Synthesis and characterization of enzyme–magnetic nanoparticle complexes: effect of size on activity and recovery

Park, Hee Joon; McConnell, Joshua T.; Boddohi, Soheil; Kipper, Matt J.; Johnson, Patrick A.

doi:10.1016/j.colsurfb.2010.11.006

Cited by 72 publications

(39 citation statements)

References 26 publications

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“…This result showed that the thermal stability of immobilized GOx was enhanced after immobilization (Zhou et al 2012a, b). As a comparison, GOx immobilized onto a 3-(aminopropyl)triethoxysilane (APTES)-coated Fe 3 O 4 nanocarrier which retained less than 50% of the native GOx activity (Park et al 2011). Thus the immobilization process in the present study is promising for enzyme immobilization.…”

Section: Immobilization Of Gox By Zif-8@cellu@fe 3 O 4 Nanocompositementioning

confidence: 99%

Magnetic ZIF-8/cellulose/Fe3O4 nanocomposite: preparation, characterization, and enzyme immobilization

Cao

Lai

et al. 2017

Bioresour. Bioprocess.

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Background:The ZIF-8-coated magnetic regenerated cellulose-coated nanoparticles (ZIF-8@cellu@Fe 3 O 4 ) were successfully prepared and characterized. The result showed that ZIF-8 was successfully composited on to the surface of the cellulose-coated Fe 3 O 4 nanoparticles by co-precipitation method. Moreover, the glucose oxidase (GOx, from Aspergillus niger) was efficiently immobilized by the ZIF-8@Cellu@Fe 3 O 4 nanocarriers with enhanced catalytic activities. The enzyme loading was 94.26 mg/g and the enzyme activity recovery was more than 124.2%. This efficiently immobilized enzyme exhibits promising applications in biotechnology, diagnosis, biosensing, and biomedical devices. Conclusions:A new core-shell magnetic ZIF-8/cellulose nanocomposite (ZIF-8@Cellu@Fe 3 O 4 ) was fabricated and structurally characterized. Glucose oxidase (GOx) was successfully immobilized by the biocompatible ZIF-8@Cellu@

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Section: Immobilization Of Gox By Zif-8@cellu@fe 3 O 4 Nanocompositementioning

confidence: 99%

Magnetic ZIF-8/cellulose/Fe3O4 nanocomposite: preparation, characterization, and enzyme immobilization

Cao

Lai

et al. 2017

Bioresour. Bioprocess.

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“…[1][2][3] From the past few decades, nanosized iron oxide particles have attracted great attention in the fields including, but not limited to, immunoassay, 4,5 biosensor, 6,7 bioseparation, 8,9 targeted drug delivery, 10,11 and environmental analysis 12,13 and protein immobilization. [14][15][16][17][18][19][20][21] However, the bare Fe 3 O 4 NPs have high reactivity and easily undergo degradation upon direct exposing to certain environment, leading to poor stability and dispersity.…”

Section: Introductionmentioning

confidence: 99%

Synthesis and Characterization of Magnetic Nanoparticles and Its Application in Lipase Immobilization

Xu¹,

Ju²,

Sheng³

et al. 2013

Bulletin of the Korean Chemical Society

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We demonstrate herein the synthesis and modification of magnetic nanoparticles and its use in the immobilization of the lipase. Magnetic Fe 3 O 4 nanoparticles (MNPs) were prepared by simple co-precipitation method in aqueous medium and then subsequently modified with tetraethyl orthosilicate (TEOS) and 3-aminopropyl triethylenesilane (APTES). Silanization magnetic nanoparticles (SMNP) and amino magnetic nanomicrosphere (AMNP) were synthesized successfully. The morphology, structure, magnetic property and chemical composition of the synthetic MNP and its derivatives were characterized using transmission electron microscopy (TEM), Fourier transform infrared spectroscopy (FT-IR) analysis, X-ray diffraction, superconducting quantum interference device (SQUID) and thermogravimetric analyses (TGA). All of these three nanoparticles exhibited good crystallization performance, apparent superparamagnetism, and the saturation magnetization of MNP, SMNP, AMNP were 47.9 emu/g, 33.0 emu/g and 19.5 emu/g, respectively. The amino content was 5.66%. The AMNP was used to immobilize lipase, and the maximum adsorption capacity of the protein was 26.3 mg/g. The maximum maintained activity (88 percent) was achieved while the amount of immobilized lipase was 23.7 mg g −1. Immobilization of enzyme on the magnetic nanoparticles can facilitate the isolation of reaction products from reaction mixture and thus lowers the cost of enzyme application.

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“…266 A similar phenomenon is noted for GOx immobilized on different Fe 3 O 4 NPs (5, 26, and 51 nm) with APTES and GLD. 267 The immobilized enzyme retains only 15−23% of the free enzyme activity. Smaller NPs exhibit greater activity loss over repeated runs due to a poor recovery of the enzyme.…”

mentioning

confidence: 99%

Immobilization of Antibodies and Enzymes on 3-Aminopropyltriethoxysilane-Functionalized Bioanalytical Platforms for Biosensors and Diagnostics

et al. 2014

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/npsi/ctrl?lang=en http://nparc.cisti-icist.nrc-cnrc.gc.ca/npsi/ctrl?lang=fr READ THESE TERMS AND CONDITIONS CAREFULLY BEFORE USING THIS WEBSITE.http://nparc.cisti-icist.nrc-cnrc.gc.ca/npsi/jsp/nparc_cp.jsp?lang=en Vous avez des questions? Nous pouvons vous aider. Pour communiquer directement avec un auteur, consultez la première page de la revue dans laquelle son article a été publié afin de trouver ses coordonnées. Si vous n'arrivez pas à les repérer, communiquez avec nous à PublicationsArchive-ArchivesPublications@nrc-cnrc.gc.ca.

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Synthesis and characterization of enzyme–magnetic nanoparticle complexes: effect of size on activity and recovery

Cited by 72 publications

References 26 publications

Magnetic ZIF-8/cellulose/Fe3O4 nanocomposite: preparation, characterization, and enzyme immobilization

Magnetic ZIF-8/cellulose/Fe3O4 nanocomposite: preparation, characterization, and enzyme immobilization

Synthesis and Characterization of Magnetic Nanoparticles and Its Application in Lipase Immobilization

Immobilization of Antibodies and Enzymes on 3-Aminopropyltriethoxysilane-Functionalized Bioanalytical Platforms for Biosensors and Diagnostics

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