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

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15310%2F19%3A73595180" target="_blank" >RIV/61989592:15310/19:73595180 - isvavai.cz</a>

Výsledek na webu

<a href="https://link.springer.com/article/10.1007/s00726-019-02704-7" target="_blank" >https://link.springer.com/article/10.1007/s00726-019-02704-7</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1007/s00726-019-02704-7" target="_blank" >10.1007/s00726-019-02704-7</a>

Jazyk výsledku

angličtina

Název v původním jazyce

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

Popis výsledku v původním jazyce

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 6months. 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.

Název v anglickém jazyce

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

Popis výsledku anglicky

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 6months. 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.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10608 - Biochemistry and molecular biology

Projekt

<a href="/cs/project/LO1204" target="_blank" >LO1204: Udržitelný rozvoj výzkumu v Centru regionu Haná</a><br>

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2019

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Amino Acids

ISSN

0939-4451

e-ISSN

—

Svazek periodika

51

Číslo periodika v rámci svazku

4

Stát vydavatele periodika

DE - Spolková republika Německo

Počet stran výsledku

12

Strana od-do

679-690

Kód UT WoS článku

000463590400011

EID výsledku v databázi Scopus

2-s2.0-85061179892