Tubular and Spherical SiO2 Obtained by Sol Gel Method for Lipase Immobilization and Enzymatic Activity

A wide range of hybrid biomaterials has been designed in order to sustain bioremediation processes by associating sol-gel SiO2 matrices with various biologically active compounds (enzymes, antibodies). SiO2 is a widespread, chemically stable and non-toxic material; thus, the immobilization of enzyme...

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Main Authors: Crina Anastasescu, Silviu Preda, Adriana Rusu, Dana Culita, Gabriel Plavan, Stefan Strungaru, Jose Maria Calderon-Moreno, Cornel Munteanu, Catalina Gifu, Mirela Enache, Radu Socoteanu, Daniel Angelescu, Mihai Anastasescu, Mariuca Gartner, Ioan Balint, Maria Zaharescu
Format: Article
Language:English
Published: MDPI AG 2018-06-01
Series:Molecules
Subjects:
Online Access:http://www.mdpi.com/1420-3049/23/6/1362
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spelling doaj-b7943925171548baa0cc59ffa326183f2020-11-24T21:37:58ZengMDPI AGMolecules1420-30492018-06-01236136210.3390/molecules23061362molecules23061362Tubular and Spherical SiO2 Obtained by Sol Gel Method for Lipase Immobilization and Enzymatic ActivityCrina Anastasescu0Silviu Preda1Adriana Rusu2Dana Culita3Gabriel Plavan4Stefan Strungaru5Jose Maria Calderon-Moreno6Cornel Munteanu7Catalina Gifu8Mirela Enache9Radu Socoteanu10Daniel Angelescu11Mihai Anastasescu12Mariuca Gartner13Ioan Balint14Maria Zaharescu15“Ilie Murgulescu” Institute of Physical Chemistry of the Romanian Academy, 060021 Bucharest, Romania“Ilie Murgulescu” Institute of Physical Chemistry of the Romanian Academy, 060021 Bucharest, Romania“Ilie Murgulescu” Institute of Physical Chemistry of the Romanian Academy, 060021 Bucharest, Romania“Ilie Murgulescu” Institute of Physical Chemistry of the Romanian Academy, 060021 Bucharest, RomaniaFaculty of Biology, “Alexandru Ioan Cuza” University, 700505 Iasi, RomaniaFaculty of Biology, “Alexandru Ioan Cuza” University, 700505 Iasi, Romania“Ilie Murgulescu” Institute of Physical Chemistry of the Romanian Academy, 060021 Bucharest, Romania“Ilie Murgulescu” Institute of Physical Chemistry of the Romanian Academy, 060021 Bucharest, RomaniaNational Research and Development Institute for Chemistry and Petrochemistry-ICECHIM, 060021 Bucharest, Romania“Ilie Murgulescu” Institute of Physical Chemistry of the Romanian Academy, 060021 Bucharest, Romania“Ilie Murgulescu” Institute of Physical Chemistry of the Romanian Academy, 060021 Bucharest, Romania“Ilie Murgulescu” Institute of Physical Chemistry of the Romanian Academy, 060021 Bucharest, Romania“Ilie Murgulescu” Institute of Physical Chemistry of the Romanian Academy, 060021 Bucharest, Romania“Ilie Murgulescu” Institute of Physical Chemistry of the Romanian Academy, 060021 Bucharest, Romania“Ilie Murgulescu” Institute of Physical Chemistry of the Romanian Academy, 060021 Bucharest, Romania“Ilie Murgulescu” Institute of Physical Chemistry of the Romanian Academy, 060021 Bucharest, RomaniaA wide range of hybrid biomaterials has been designed in order to sustain bioremediation processes by associating sol-gel SiO2 matrices with various biologically active compounds (enzymes, antibodies). SiO2 is a widespread, chemically stable and non-toxic material; thus, the immobilization of enzymes on silica may lead to improving the efficiency of biocatalysts in terms of endurance and economic costs. Our present work explores the potential of different hybrid morphologies, based on hollow tubes and solid spheres of amorphous SiO2, for enzyme immobilization and the development of competitive biocatalysts. The synthesis protocol and structural characterization of spherical and tubular SiO2 obtained by the sol gel method were fully investigated in connection with the subsequent immobilization of lipase from Rhizopus orizae. The immobilization is conducted at pH 6, lower than the isoelectric point of lipase and higher than the isoelectric point of silica, which is meant to sustain the physical interactions of the enzyme with the SiO2 matrix. The morphological, textural and surface properties of spherical and tubular SiO2 were investigated by SEM, nitrogen sorption, and electrokinetic potential measurements, while the formation and characterization of hybrid organic-inorganic complexes were studied by UV-VIS, FTIR-ATR and fluorescence spectroscopy. The highest degree of enzyme immobilization (as depicted from total organic carbon) was achieved for tubular morphology and the hydrolysis of p-nitrophenyl acetate was used as an enzymatic model reaction conducted in the presence of hybrid lipase–SiO2 complex.http://www.mdpi.com/1420-3049/23/6/1362SiO2tubular and spherical morphologylipase immobilizationenzymatic catalysis
collection DOAJ
language English
format Article
sources DOAJ
author Crina Anastasescu
Silviu Preda
Adriana Rusu
Dana Culita
Gabriel Plavan
Stefan Strungaru
Jose Maria Calderon-Moreno
Cornel Munteanu
Catalina Gifu
Mirela Enache
Radu Socoteanu
Daniel Angelescu
Mihai Anastasescu
Mariuca Gartner
Ioan Balint
Maria Zaharescu
spellingShingle Crina Anastasescu
Silviu Preda
Adriana Rusu
Dana Culita
Gabriel Plavan
Stefan Strungaru
Jose Maria Calderon-Moreno
Cornel Munteanu
Catalina Gifu
Mirela Enache
Radu Socoteanu
Daniel Angelescu
Mihai Anastasescu
Mariuca Gartner
Ioan Balint
Maria Zaharescu
Tubular and Spherical SiO2 Obtained by Sol Gel Method for Lipase Immobilization and Enzymatic Activity
Molecules
SiO2
tubular and spherical morphology
lipase immobilization
enzymatic catalysis
author_facet Crina Anastasescu
Silviu Preda
Adriana Rusu
Dana Culita
Gabriel Plavan
Stefan Strungaru
Jose Maria Calderon-Moreno
Cornel Munteanu
Catalina Gifu
Mirela Enache
Radu Socoteanu
Daniel Angelescu
Mihai Anastasescu
Mariuca Gartner
Ioan Balint
Maria Zaharescu
author_sort Crina Anastasescu
title Tubular and Spherical SiO2 Obtained by Sol Gel Method for Lipase Immobilization and Enzymatic Activity
title_short Tubular and Spherical SiO2 Obtained by Sol Gel Method for Lipase Immobilization and Enzymatic Activity
title_full Tubular and Spherical SiO2 Obtained by Sol Gel Method for Lipase Immobilization and Enzymatic Activity
title_fullStr Tubular and Spherical SiO2 Obtained by Sol Gel Method for Lipase Immobilization and Enzymatic Activity
title_full_unstemmed Tubular and Spherical SiO2 Obtained by Sol Gel Method for Lipase Immobilization and Enzymatic Activity
title_sort tubular and spherical sio2 obtained by sol gel method for lipase immobilization and enzymatic activity
publisher MDPI AG
series Molecules
issn 1420-3049
publishDate 2018-06-01
description A wide range of hybrid biomaterials has been designed in order to sustain bioremediation processes by associating sol-gel SiO2 matrices with various biologically active compounds (enzymes, antibodies). SiO2 is a widespread, chemically stable and non-toxic material; thus, the immobilization of enzymes on silica may lead to improving the efficiency of biocatalysts in terms of endurance and economic costs. Our present work explores the potential of different hybrid morphologies, based on hollow tubes and solid spheres of amorphous SiO2, for enzyme immobilization and the development of competitive biocatalysts. The synthesis protocol and structural characterization of spherical and tubular SiO2 obtained by the sol gel method were fully investigated in connection with the subsequent immobilization of lipase from Rhizopus orizae. The immobilization is conducted at pH 6, lower than the isoelectric point of lipase and higher than the isoelectric point of silica, which is meant to sustain the physical interactions of the enzyme with the SiO2 matrix. The morphological, textural and surface properties of spherical and tubular SiO2 were investigated by SEM, nitrogen sorption, and electrokinetic potential measurements, while the formation and characterization of hybrid organic-inorganic complexes were studied by UV-VIS, FTIR-ATR and fluorescence spectroscopy. The highest degree of enzyme immobilization (as depicted from total organic carbon) was achieved for tubular morphology and the hydrolysis of p-nitrophenyl acetate was used as an enzymatic model reaction conducted in the presence of hybrid lipase–SiO2 complex.
topic SiO2
tubular and spherical morphology
lipase immobilization
enzymatic catalysis
url http://www.mdpi.com/1420-3049/23/6/1362
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