Offline and online capillary electrophoresis enzyme assays of beta-N-acetylhexosaminidase
Identifikátory výsledku
Kód výsledku v IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F13%3A10133390" target="_blank" >RIV/00216208:11310/13:10133390 - isvavai.cz</a>
Výsledek na webu
<a href="http://dx.doi.org/10.1007/s00216-012-6607-1" target="_blank" >http://dx.doi.org/10.1007/s00216-012-6607-1</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1007/s00216-012-6607-1" target="_blank" >10.1007/s00216-012-6607-1</a>
Alternativní jazyky
Jazyk výsledku
angličtina
Název v původním jazyce
Offline and online capillary electrophoresis enzyme assays of beta-N-acetylhexosaminidase
Popis výsledku v původním jazyce
Enzyme assays of beta-N-acetylhexosaminidase from Aspergillus oryzae using capillary electrophoresis in the offline and online setup have been developed. The pH value and concentration of the borate-based background electrolyte were optimized in order toachieve baseline separation of N,N',N"-triacetylchitotriose, N,N'-diacetylchitobiose, and N-acetyl-D-glucosamine. The optimized method using 25 mM tetraborate buffer, pH 10.0, was evaluated in terms of repeatability, limits of detection, quantification,and linearity. The method was successfully applied to the offline enzyme assay of beta-N-acetylhexosaminidase, which was demonstrated by monitoring the hydrolysis of N,N',N"- triacetylchitotriose. The presented method was also utilized to study the pH dependence of enzyme activity. An online assay with N,N'-diacetylchitobiose as a substrate was developed using the Transverse Diffusion of Laminar Flow Profiles model to optimize the injection sequence and incapillary mixing of substrate a
Název v anglickém jazyce
Offline and online capillary electrophoresis enzyme assays of beta-N-acetylhexosaminidase
Popis výsledku anglicky
Enzyme assays of beta-N-acetylhexosaminidase from Aspergillus oryzae using capillary electrophoresis in the offline and online setup have been developed. The pH value and concentration of the borate-based background electrolyte were optimized in order toachieve baseline separation of N,N',N"-triacetylchitotriose, N,N'-diacetylchitobiose, and N-acetyl-D-glucosamine. The optimized method using 25 mM tetraborate buffer, pH 10.0, was evaluated in terms of repeatability, limits of detection, quantification,and linearity. The method was successfully applied to the offline enzyme assay of beta-N-acetylhexosaminidase, which was demonstrated by monitoring the hydrolysis of N,N',N"- triacetylchitotriose. The presented method was also utilized to study the pH dependence of enzyme activity. An online assay with N,N'-diacetylchitobiose as a substrate was developed using the Transverse Diffusion of Laminar Flow Profiles model to optimize the injection sequence and incapillary mixing of substrate a
Klasifikace
Druh
J<sub>x</sub> - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)
CEP obor
CB - Analytická chemie, separace
OECD FORD obor
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Návaznosti výsledku
Projekt
<a href="/cs/project/GBP206%2F12%2FG151" target="_blank" >GBP206/12/G151: Centrum nových přístupů k bioanalýze a molekulární diagnostice</a><br>
Návaznosti
Z - Vyzkumny zamer (s odkazem do CEZ)<br>S - Specificky vyzkum na vysokych skolach<br>I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Ostatní
Rok uplatnění
2013
Kód důvěrnosti údajů
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Údaje specifické pro druh výsledku
Název periodika
Analytical and Bioanalytical Chemistry
ISSN
1618-2642
e-ISSN
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Svazek periodika
405
Číslo periodika v rámci svazku
8
Stát vydavatele periodika
DE - Spolková republika Německo
Počet stran výsledku
10
Strana od-do
2425-2434
Kód UT WoS článku
000315464800003
EID výsledku v databázi Scopus
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