Superficially bound acetylcholinesterase based on a chitosan matrix for neurotoxic compound assay by a photographic technique

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216275%3A25310%2F18%3A39910751" target="_blank" >RIV/00216275:25310/18:39910751 - isvavai.cz</a>

Výsledek na webu

<a href="http://dx.doi.org/10.1080/00032719.2017.1381846" target="_blank" >http://dx.doi.org/10.1080/00032719.2017.1381846</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1080/00032719.2017.1381846" target="_blank" >10.1080/00032719.2017.1381846</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Superficially bound acetylcholinesterase based on a chitosan matrix for neurotoxic compound assay by a photographic technique

Popis výsledku v původním jazyce

Smartphones scored big success in the last decade and they broke into analytical chemistry as an easy detection system with comparable parameters to standard laboratory equipment. This work focuses on attachment of enzyme acetylcholinesterase (AChE) onto previously activated chitosan. Here, AChE splits alternative substrate indoxyl acetate. Conversion of substrate is blocking or slowing down by inhibitors from which galantamine and tacrine were tested here as model inhibitors with detection limits, 1.1 µM and 0.18 µM, respectively. Measurement procedure was carried out on a 3D three-dimensional printed holder and red-green-blue (RGB) channels served for digital photography evaluation. The method was validated to standard Ellman´s spectrophotometric assay. Long-term stability of immobilized enzyme as well as sensitivity to organic solvents were also tested.

Název v anglickém jazyce

Superficially bound acetylcholinesterase based on a chitosan matrix for neurotoxic compound assay by a photographic technique

Popis výsledku anglicky

Smartphones scored big success in the last decade and they broke into analytical chemistry as an easy detection system with comparable parameters to standard laboratory equipment. This work focuses on attachment of enzyme acetylcholinesterase (AChE) onto previously activated chitosan. Here, AChE splits alternative substrate indoxyl acetate. Conversion of substrate is blocking or slowing down by inhibitors from which galantamine and tacrine were tested here as model inhibitors with detection limits, 1.1 µM and 0.18 µM, respectively. Measurement procedure was carried out on a 3D three-dimensional printed holder and red-green-blue (RGB) channels served for digital photography evaluation. The method was validated to standard Ellman´s spectrophotometric assay. Long-term stability of immobilized enzyme as well as sensitivity to organic solvents were also tested.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10608 - Biochemistry and molecular biology

Projekt

—

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2018

Kód důvěrnosti údajů

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

Název periodika

Analytical Letters

ISSN

0003-2719

e-ISSN

—

Svazek periodika

51

Číslo periodika v rámci svazku

10

Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

11

Strana od-do

1622-1632

Kód UT WoS článku

000429348300013

EID výsledku v databázi Scopus

2-s2.0-85044085562