilization
Magnetite nanoparticles
Magnetic separation
Sodium dodecyl sulfate
Magnetometers
Vibration
Transmission Electron Microscopy
Catalyst supports
X-Ray Diffraction
Sodium Dodecyl Sulfate
Sulfates

All Science Journal Classification (ASJC) codes

  • Catalysis
  • Bioengineering
  • Biochemistry
  • Process Chemistry and Technology

Cite this

Lee, Dong Geun ; Ponvel, Kanagasabai M. ; Kim, Mir ; Hwang, Sangpill ; Ahn, Ik Sung ; Lee, Chang Ha. / Immobilization of lipase on hydrophobic nano-sized magnetite particles. In: Journal of Molecular Catalysis B: Enzymatic. 2009 ; Vol. 57, No. 1-4. pp. 62-66.
@article{a351bfb00ad2403cb3c890a590faacd5,
title = "Immobilization of lipase on hydrophobic nano-sized magnetite particles",
abstract = "As a tool for the stable enzyme reuse, enzyme immobilization has been studied for several decades. Surface-modified nano-sized magnetite (S-NSM) particles have been suggested as a support for the immobilization of enzyme in this study. Based on the finding that a lipase is strongly adsorbed onto a hydrophobic surface, NSM particles (8-12 nm) were made hydrophobic by binding of sodium dodecyl sulfate via a sulfate ester bond. Various types of measurements, such as transmission electron microscopy, X-ray diffraction, infrared spectroscopy, vibration sample magnetometer, and thermo gravimetric analysis, were conducted in characterizing S-NSM nanoparticles. S-NSM particles were used for the adsorption of porcine pancreas lipase (PPL). A dodecyl carbon chain is expected to form a spacer between the surface of the NSM and the lipase adsorbed. The immobilized PPL showed the higher specific activity of oil hydrolysis than that of free one. Immobilized PPL could be recovered by magnetic separation, and showed the constant activity during the recycles.",
author = "Lee, {Dong Geun} and Ponvel, {Kanagasabai M.} and Mir Kim and Sangpill Hwang and Ahn, {Ik Sung} and Lee, {Chang Ha}",
year = "2009",
month = "5",
day = "1",
doi = "10.1016/j.molcatb.2008.06.017",
language = "English",
volume = "57",
pages = "62--66",
journal = "Journal of Molecular Catalysis - B Enzymatic",
issn = "1381-1177",
publisher = "Elsevier",
number = "1-4",

}

Immobilization of lipase on hydrophobic nano-sized magnetite particles. / Lee, Dong Geun; Ponvel, Kanagasabai M.; Kim, Mir; Hwang, Sangpill; Ahn, Ik Sung; Lee, Chang Ha.

In: Journal of Molecular Catalysis B: Enzymatic, Vol. 57, No. 1-4, 01.05.2009, p. 62-66.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Immobilization of lipase on hydrophobic nano-sized magnetite particles

AU - Lee, Dong Geun

AU - Ponvel, Kanagasabai M.

AU - Kim, Mir

AU - Hwang, Sangpill

AU - Ahn, Ik Sung

AU - Lee, Chang Ha

PY - 2009/5/1

Y1 - 2009/5/1

N2 - As a tool for the stable enzyme reuse, enzyme immobilization has been studied for several decades. Surface-modified nano-sized magnetite (S-NSM) particles have been suggested as a support for the immobilization of enzyme in this study. Based on the finding that a lipase is strongly adsorbed onto a hydrophobic surface, NSM particles (8-12 nm) were made hydrophobic by binding of sodium dodecyl sulfate via a sulfate ester bond. Various types of measurements, such as transmission electron microscopy, X-ray diffraction, infrared spectroscopy, vibration sample magnetometer, and thermo gravimetric analysis, were conducted in characterizing S-NSM nanoparticles. S-NSM particles were used for the adsorption of porcine pancreas lipase (PPL). A dodecyl carbon chain is expected to form a spacer between the surface of the NSM and the lipase adsorbed. The immobilized PPL showed the higher specific activity of oil hydrolysis than that of free one. Immobilized PPL could be recovered by magnetic separation, and showed the constant activity during the recycles.

AB - As a tool for the stable enzyme reuse, enzyme immobilization has been studied for several decades. Surface-modified nano-sized magnetite (S-NSM) particles have been suggested as a support for the immobilization of enzyme in this study. Based on the finding that a lipase is strongly adsorbed onto a hydrophobic surface, NSM particles (8-12 nm) were made hydrophobic by binding of sodium dodecyl sulfate via a sulfate ester bond. Various types of measurements, such as transmission electron microscopy, X-ray diffraction, infrared spectroscopy, vibration sample magnetometer, and thermo gravimetric analysis, were conducted in characterizing S-NSM nanoparticles. S-NSM particles were used for the adsorption of porcine pancreas lipase (PPL). A dodecyl carbon chain is expected to form a spacer between the surface of the NSM and the lipase adsorbed. The immobilized PPL showed the higher specific activity of oil hydrolysis than that of free one. Immobilized PPL could be recovered by magnetic separation, and showed the constant activity during the recycles.

UR - http://www.scopus.com/inward/record.url?scp=68649097889&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=68649097889&partnerID=8YFLogxK

U2 - 10.1016/j.molcatb.2008.06.017

DO - 10.1016/j.molcatb.2008.06.017

M3 - Article

AN - SCOPUS:68649097889

VL - 57

SP - 62

EP - 66

JO - Journal of Molecular Catalysis - B Enzymatic

JF - Journal of Molecular Catalysis - B Enzymatic

SN - 1381-1177

IS - 1-4

ER -