Microscopic Monitoring Provides Information on Structure and Properties During Biocatalyst Immobilisation.
Identifikátory výsledku
Kód výsledku v IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F14%3A00074208" target="_blank" >RIV/00216224:14310/14:00074208 - isvavai.cz</a>
Nalezeny alternativní kódy
RIV/00159816:_____/14:00061048
Výsledek na webu
<a href="http://dx.doi.org/10.1002/biot.201300049" target="_blank" >http://dx.doi.org/10.1002/biot.201300049</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1002/biot.201300049" target="_blank" >10.1002/biot.201300049</a>
Alternativní jazyky
Jazyk výsledku
angličtina
Název v původním jazyce
Microscopic Monitoring Provides Information on Structure and Properties During Biocatalyst Immobilisation.
Popis výsledku v původním jazyce
Enzymes have a wide range of applications in different industries owing to their high specificity and efficiency. Immobilisation is often used to improve biocatalyst properties, operational stability and reusability. However, changes in the structure ofbiocatalysts during immobilisation and under process conditions are still largely uncertain. Here, three microscopy techniques ? bright-field, confocal and electron microscopy ? were applied to determine the distribution and structure of an immobilised biocatalyst. Free enzyme (haloalkane dehalogenase), cross-linked enzyme aggregates (CLEAs) and CLEAs entrapped in polyvinyl alcohol lenses (lentikats) were used as model systems. Electron microscopy revealed that sonicated CLEAs underwent morphological changes that strongly correlated with increased catalytic activity compared to less structured, non-treated CLEAs. Confocal microscopy confirmed that loading of the biocatalyst was not the only factor affecting the catalytic activity of the
Název v anglickém jazyce
Microscopic Monitoring Provides Information on Structure and Properties During Biocatalyst Immobilisation.
Popis výsledku anglicky
Enzymes have a wide range of applications in different industries owing to their high specificity and efficiency. Immobilisation is often used to improve biocatalyst properties, operational stability and reusability. However, changes in the structure ofbiocatalysts during immobilisation and under process conditions are still largely uncertain. Here, three microscopy techniques ? bright-field, confocal and electron microscopy ? were applied to determine the distribution and structure of an immobilised biocatalyst. Free enzyme (haloalkane dehalogenase), cross-linked enzyme aggregates (CLEAs) and CLEAs entrapped in polyvinyl alcohol lenses (lentikats) were used as model systems. Electron microscopy revealed that sonicated CLEAs underwent morphological changes that strongly correlated with increased catalytic activity compared to less structured, non-treated CLEAs. Confocal microscopy confirmed that loading of the biocatalyst was not the only factor affecting the catalytic activity of the
Klasifikace
Druh
J<sub>x</sub> - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)
CEP obor
CE - Biochemie
OECD FORD obor
—
Návaznosti výsledku
Projekt
Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.
Návaznosti
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Ostatní
Rok uplatnění
2014
Kód důvěrnosti údajů
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Údaje specifické pro druh výsledku
Název periodika
Biotechnology Journal
ISSN
1860-6768
e-ISSN
—
Svazek periodika
9
Číslo periodika v rámci svazku
6
Stát vydavatele periodika
DE - Spolková republika Německo
Počet stran výsledku
9
Strana od-do
852-860
Kód UT WoS článku
000337700000015
EID výsledku v databázi Scopus
—