Pectinases immobilization on magnetic nanoparticles and their anti-fouling performance in a biocatalytic membrane reactor. Issue 101 (17th October 2016)
- Record Type:
- Journal Article
- Title:
- Pectinases immobilization on magnetic nanoparticles and their anti-fouling performance in a biocatalytic membrane reactor. Issue 101 (17th October 2016)
- Main Title:
- Pectinases immobilization on magnetic nanoparticles and their anti-fouling performance in a biocatalytic membrane reactor
- Authors:
- Gebreyohannes, Abaynesh Yihdego
Mazzei, Rosalinda
Poerio, Teresa
Aimar, Pierre
Vankelecom, Ivo F. J.
Giorno, Lidietta - Abstract:
- Abstract : Reversible enzyme immobilization on membrane using magneto-responsive bionanocomposites, magneto-responsive mixed matrix membrane and an external magnetic field for in situ membrane biocatalysis. Abstract : Enzyme immobilization on commercial superparamagnetic nanoparticles (NP SP ) was performed using covalent bonding. The biofunctionalized NP SP was then immobilized on the surface of the membrane using an external magnetic field to form a magneto-responsive biocatalytic membrane reactor (BMR SP ). The magnetically formed smart nanolayer can be easily re-dispersed and recovered from the membrane when the enzyme is deactivated or whenever cleaning is required due to substrate over-accumulation. The system was used to hydrolyze pectin contained in different streams. Results are supported with complementary data from hydrodynamic, kinetic and morphological characterization in a flow-through reactive filtration. Wavelength-dispersive X-ray spectroscopy (WDS) elemental mapping revealed that the NP SP are uniformly dispersed on the surface of the membrane forming a thin biocatalytic layer. Both results of hydrodynamic studies and SEM micrographs of the membrane with the enzyme layer under various operating conditions, show that the immobilized enzyme effectively reduced membrane–foulant interaction. Comparison of filtration data using this commercial NP SP reveals good agreement with our previously used home-made NP SP . This implies that the scaling-up andAbstract : Reversible enzyme immobilization on membrane using magneto-responsive bionanocomposites, magneto-responsive mixed matrix membrane and an external magnetic field for in situ membrane biocatalysis. Abstract : Enzyme immobilization on commercial superparamagnetic nanoparticles (NP SP ) was performed using covalent bonding. The biofunctionalized NP SP was then immobilized on the surface of the membrane using an external magnetic field to form a magneto-responsive biocatalytic membrane reactor (BMR SP ). The magnetically formed smart nanolayer can be easily re-dispersed and recovered from the membrane when the enzyme is deactivated or whenever cleaning is required due to substrate over-accumulation. The system was used to hydrolyze pectin contained in different streams. Results are supported with complementary data from hydrodynamic, kinetic and morphological characterization in a flow-through reactive filtration. Wavelength-dispersive X-ray spectroscopy (WDS) elemental mapping revealed that the NP SP are uniformly dispersed on the surface of the membrane forming a thin biocatalytic layer. Both results of hydrodynamic studies and SEM micrographs of the membrane with the enzyme layer under various operating conditions, show that the immobilized enzyme effectively reduced membrane–foulant interaction. Comparison of filtration data using this commercial NP SP reveals good agreement with our previously used home-made NP SP . This implies that the scaling-up and commercialization of the developed BMR SP can be straightforward. … (more)
- Is Part Of:
- RSC advances. Volume 6:Issue 101(2016)
- Journal:
- RSC advances
- Issue:
- Volume 6:Issue 101(2016)
- Issue Display:
- Volume 6, Issue 101 (2016)
- Year:
- 2016
- Volume:
- 6
- Issue:
- 101
- Issue Sort Value:
- 2016-0006-0101-0000
- Page Start:
- 98737
- Page End:
- 98747
- Publication Date:
- 2016-10-17
- Subjects:
- Chemistry -- Periodicals
540.5 - Journal URLs:
- http://pubs.rsc.org/en/Journals/JournalIssues/RA ↗
http://www.rsc.org/ ↗ - DOI:
- 10.1039/c6ra20455d ↗
- Languages:
- English
- ISSNs:
- 2046-2069
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 8036.750300
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 1296.xml