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Two-step modification of silica nanoparticles for covalent lipase immobilization

Authorized Users Only
2013
Authors
Prlainović, Nevena
Stojanović, Marija
Carević, Milica
Mihailović, Mladen
Banjanac, Katarina
Marinković, Aleksandar
Bezbradica, Dejan
Conference object (Published version)
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Abstract
Lipases are enzymes very well known for their laboratory and industrial application. Various immobilization supports and techniques were examined in order to improve lipase stability and activity for industrial application. Lipase can be immobilized by adsorption, entrapment or by covalent binding [1]. Different supports are considered for enzyme immobilization, organic or inorganic, natural or synthetic, but there is no unique solution. Ideal support should posses enough active groups to interact with enzyme, but to be inert to reaction media; it should be mechanically stable, renewable for many cycles and inexpensive. Lately, nanoparticles of silica are used for enzyme immobilization because of its extremely high surface area and controllable pore size. Nanoparticles of silica are characterized by surface to volume ratio that is significantly higher than commonly used supports. Some of the authors have also presented that nanoparticles of silica have stabilization effect f...or the immobilized enzyme molecules[2]. Also in some cases immobilization on nanoparticles also provides temperature stability of immobilized enzyme[3]. In this study, nanoparticles of silica were modified in two-step process. The goal was to introduce new reactive groups on silica surface, and make silica surface more suitable for immobilization of lipase. In first step, nanoparticles of silica were treated with (3- aminopropyl)-trimethoxysilane (APTMS), and then in step two, silica particles were treated with cyanuric chloride (CTC) (temperature and molar ratio silica/CTC were variated). This way nanoparticle of silica became rich in chloride groups, which enabled covalent immobilization of lipase. FTIR analysis was performed after each modification step, and confirmed presence of new active groups. Better results were obtained when second step of modification was performed at 0 °C and high molar ratio silica/CTC. Lipase from Candida rugosa was immobilized on modified nanoparticles of silica. Amount of proteins bound was in range between 55 and 78%, but activity retention after immobilization process was approximately 30%. Immobilized enzyme was used in reaction of aroma ester synthesis, and reached conversion rate of 30% within 8 h.

Source:
8th International Conference of the Chemical Societies of the South-East European Countries, Belgrade, Serbia, 2013, 178-

ISBN: 978-86-7132-053-5

[ Google Scholar ]
Handle
https://hdl.handle.net/21.15107/rcub_technorep_6072
URI
http://TechnoRep.tmf.bg.ac.rs/handle/123456789/6072
Collections
  • Radovi istraživača / Researchers’ publications (TMF)
Institution/Community
Tehnološko-metalurški fakultet
TY  - CONF
AU  - Prlainović, Nevena
AU  - Stojanović, Marija
AU  - Carević, Milica
AU  - Mihailović, Mladen
AU  - Banjanac, Katarina
AU  - Marinković, Aleksandar
AU  - Bezbradica, Dejan
PY  - 2013
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/6072
AB  - Lipases are enzymes very well known for their laboratory and industrial application.
Various immobilization supports and techniques were examined in order to improve lipase
stability and activity for industrial application. Lipase can be immobilized by adsorption,
entrapment or by covalent binding [1]. Different supports are considered for enzyme
immobilization, organic or inorganic, natural or synthetic, but there is no unique solution.
Ideal support should posses enough active groups to interact with enzyme, but to be inert
to reaction media; it should be mechanically stable, renewable for many cycles and
inexpensive. Lately, nanoparticles of silica are used for enzyme immobilization because of
its extremely high surface area and controllable pore size. Nanoparticles of silica are
characterized by surface to volume ratio that is significantly higher than commonly used
supports. Some of the authors have also presented that nanoparticles of silica have
stabilization effect for the immobilized enzyme molecules[2]. Also in some cases
immobilization on nanoparticles also provides temperature stability of immobilized
enzyme[3].
In this study, nanoparticles of silica were modified in two-step process. The goal was to
introduce new reactive groups on silica surface, and make silica surface more suitable for
immobilization of lipase. In first step, nanoparticles of silica were treated with (3-
aminopropyl)-trimethoxysilane (APTMS), and then in step two, silica particles were treated
with cyanuric chloride (CTC) (temperature and molar ratio silica/CTC were variated). This
way nanoparticle of silica became rich in chloride groups, which enabled covalent
immobilization of lipase. FTIR analysis was performed after each modification step, and
confirmed presence of new active groups. Better results were obtained when second step
of modification was performed at 0 °C and high molar ratio silica/CTC. Lipase from
Candida rugosa was immobilized on modified nanoparticles of silica. Amount of proteins
bound was in range between 55 and 78%, but activity retention after immobilization
process was approximately 30%. Immobilized enzyme was used in reaction of aroma ester
synthesis, and reached conversion rate of 30% within 8 h.
C3  - 8th International Conference of the Chemical Societies of the South-East European Countries, Belgrade, Serbia
T1  - Two-step modification of silica nanoparticles for covalent lipase immobilization
SP  - 178
UR  - https://hdl.handle.net/21.15107/rcub_technorep_6072
ER  - 
@conference{
author = "Prlainović, Nevena and Stojanović, Marija and Carević, Milica and Mihailović, Mladen and Banjanac, Katarina and Marinković, Aleksandar and Bezbradica, Dejan",
year = "2013",
abstract = "Lipases are enzymes very well known for their laboratory and industrial application.
Various immobilization supports and techniques were examined in order to improve lipase
stability and activity for industrial application. Lipase can be immobilized by adsorption,
entrapment or by covalent binding [1]. Different supports are considered for enzyme
immobilization, organic or inorganic, natural or synthetic, but there is no unique solution.
Ideal support should posses enough active groups to interact with enzyme, but to be inert
to reaction media; it should be mechanically stable, renewable for many cycles and
inexpensive. Lately, nanoparticles of silica are used for enzyme immobilization because of
its extremely high surface area and controllable pore size. Nanoparticles of silica are
characterized by surface to volume ratio that is significantly higher than commonly used
supports. Some of the authors have also presented that nanoparticles of silica have
stabilization effect for the immobilized enzyme molecules[2]. Also in some cases
immobilization on nanoparticles also provides temperature stability of immobilized
enzyme[3].
In this study, nanoparticles of silica were modified in two-step process. The goal was to
introduce new reactive groups on silica surface, and make silica surface more suitable for
immobilization of lipase. In first step, nanoparticles of silica were treated with (3-
aminopropyl)-trimethoxysilane (APTMS), and then in step two, silica particles were treated
with cyanuric chloride (CTC) (temperature and molar ratio silica/CTC were variated). This
way nanoparticle of silica became rich in chloride groups, which enabled covalent
immobilization of lipase. FTIR analysis was performed after each modification step, and
confirmed presence of new active groups. Better results were obtained when second step
of modification was performed at 0 °C and high molar ratio silica/CTC. Lipase from
Candida rugosa was immobilized on modified nanoparticles of silica. Amount of proteins
bound was in range between 55 and 78%, but activity retention after immobilization
process was approximately 30%. Immobilized enzyme was used in reaction of aroma ester
synthesis, and reached conversion rate of 30% within 8 h.",
journal = "8th International Conference of the Chemical Societies of the South-East European Countries, Belgrade, Serbia",
title = "Two-step modification of silica nanoparticles for covalent lipase immobilization",
pages = "178",
url = "https://hdl.handle.net/21.15107/rcub_technorep_6072"
}
Prlainović, N., Stojanović, M., Carević, M., Mihailović, M., Banjanac, K., Marinković, A.,& Bezbradica, D.. (2013). Two-step modification of silica nanoparticles for covalent lipase immobilization. in 8th International Conference of the Chemical Societies of the South-East European Countries, Belgrade, Serbia, 178.
https://hdl.handle.net/21.15107/rcub_technorep_6072
Prlainović N, Stojanović M, Carević M, Mihailović M, Banjanac K, Marinković A, Bezbradica D. Two-step modification of silica nanoparticles for covalent lipase immobilization. in 8th International Conference of the Chemical Societies of the South-East European Countries, Belgrade, Serbia. 2013;:178.
https://hdl.handle.net/21.15107/rcub_technorep_6072 .
Prlainović, Nevena, Stojanović, Marija, Carević, Milica, Mihailović, Mladen, Banjanac, Katarina, Marinković, Aleksandar, Bezbradica, Dejan, "Two-step modification of silica nanoparticles for covalent lipase immobilization" in 8th International Conference of the Chemical Societies of the South-East European Countries, Belgrade, Serbia (2013):178,
https://hdl.handle.net/21.15107/rcub_technorep_6072 .

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