Change search
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • harvard1
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf
Development of Protein-Functionalized Magnetic Iron Oxide Nanoparticles: Potential Application in Water Treatment
KTH, School of Chemical Science and Engineering (CHE), Chemical Engineering and Technology, Chemical Technology. KTH, School of Biotechnology (BIO), Industrial Biotechnology.
2012 (English)Doctoral thesis, comprehensive summary (Other academic)
Abstract [en]

The treatment of water to make it safe for human consumption is a problem of immense concern, both in developing and developed countries. However, the production of clean water with chemicals as coagulants has several drawbacks associated with cost, health risks and complexity in sludge management. The application of nanotechnology in water treatment is a fast growing discipline proposed as an efficient alternative that will combat these hurdles. The aim of this thesis is to develop new water treatment strategies in a more eco-friendly manner based on a bottom-up approach using: (i) a natural coagulant protein from Moringa oleifera purified with nanoscale magnetic iron oxide nanoparticles for in situ treatment; and (ii) a protein-functionalized nanoparticle (MOCP-MNPs) system by means of binding the coagulant protein onto the nanoparticles in order to develop a potential reusable water treatment process.

Magnetic iron oxide nanoparticles with different surface chemistry have been prepared from co-precipitation in aqueous solution and (water-in-oil and oil-in-water) microemulsion methods.  

The prepared nanoparticles were studied in terms of size, morphology, magnetic behavior, structure, surface area including surface chemical structure and charges using different techniques such as TEM, VSM/SQUID, XRD, BET, FT-IR and zeta potential. The prepared nanoparticles exhibited a size ranging from 2-30 nm with superparamagnetic properties. The Moringa oleifera  coagulant protein (MOCP) with known molecular mass (6.5 kDa) was purified from the crude Moringa oleifera (MO) seed extracts using nanoparticles prepared from both methods. The obtained MOCP exhibits comparable coagulation activity with alum in terms of water turbidity removal, implying alternative replacement to chemical coagulants. This technique can be easily applied where natural materials are available locally.

Studies on the interaction between MOCP and surface modified nanoparticles were essential to understand the binding mechanism for the development of a protein-functionalized nanoparticle. Based on in silico investigation, the overall molecular docking studies reveal the interactions between protein-ligand complexes by electrostatic, van der Waals and hydrogen-bonding; which imply, that there are at least two binding sites is i.e. one located at the core binding site (TEOS and APTES ligand) while the other located at the side chain residues (TSC and Si60-OH).

This work underscores advancement in the development and use of MOCP-MNPs for potential water treatment. About 70% turbidity removal was achieved gravimetrically using MOCP-MNPs (60 min) in high and low turbid waters, whereas alum requires 180 min to reduce the turbidity especially in low turbid waters. The turbidity removal efficiency was enhanced by the use of MOCP-MNPs under the influence of an external magnetic field. More than 95% turbidity removal was achieved within 12 min in high and low turbid waters when MOCP-MNPs were used. The combination of natural coagulant protein and magnetic nanoparticles as well as the use of applied magnetic field enhanced the performance coagulating/flocculating properties in the water samples.

These results suggest a successful development of MOCP-MNPs as demonstrated in the regeneration study. The data shown in this work represent novel potential water treatment strategies that could be cost-effective, simple, robust and environmentally friendly whilst utilizing biocompatible materials. 

Place, publisher, year, edition, pages
Stockholm: KTH Royal Institute of Technology, 2012. , x, 71 p.
Series
TRITA-BIO-Report, ISSN 1654-2312 ; 2012:8
National Category
Water Treatment Nano Technology
Identifiers
URN: urn:nbn:se:kth:diva-94025ISBN: 978-91-7501-311-4 (print)OAI: oai:DiVA.org:kth-94025DiVA: diva2:525687
Public defence
2012-05-25, Conference hall D3, Lindstedtsvägen 5, KTH, Stockholm, 10:00 (English)
Opponent
Supervisors
Note

QC 20120509

Available from: 2012-05-09 Created: 2012-05-05 Last updated: 2014-01-15Bibliographically approved
List of papers
1. Characterization of Superparamagnetic Iron Oxide Nanoparticles and Its Application in Protein Purification
Open this publication in new window or tab >>Characterization of Superparamagnetic Iron Oxide Nanoparticles and Its Application in Protein Purification
Show others...
2011 (English)In: Journal of Nanoscience and Nanotechnology, ISSN 1533-4880, E-ISSN 1533-4899, Vol. 11, no 11, 10201-10206 p.Article in journal (Refereed) Published
Abstract [en]

The application of surface modified magnetic adsorbent particles in combination with magnetic separation techniques has received considerable awareness in recent years. There is a particular need in protein purification and analysis for specific, functional and generic methods of protein binding on solid supports. Nanoscale superparamagnetic iron oxide particles have been used to purify a natural coagulant protein extracted from Moringa oleiferaseeds. Spectrophotometric analysis of the coagulant protein was performed using synthetic clay solution as substrate. Protein binding with carboxyl and silica surface modified superparamagnetic iron oxide nanoparticles (SPION) were compared with the known carboxyl methyl cellulose (CMC) beads of ∼1 m. SPION modified with carboxyl surface showed higher binding capacity towards the coagulant protein compared to the CMC beads. The high surface area to volume ratio of the carboxyl-coated SPION resulted in high binding capacity and rapid adsorption kinetics of the crude protein extract. The purification and molecular weight of coagulant protein is analyzed by SDS-PAGE. This approach utilizes the most efficient, feasible and economical method of coagulant protein purification and it can also be applicable to other proteins that possess similar properties.

Place, publisher, year, edition, pages
American Scientific Publishers, 2011
Keyword
Coagulation Activity, Nanoscale, Immobilization, Surface Effect, Magnetic Adsorbent
National Category
Nano Technology
Identifiers
urn:nbn:se:kth:diva-59580 (URN)10.1166/jnn.2011.5007 (DOI)000298765800152 ()2-s2.0-84857174054 (Scopus ID)
Note
QC 20120119Available from: 2012-01-19 Created: 2012-01-11 Last updated: 2017-12-08Bibliographically approved
2. Application of magnetic iron oxide nanoparticles prepared from microemulsions for protein purification
Open this publication in new window or tab >>Application of magnetic iron oxide nanoparticles prepared from microemulsions for protein purification
Show others...
2011 (English)In: Journal of chemical technology and biotechnology (1986), ISSN 0268-2575, E-ISSN 1097-4660, Vol. 86, no 11, 1386-1393 p.Article in journal (Refereed) Published
Abstract [en]

BACKGROUND: Magnetic nanoparticles are of immense interest for their applications in biotechnology. This paper reports the synthesis of magnetic iron oxide nanoparticles from two different water-in-oil microemulsion systems (ME-MIONs), their characterization and also their use in purification of coagulant protein. RESULTS: ME-MIONs have demonstrated to be an efficient binder in the purification of Moringa oleifera protein when compared with the superparamagnetic iron oxide nanoparticles prepared from coprecipitation in aqueous media. The size and morphology of the ME-MIONs were studied by transmission electron microscopy (TEM) while the structural characteristics were studied by X-ray diffraction (XRD). The microemulsion magnetic iron oxide nanoparticles (ME 1-MION and ME 2-MION) obtained have a size range 7-10 nm. The protein and ME-MIONs interaction was investigated by Fourier transform infrared spectroscopy (FT-IR); the presence of three peaks at 2970, 2910 and 2870 cm(-1) respectively, confirms the binding of the protein. The purification and molecular weight of the coagulant protein was 6.5 kDa as analyzed by SDS-PAGE. CONCLUSION: The ME-MIONs have the advantage of being easily tailored in size, are highly efficient as well as magnetic, cost effective and versatile; they are, thus, very suitable for use in a novel purification technique for protein or biomolecules that possess similar characteristics to the Moringa oleifera coagulant protein.

Place, publisher, year, edition, pages
John Wiley & Sons, 2011
Keyword
microemulsion, magnetic nanoparticles, iron oxide, protein purification, magnetic separation, Moringa oleifera
National Category
Nano Technology
Identifiers
urn:nbn:se:kth:diva-49406 (URN)10.1002/jctb.2704 (DOI)000297026100006 ()2-s2.0-80054095563 (Scopus ID)
Note
QC 20111208Available from: 2012-01-19 Created: 2011-11-27 Last updated: 2017-12-08Bibliographically approved
3. Comparison and Functionalization Study of Microemulsion-Prepared Magnetic Iron Oxide Nanoparticles
Open this publication in new window or tab >>Comparison and Functionalization Study of Microemulsion-Prepared Magnetic Iron Oxide Nanoparticles
Show others...
2012 (English)In: Langmuir, ISSN 0743-7463, E-ISSN 1520-5827, Vol. 28, no 22, 8479-8485 p.Article in journal (Refereed) Published
Abstract [en]

Magnetic iron oxide nanoparticles (MION) for protein binding and separation were obtained from water-in-oil (w/o) and oil-in-water (o/w) microemulsions. Characterization of the prepared nanoparticles have been performed by TEM, XRD, SQUID magnetometry, and BET. Microemulsion-prepared magnetic iron oxide nanoparticles (ME-MION) with sizes ranging from 2 to 10 rim were obtained. Study on the magnetic properties at 300 K shows a large increase of the magnetization similar to 35 emu/g for w/o-ME-MION with superparamagnetic behavior and nanoscale dimensions in comparison with o/w-ME-MION (10 emu/g) due to larger particle size and anisotropic property. Moringa oleifera coagulation protein (MOCP) bound w/o- and o/w-ME-MION showed an enhanced performance in terms of coagulation activity. A significant interaction between the magnetic nanoparticles and the protein can be described by changes in fluorescence emission spectra. Adsorbed protein from MOCP is still retaining its functionality even after binding to the nanoparticles, thus implying the extension of this technique for various applications.

Keyword
Anisotropic property, Coagulation proteins, Fluorescence emission spectra, Functionalizations, Larger particle sizes, Magnetic iron oxide nanoparticles, Magnetic nanoparticles, Moringa oleifera, Nanoscale dimensions, Oil-in-water, Protein binding, SQUID magnetometry, Superparamagnetic behavior, Water-in-oil, XRD, Biochemistry, Coagulation, Emission spectroscopy, Magnetic properties, Metal nanoparticles, Proteins, Superparamagnetism
National Category
Nano Technology
Identifiers
urn:nbn:se:kth:diva-94164 (URN)10.1021/la300599q (DOI)000304783300024 ()2-s2.0-84861871386 (Scopus ID)
Funder
Formas
Note

QC 20120703. Updated from in press to published.

Available from: 2012-05-09 Created: 2012-05-09 Last updated: 2017-12-07Bibliographically approved
4. Protein-functionalized magnetic iron oxide nanoparticles: time efficient potential-water treatment
Open this publication in new window or tab >>Protein-functionalized magnetic iron oxide nanoparticles: time efficient potential-water treatment
2012 (English)In: Journal of nanoparticle research, ISSN 1388-0764, E-ISSN 1572-896X, Vol. 14, no 10, 1194- p.Article in journal (Refereed) Published
Abstract [en]

Recent advances in nanoscience suggest that the existing issues involving water quality could be resolved or greatly improved using nanomaterials, especially magnetic iron oxide nanoparticles. Magnetic nanoparticles have been synthesized for the development and use, in association with natural coagulant protein for water treatment. The nanoparticles size, morphology, structure, and magnetic properties were characterized by transmission electron microscope, X-ray diffraction, and superconducting quantum interference device magnetometry. Purified Moringa oleifera protein was attached onto microemulsions-prepared magnetic iron oxide nanoparticles (ME-MION) to form stable protein-functionalized magnetic nanoparticles (PMO+ME-MION). The turbidity removal efficiency in both synthetic and surface water samples were investigated and compared with the commonly used synthetic coagulant (alum) as well as PMO. More than 90 % turbidity could be removed from the surface waters within 12 min by magnetic separation of PMO? ME-MION; whereas gravimetrically, 70 % removal in high and low turbid waters can be achieved within 60 min. In contrast, alum requires 180 min to reduce the turbidity of low turbid water sample. These data support the advantage of separation with external magnetic field (magnetophoresis) over gravitational force. Time kinetics studies show a significant enhancement in ME-MION efficiency after binding with PMO implying the availability of large surface of the ME-MION. The coagulated particles (impurities) can be removed from PMO+ME-MIONby washing with mild detergent or cleaning solution. To our knowledge, this is the first report on surface water turbidity removal using protein-functionalized magnetic nanoparticle.

Keyword
Magnetic separation, Microemulsions, Magnetophoresis, Purified Moringa oleifera, Coagulant protein, Surface water
National Category
Water Treatment
Identifiers
urn:nbn:se:kth:diva-94165 (URN)10.1007/s11051-012-1194-9 (DOI)000309341200057 ()2-s2.0-84866497631 (Scopus ID)
Funder
Formas
Note

QC 20121105. Updated from submitted to published.

Available from: 2012-05-09 Created: 2012-05-09 Last updated: 2017-12-07Bibliographically approved
5. In silico modeling and experimental evidence of coagulant protein interaction with precursors for nanoparticle functionalization
Open this publication in new window or tab >>In silico modeling and experimental evidence of coagulant protein interaction with precursors for nanoparticle functionalization
Show others...
2013 (English)In: Journal of Biomolecular Structure and Dynamics, ISSN 0739-1102, E-ISSN 1538-0254, Vol. 31, no 10, 1182-1190 p.Article in journal (Refereed) Published
Abstract [en]

The design of novel protein-nanoparticle hybrid systems has applications in many fields of science ranging from biomedicine, catalysis, water treatment, etc. The main barrier in devising such tool is lack of adequate information or poor understanding of protein-ligand chemistry. Here, we establish a new strategy based on computational modeling for protein and precursor linkers that can decorate the nanoparticles. Moringa oleifera (MO2.1) seed protein that has coagulation and antimicrobial properties was used. Superparamagnetic nanoparticles (SPION) with precursor ligands were used for the protein-ligand interaction studies. The molecular docking studies reveal that there are two binding sites, one is located at the core binding site; tetraethoxysilane (TEOS) or 3-aminopropyl trimethoxysilane (APTES) binds to this site while the other one is located at the side chain residues where trisodium citrate (TSC) or Si-60 binds to this site. The protein-ligand distance profile analysis explains the differences in functional activity of the decorated SPION. Experimentally, TSC-coated nanoparticles showed higher coagulation activity as compared to TEOS- and APTES-coated SPION. To our knowledge, this is the first report on in vitro experimental data, which endorses the computational modeling studies as a powerful tool to design novel precursors for functionalization of nanomaterials; and develop interface hybrid systems for various applications.

Keyword
molecular docking, magnetic nanoparticle, Moringa oleifera, surface coating, coagulation activity, binding free energy
National Category
Nano Technology
Identifiers
urn:nbn:se:kth:diva-94166 (URN)10.1080/07391102.2012.726534 (DOI)000324002100014 ()2-s2.0-84884565897 (Scopus ID)
Funder
Formas
Note

QC 20131004. Updated from submitted to published.

Available from: 2012-05-09 Created: 2012-05-09 Last updated: 2017-12-07Bibliographically approved
6. Dimerization of flocculent protein from Moringa oleifera: experimental evidence and in silico interpretation
Open this publication in new window or tab >>Dimerization of flocculent protein from Moringa oleifera: experimental evidence and in silico interpretation
Show others...
(English)Article in journal (Refereed) Epub ahead of print
Abstract [en]

Many proteins exist in dimeric and other oligomeric forms to gain stability and functional advantages. In this study, the dimerization property of a coagulant protein (MO2.1) from Moringa oleifera seeds was addressed through laboratory experiments, protein-protein docking studies and binding free energy calculations. The structure of MO2.1 was predicted by homology modelling, while binding free energy and residues-distance profile analyses provided insight into the energetics and structural factors for dimer formation. Since the coagulation activities of the monomeric and dimeric forms of MO2.1 were comparable, it was concluded that oligomerization does not affect the biological activity of the protein.

National Category
Nano Technology
Identifiers
urn:nbn:se:kth:diva-94179 (URN)23662981 (PubMedID)
Note

QP 2013

Available from: 2012-05-09 Created: 2012-05-09 Last updated: 2013-05-31Bibliographically approved
7. Effect of Magnetic Iron Oxide Nanoparticles for Surface Water Treatment: Trace Minerals and Microbes
Open this publication in new window or tab >>Effect of Magnetic Iron Oxide Nanoparticles for Surface Water Treatment: Trace Minerals and Microbes
Show others...
(English)Manuscript (preprint) (Other academic)
National Category
Water Treatment
Identifiers
urn:nbn:se:kth:diva-94172 (URN)
Note

QS 2012

Available from: 2012-05-09 Created: 2012-05-09 Last updated: 2013-09-12Bibliographically approved

Open Access in DiVA

fulltext(3061 kB)2000 downloads
File information
File name FULLTEXT01.pdfFile size 3061 kBChecksum SHA-512
303568f65d127c8f7dfde1686dbe3ee6a5e1e9935498350cde2f6ba0cb340f5befc028f61a7f465f7c816c22220bb29ebab049b4ccbbe4bd7cc7a41394229693
Type fulltextMimetype application/pdf

Search in DiVA

By author/editor
Okoli, Chuka
By organisation
Chemical TechnologyIndustrial Biotechnology
Water TreatmentNano Technology

Search outside of DiVA

GoogleGoogle Scholar
Total: 2000 downloads
The number of downloads is the sum of all downloads of full texts. It may include eg previous versions that are now no longer available

isbn
urn-nbn

Altmetric score

isbn
urn-nbn
Total: 1092 hits
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • harvard1
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf