Enhancement of biodegradation potential of catechol 1,2-dioxygenase through its immobilization in calcium alginate gel

Background In biodegradation processes free enzymes often undergo deactivation. Thus, it is very important to obtain highly stable enzymes by different methods. Immobilization allows for successful stabilization of many multimeric enzymes by increasing the rigidity of the enzyme structure. This stud...

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Autores principales:	Guzik,Urszula, Hupert-Kocurek,Katarzyna, Marchlewicz,Ariel, Wojcieszynska,Danuta
Lenguaje:	English
Publicado:	Pontificia Universidad Católica de Valparaíso 2014
Materias:	Arenes Entrapment Intradiol dioxygenase Stenotrophomonas
Acceso en línea:	http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582014000200005
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spelling	oai:scielo:S0717-345820140002000052014-09-02Enhancement of biodegradation potential of catechol 1,2-dioxygenase through its immobilization in calcium alginate gelGuzik,UrszulaHupert-Kocurek,KatarzynaMarchlewicz,ArielWojcieszynska,Danuta Arenes Entrapment Intradiol dioxygenase Stenotrophomonas Background In biodegradation processes free enzymes often undergo deactivation. Thus, it is very important to obtain highly stable enzymes by different methods. Immobilization allows for successful stabilization of many multimeric enzymes by increasing the rigidity of the enzyme structure. This study aimed to evaluate some environmental factors that affect catechol 1,2-dioxygenase from Stenotrophomonas maltophilia KB2 immobilized in alginate hydrogel. The goal of the present work was to improve the functional stability of the enzyme by increasing its structural rigidity. Results Immobilization yield and expressed activity were 100% and 56%, respectively. Under the same storage conditions, the activity of the immobilized enzyme was still observed on the 28th d of incubation at 4°C, whereas the free enzyme lost its activity after 14 d. The immobilized enzyme required approximately 10°C lower temperature for its optimal activity than the free enzyme. Immobilization shifted the optimal pH from 8 for the soluble enzyme to 7 for the immobilized enzyme. The immobilized catechol 1,2-dioxygenase showed activity against 3-methylcatechol, 4-methylcatechol, 3-chlorocatechol, 4-chlorocatechol, and 3,5-dichlorocatechol. The immobilization of the enzyme promoted its stabilization against any distorting agents: aliphatic alcohols, phenols, and chelators. Conclusions The entrapment of the catechol 1,2-dioxygenase from S. maltophilia KB2 has been shown to be an effective method for improving the functional properties of the enzyme. Increased resistance to inactivation by higher substrate concentration and other factors affecting enzyme activity as well as broadened substrate specificity compared to the soluble enzyme, makes the immobilized catechol 1,2-dioxygenase suitable for the bioremediation and detoxification of xenobiotic-contaminated environments.info:eu-repo/semantics/openAccessPontificia Universidad Católica de ValparaísoElectronic Journal of Biotechnology v.17 n.2 20142014-03-01text/htmlhttp://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582014000200005en10.1016/j.ejbt.2014.02.001
institution	Scielo Chile
collection	Scielo Chile
language	English
topic	Arenes Entrapment Intradiol dioxygenase Stenotrophomonas
spellingShingle	Arenes Entrapment Intradiol dioxygenase Stenotrophomonas Guzik,Urszula Hupert-Kocurek,Katarzyna Marchlewicz,Ariel Wojcieszynska,Danuta Enhancement of biodegradation potential of catechol 1,2-dioxygenase through its immobilization in calcium alginate gel
description	Background In biodegradation processes free enzymes often undergo deactivation. Thus, it is very important to obtain highly stable enzymes by different methods. Immobilization allows for successful stabilization of many multimeric enzymes by increasing the rigidity of the enzyme structure. This study aimed to evaluate some environmental factors that affect catechol 1,2-dioxygenase from Stenotrophomonas maltophilia KB2 immobilized in alginate hydrogel. The goal of the present work was to improve the functional stability of the enzyme by increasing its structural rigidity. Results Immobilization yield and expressed activity were 100% and 56%, respectively. Under the same storage conditions, the activity of the immobilized enzyme was still observed on the 28th d of incubation at 4°C, whereas the free enzyme lost its activity after 14 d. The immobilized enzyme required approximately 10°C lower temperature for its optimal activity than the free enzyme. Immobilization shifted the optimal pH from 8 for the soluble enzyme to 7 for the immobilized enzyme. The immobilized catechol 1,2-dioxygenase showed activity against 3-methylcatechol, 4-methylcatechol, 3-chlorocatechol, 4-chlorocatechol, and 3,5-dichlorocatechol. The immobilization of the enzyme promoted its stabilization against any distorting agents: aliphatic alcohols, phenols, and chelators. Conclusions The entrapment of the catechol 1,2-dioxygenase from S. maltophilia KB2 has been shown to be an effective method for improving the functional properties of the enzyme. Increased resistance to inactivation by higher substrate concentration and other factors affecting enzyme activity as well as broadened substrate specificity compared to the soluble enzyme, makes the immobilized catechol 1,2-dioxygenase suitable for the bioremediation and detoxification of xenobiotic-contaminated environments.
author	Guzik,Urszula Hupert-Kocurek,Katarzyna Marchlewicz,Ariel Wojcieszynska,Danuta
author_facet	Guzik,Urszula Hupert-Kocurek,Katarzyna Marchlewicz,Ariel Wojcieszynska,Danuta
author_sort	Guzik,Urszula
title	Enhancement of biodegradation potential of catechol 1,2-dioxygenase through its immobilization in calcium alginate gel
title_short	Enhancement of biodegradation potential of catechol 1,2-dioxygenase through its immobilization in calcium alginate gel
title_full	Enhancement of biodegradation potential of catechol 1,2-dioxygenase through its immobilization in calcium alginate gel
title_fullStr	Enhancement of biodegradation potential of catechol 1,2-dioxygenase through its immobilization in calcium alginate gel
title_full_unstemmed	Enhancement of biodegradation potential of catechol 1,2-dioxygenase through its immobilization in calcium alginate gel
title_sort	enhancement of biodegradation potential of catechol 1,2-dioxygenase through its immobilization in calcium alginate gel
publisher	Pontificia Universidad Católica de Valparaíso
publishDate	2014
url	http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582014000200005
work_keys_str_mv	AT guzikurszula enhancementofbiodegradationpotentialofcatechol12dioxygenasethroughitsimmobilizationincalciumalginategel AT hupertkocurekkatarzyna enhancementofbiodegradationpotentialofcatechol12dioxygenasethroughitsimmobilizationincalciumalginategel AT marchlewiczariel enhancementofbiodegradationpotentialofcatechol12dioxygenasethroughitsimmobilizationincalciumalginategel AT wojcieszynskadanuta enhancementofbiodegradationpotentialofcatechol12dioxygenasethroughitsimmobilizationincalciumalginategel
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Enhancement of biodegradation potential of catechol 1,2-dioxygenase through its immobilization in calcium alginate gel

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