Covalent Anchoring of Chloroperoxidase and Glucose Oxidase on the Mesoporous Molecular Sieve SBA-15

Publikationstyp:
Zeitschriftenaufsatz
Metadaten:
Autoren
Autoren-URL
https://www.webofscience.com/api/gateway?GWVersion=2&SrcApp=fis-test-1&SrcAuth=WosAPI&KeyUT=WOS:000274973500023&DestLinkType=FullRecord&DestApp=WOS_CPL
DOI
10.3390/ijms11020762
Externe Identifier
  • Clarivate Analytics Document Solution ID: 561JV
  • PubMed Identifier: 20386667
ISSN
1422-0067
Ausgabe der Veröffentlichung
2
Zeitschrift
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
Schlüsselwörter
  • functionalization
  • mesoporous silica
  • enzyme immobilization
Paginierung
762 - 778
Datum der Veröffentlichung
2010
Status
Published
Titel
Covalent Anchoring of Chloroperoxidase and Glucose Oxidase on the Mesoporous Molecular Sieve SBA-15
Sub types
  • Article
Ausgabe der Zeitschrift
11

Datenquelle: Web of Science (Lite)

Andere Metadatenquellen:
Abstract
<jats:p>Functionalization of porous solids plays an important role in many areas, including heterogeneous catalysis and enzyme immobilization. In this study, large-pore ordered mesoporous SBA-15 molecular sieves were synthesized with tetraethyl orthosilicate (TEOS) in the presence of the non-ionic triblock co-polymer Pluronic P123 under acidic conditions. These materials were grafted with 3 aminopropyltrimethoxysilane (ATS), 3-glycidoxypropyltrimethoxysilane (GTS) and with 3 aminopropyltrimethoxysilane and glutaraldehyde (GA-ATS) in order to provide covalent anchoring points for enzymes. The samples were characterized by nitrogen adsorption, powder X-ray diffraction, solid-state NMR spectroscopy, elemental analysis, diffuse reflectance fourier transform infrared spectroscopy and diffuse reflectance UV/Vis spectroscopy. The obtained grafted materials were then used for the immobilization of chloroperoxidase (CPO) and glucose oxidase (GOx) and the resulting biocatalysts were tested in the oxidation of indole. It is found that enzymes anchored to the mesoporous host by the organic moieties can be stored for weeks without losing their activity. Furthermore, the covalently linked enzymes are shown to be less prone to leaching than the physically adsorbed enzymes, as tested in a fixed-bed reactor under continuous operation conditions.</jats:p>
Autoren
DOI
10.3390/ijms11020762
eISSN
1422-0067
Ausgabe der Veröffentlichung
2
Zeitschrift
International Journal of Molecular Sciences
Sprache
en
Online publication date
2010
Paginierung
762 - 778
Status
Published online
Herausgeber
MDPI AG
Herausgeber URL
http://dx.doi.org/10.3390/ijms11020762
Datum der Datenerfassung
2024
Titel
Covalent Anchoring of Chloroperoxidase and Glucose Oxidase on the Mesoporous Molecular Sieve SBA-15
Ausgabe der Zeitschrift
11

Datenquelle: Crossref

Abstract
Functionalization of porous solids plays an important role in many areas, including heterogeneous catalysis and enzyme immobilization. In this study, large-pore ordered mesoporous SBA-15 molecular sieves were synthesized with tetraethyl orthosilicate (TEOS) in the presence of the non-ionic triblock co-polymer Pluronic P123 under acidic conditions. These materials were grafted with 3-aminopropyltrimethoxysilane (ATS), 3-glycidoxypropyltrimethoxysilane (GTS) and with 3-aminopropyltrimethoxysilane and glutaraldehyde (GA-ATS) in order to provide covalent anchoring points for enzymes. The samples were characterized by nitrogen adsorption, powder X-ray diffraction, solid-state NMR spectroscopy, elemental analysis, diffuse reflectance fourier transform infrared spectroscopy and diffuse reflectance UV/Vis spectroscopy. The obtained grafted materials were then used for the immobilization of chloroperoxidase (CPO) and glucose oxidase (GOx) and the resulting biocatalysts were tested in the oxidation of indole. It is found that enzymes anchored to the mesoporous host by the organic moieties can be stored for weeks without losing their activity. Furthermore, the covalently linked enzymes are shown to be less prone to leaching than the physically adsorbed enzymes, as tested in a fixed-bed reactor under continuous operation conditions.
Addresses
  • Erlangen Catalysis Resource Center, Universität Erlangen Nürnberg, Germany. dirk.jung@ecrc.uni-erlangen.de
Autoren
DOI
10.3390/ijms11020762
eISSN
1422-0067
Externe Identifier
  • PubMed Identifier: 20386667
  • PubMed Central ID: PMC2852867
Open access
true
ISSN
1422-0067
Ausgabe der Veröffentlichung
2
Zeitschrift
International journal of molecular sciences
Schlüsselwörter
  • Silicon Dioxide
  • Silanes
  • Poloxalene
  • Propylamines
  • Indoles
  • Enzymes, Immobilized
  • Glucose Oxidase
  • Chloride Peroxidase
  • Oxidation-Reduction
  • Porosity
  • Biocatalysis
  • Protein Stability
Sprache
eng
Medium
Electronic
Online publication date
2010
Open access status
Open Access
Paginierung
762 - 778
Datum der Veröffentlichung
2010
Status
Published
Publisher licence
CC BY
Datum der Datenerfassung
2010
Titel
Covalent anchoring of chloroperoxidase and glucose oxidase on the mesoporous molecular sieve SBA-15.
Sub types
  • Research Support, Non-U.S. Gov't
  • research-article
  • Journal Article
Ausgabe der Zeitschrift
11

Files

https://www.mdpi.com/1422-0067/11/2/762/pdf?version=1403139279 https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/20386667/pdf/?tool=EBI https://europepmc.org/articles/PMC2852867?pdf=render

Datenquelle: Europe PubMed Central

Abstract
Functionalization of porous solids plays an important role in many areas, including heterogeneous catalysis and enzyme immobilization. In this study, large-pore ordered mesoporous SBA-15 molecular sieves were synthesized with tetraethyl orthosilicate (TEOS) in the presence of the non-ionic triblock co-polymer Pluronic P123 under acidic conditions. These materials were grafted with 3-aminopropyltrimethoxysilane (ATS), 3-glycidoxypropyltrimethoxysilane (GTS) and with 3-aminopropyltrimethoxysilane and glutaraldehyde (GA-ATS) in order to provide covalent anchoring points for enzymes. The samples were characterized by nitrogen adsorption, powder X-ray diffraction, solid-state NMR spectroscopy, elemental analysis, diffuse reflectance fourier transform infrared spectroscopy and diffuse reflectance UV/Vis spectroscopy. The obtained grafted materials were then used for the immobilization of chloroperoxidase (CPO) and glucose oxidase (GOx) and the resulting biocatalysts were tested in the oxidation of indole. It is found that enzymes anchored to the mesoporous host by the organic moieties can be stored for weeks without losing their activity. Furthermore, the covalently linked enzymes are shown to be less prone to leaching than the physically adsorbed enzymes, as tested in a fixed-bed reactor under continuous operation conditions.
Date of acceptance
2010
Autoren
Autoren-URL
https://www.ncbi.nlm.nih.gov/pubmed/20386667
DOI
10.3390/ijms11020762
eISSN
1422-0067
Externe Identifier
  • PubMed Central ID: PMC2852867
Ausgabe der Veröffentlichung
2
Zeitschrift
Int J Mol Sci
Schlüsselwörter
  • enzyme immobilization
  • functionalization
  • mesoporous silica
  • Biocatalysis
  • Chloride Peroxidase
  • Enzymes, Immobilized
  • Glucose Oxidase
  • Indoles
  • Oxidation-Reduction
  • Poloxalene
  • Porosity
  • Propylamines
  • Protein Stability
  • Silanes
  • Silicon Dioxide
Sprache
eng
Country
Switzerland
Paginierung
762 - 778
PII
ijms11020762
Datum der Veröffentlichung
2010
Status
Published online
Datum, an dem der Datensatz öffentlich gemacht wurde
2014
Titel
Covalent anchoring of chloroperoxidase and glucose oxidase on the mesoporous molecular sieve SBA-15.
Sub types
  • Journal Article
  • Research Support, Non-U.S. Gov't
Ausgabe der Zeitschrift
11

Datenquelle: PubMed

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