Amino Acids

, Volume 51, Issue 4, pp 679–690 | Cite as

Enzyme self-assembly on naked iron oxide nanoparticles for aminoaldehyde biosensing

  • Massimiliano Magro
  • Davide Baratella
  • Giovanni Miotto
  • Jan Frömmel
  • Marek Šebela
  • Martina Kopečná
  • Enzo Agostinelli
  • Fabio VianelloEmail author
Original Article


The preservation of enzymatic activity is a fundamental requirement for exploiting hybrid nano-bio-conjugates, and the control over protein–nanoparticle interactions, leading to stable and catalytically active hybrids, represents the key for designing new biosensing platforms. In this scenario, surface active maghemite nanoparticles (SAMNs) represent a new class of naked magnetic nanoparticles, displaying peculiar electrocatalytic features and the ability to selectively bind proteins. Recombinant aminoaldehyde dehydrogenase from tomato (SlAMADH1) was used as a model protein, and successfully immobilized by self-assembly on the surface of naked SAMNs, where its enzymatic activity resulted preserved for more than 6 months. The hybrid nanomaterial (SAMN@SlAMADH1) was characterized by UV–Vis spectroscopy, mass spectrometry, and TEM microscopy, and applied for the development of a biosensor for the determination of aminoaldehydes in alcoholic beverages. Measurements were carried out in a low volume electrochemical flow cell comprising a SAMN modified carbon paste electrode for the coulometric determination of the NADH produced during the enzymatic catalysis. The present findings, besides representing the first example of an electrochemical biosensor for aminoaldehydes in an alcoholic matrix, open the door to the use of immobilized enzymes on naked metal oxides nanomaterials for biosensing.


Metal nanoparticles Nanomaterial electrocatalysis NADH electro-oxidation Coulometric detection Aminoaldehyde dehydrogenase Aminoaldehyde biosensor 



3-Aminopropionaldehyde diethylacetal


Carbon paste


Carbon paste electrode


Cyclic voltammetry


False discovery rates


Fourier-transform infrared






Isopropyl β-d-1-thiogalactopyranoside




Liquid chromatography


Limit of detection


Mascot generic format


Mass spectrometry


Nicotinamide adenine dinucleotide


Quadrupole time of flight




Relative standard deviation


Surface active maghemite nanoparticles


(Solanum lycopersium) aminoaldehyde dehydrogenase 1


Saturated calomel electrode


Standard deviation




Transmission electron microscopy






X-ray diffraction



The present experimental work was partially funded by Italian Institutional Ministry Grants Cod. 60A06-7411 and 60A06-8055. The authors gratefully acknowledge the University of Padua (Italy), Grant PRAT 2015 (progetti di Ateneo) n. CPDA159850 and the CARIPARO Foundation for the support. The team members from the Czech Republic were supported by Grant No. LO1204 from the Ministry of Education, Youth and Sports. The authors also thank ‘La Sapienza’ University of Rome and Italian MIUR (Ministero dell’Istruzione, dell’Università e della Ricerca). Our gratitude is also due to the “International Polyamine Foundation-ONLUS” for the availability to look up in the Polyamines documentation.

Compliance with ethical standards

Conflict of interest

The authors declare that they have no conflicts of interest with the contents of this article.

Research involving human participants and/or animals

This article does not contain any studies with human participants or animals performed by any of the authors.

Supplementary material

726_2019_2704_MOESM1_ESM.docx (26 kb)
Supplementary material 1 (DOCX 26 kb)


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Copyright information

© Springer-Verlag GmbH Austria, part of Springer Nature 2019

Authors and Affiliations

  1. 1.Department of Comparative Biomedicine and Food ScienceUniversity of PaduaLegnaroItaly
  2. 2.Regional Centre of Advanced Technologies and Materials, Department of Physical Chemistry, Faculty of SciencePalacký University in OlomoucOlomoucCzech Republic
  3. 3.Department of Molecular MedicineUniversity of PaduaPaduaItaly
  4. 4.Proteomic Center of Padua University, VIMM and Padua University HospitalPaduaItaly
  5. 5.Department of Protein Biochemistry and Proteomics, Centre of the Region Haná for Biotechnological and Agricultural Research, Faculty of SciencePalacký University in OlomoucOlomoucCzech Republic
  6. 6.Department of Biochemical Sciences “A. Rossi Fanelli”University of Rome La Sapienza and CNR, Institute of Biology and Molecular PathologyRomeItaly
  7. 7.International Polyamines Foundation-ONLUSRomeItaly

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