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Lipase-immobilized chitosan-crosslinked magnetic nanoparticle as a biocatalyst for ring opening esterification of itaconic anhydride

Hosseini, Seyed Mehdi; Kim, Soo Min; Sayed, Mahmoud LU ; Younesi, Habibollah; Bahramifar, Nader; Park, Ji Hoon and Pyo, Sang Hyun LU (2019) In Biochemical Engineering Journal 143. p.141-150
Abstract

Nano-magnetic biocatalyst particles, lipase-immobilized chitosan-crosslinked magnetic nanoparticles (LCMNs) were prepared by a new approach integrated from magnetic nanoparticle preparation, in situ thin layer coating and crosslinking of chitosan, and enzyme immobilization method. Thin layer coating of magnetic (Fe3O4) by crosslinked chitosan nanoparticles were prepared by reacting FeCl3.6H2O and sodium acetate in ethylene glycol, followed by suspension cross-linking using citric acid on the hydroxyl and amine group of chitosan at neutral pH. The resulting nanoparticles were used to immobilize the lipase from Candida antarctica Lipase B by linking using glutaraldehyde. The particles in each... (More)

Nano-magnetic biocatalyst particles, lipase-immobilized chitosan-crosslinked magnetic nanoparticles (LCMNs) were prepared by a new approach integrated from magnetic nanoparticle preparation, in situ thin layer coating and crosslinking of chitosan, and enzyme immobilization method. Thin layer coating of magnetic (Fe3O4) by crosslinked chitosan nanoparticles were prepared by reacting FeCl3.6H2O and sodium acetate in ethylene glycol, followed by suspension cross-linking using citric acid on the hydroxyl and amine group of chitosan at neutral pH. The resulting nanoparticles were used to immobilize the lipase from Candida antarctica Lipase B by linking using glutaraldehyde. The particles in each step were characterized by Fourier transform infrared spectrometry (FT-IR), vibrating-sample magnetometer measurements (VSM), and transmission electron microscopy (TEM). The magnetic biocatalyst, LCMN was found to have high storage stability and reusability due to the tightly crosslinked structure of chitosan and covalent bond immobilization. LCMNs were used for the oligomerization of itaconic anhydride by ring opening esterification, and the results were compared with those from free lipase and commercial immobilized lipase. The molecular mass of the products obtained with the biocatalysts showed similar Mn profiles with 308–381. This process represents a green approach for the preparation of both biobased magnetic biocatalysts and functional oligo-esters, and can be applied for both the immobilization of other enzymes and the utilization of photo-curable functional esters as biobased functional materials.

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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Characterization, Green process and material, Itaconic anhydride, Lipase immobilized magnetic nanochitosan, Magnetic nanochitosan, Ring opening esterification
in
Biochemical Engineering Journal
volume
143
pages
10 pages
publisher
The Association for the Study of Animal Behaviour / Elsevier B.V.
external identifiers
  • scopus:85059231577
ISSN
1369-703X
DOI
10.1016/j.bej.2018.12.022
language
English
LU publication?
yes
id
11fbbd93-ac8a-4389-895f-9d47026bbe5d
date added to LUP
2019-01-10 14:27:36
date last changed
2019-02-20 11:42:32
@article{11fbbd93-ac8a-4389-895f-9d47026bbe5d,
  abstract     = {<p>Nano-magnetic biocatalyst particles, lipase-immobilized chitosan-crosslinked magnetic nanoparticles (LCMNs) were prepared by a new approach integrated from magnetic nanoparticle preparation, in situ thin layer coating and crosslinking of chitosan, and enzyme immobilization method. Thin layer coating of magnetic (Fe<sub>3</sub>O<sub>4</sub>) by crosslinked chitosan nanoparticles were prepared by reacting FeCl<sub>3</sub>.6H<sub>2</sub>O and sodium acetate in ethylene glycol, followed by suspension cross-linking using citric acid on the hydroxyl and amine group of chitosan at neutral pH. The resulting nanoparticles were used to immobilize the lipase from Candida antarctica Lipase B by linking using glutaraldehyde. The particles in each step were characterized by Fourier transform infrared spectrometry (FT-IR), vibrating-sample magnetometer measurements (VSM), and transmission electron microscopy (TEM). The magnetic biocatalyst, LCMN was found to have high storage stability and reusability due to the tightly crosslinked structure of chitosan and covalent bond immobilization. LCMNs were used for the oligomerization of itaconic anhydride by ring opening esterification, and the results were compared with those from free lipase and commercial immobilized lipase. The molecular mass of the products obtained with the biocatalysts showed similar M<sub>n</sub> profiles with 308–381. This process represents a green approach for the preparation of both biobased magnetic biocatalysts and functional oligo-esters, and can be applied for both the immobilization of other enzymes and the utilization of photo-curable functional esters as biobased functional materials.</p>},
  author       = {Hosseini, Seyed Mehdi and Kim, Soo Min and Sayed, Mahmoud and Younesi, Habibollah and Bahramifar, Nader and Park, Ji Hoon and Pyo, Sang Hyun},
  issn         = {1369-703X},
  keyword      = {Characterization,Green process and material,Itaconic anhydride,Lipase immobilized magnetic nanochitosan,Magnetic nanochitosan,Ring opening esterification},
  language     = {eng},
  month        = {03},
  pages        = {141--150},
  publisher    = {The Association for the Study of Animal Behaviour / Elsevier B.V.},
  series       = {Biochemical Engineering Journal},
  title        = {Lipase-immobilized chitosan-crosslinked magnetic nanoparticle as a biocatalyst for ring opening esterification of itaconic anhydride},
  url          = {http://dx.doi.org/10.1016/j.bej.2018.12.022},
  volume       = {143},
  year         = {2019},
}