Properties of catechol 1,2-dioxygenase from Pseudomonas putida immobilized in calcium alginate hydrogels

Kalogeris, E; Sanakis, Y; Mamma, D; Christakopoulos, P; Kekos, D; Stamatis, H

dc.contributor.author	Kalogeris, E	en
dc.contributor.author	Sanakis, Y	en
dc.contributor.author	Mamma, D	en
dc.contributor.author	Christakopoulos, P	en
dc.contributor.author	Kekos, D	en
dc.contributor.author	Stamatis, H	en
dc.date.accessioned	2014-03-01T01:24:54Z
dc.date.available	2014-03-01T01:24:54Z
dc.date.issued	2006	en
dc.identifier.issn	0141-0229	en
dc.identifier.uri	https://dspace.lib.ntua.gr/xmlui/handle/123456789/17500
dc.subject	Alginate	en
dc.subject	Catechol 1,2-dioxygenase	en
dc.subject	EPR spectroscopy	en
dc.subject	Hydrogel	en
dc.subject	Immobilization	en
dc.subject	Mass transfer	en
dc.subject	Pseudomonas putida	en
dc.subject.classification	Biotechnology & Applied Microbiology	en
dc.subject.other	Catalysts	en
dc.subject.other	Cell immobilization	en
dc.subject.other	Enzyme kinetics	en
dc.subject.other	Hydrogels	en
dc.subject.other	Mass transfer	en
dc.subject.other	Organic solvents	en
dc.subject.other	Paramagnetic resonance	en
dc.subject.other	Thermal effects	en
dc.subject.other	Alginate	en
dc.subject.other	Catechol 1,2-dioxygenase	en
dc.subject.other	EPR spectroscopy	en
dc.subject.other	Immobilization	en
dc.subject.other	Pseudomonas putida	en
dc.subject.other	Enzymes	en
dc.subject.other	calcium alginate	en
dc.subject.other	catechol	en
dc.subject.other	catechol 1,2 dioxygenase	en
dc.subject.other	organic solvent	en
dc.subject.other	article	en
dc.subject.other	bacterium isolation	en
dc.subject.other	binding affinity	en
dc.subject.other	controlled study	en
dc.subject.other	electron spin resonance	en
dc.subject.other	enzyme activity	en
dc.subject.other	enzyme analysis	en
dc.subject.other	enzyme binding	en
dc.subject.other	enzyme immobilization	en
dc.subject.other	enzyme mechanism	en
dc.subject.other	enzyme stability	en
dc.subject.other	enzyme structure	en
dc.subject.other	enzyme substrate	en
dc.subject.other	hydrogel	en
dc.subject.other	hypothesis	en
dc.subject.other	nonhuman	en
dc.subject.other	oxidation	en
dc.subject.other	Pseudomonas putida	en
dc.subject.other	structure analysis	en
dc.subject.other	Pseudomonas putida	en
dc.title	Properties of catechol 1,2-dioxygenase from Pseudomonas putida immobilized in calcium alginate hydrogels	en
heal.type	journalArticle	en
heal.identifier.primary	10.1016/j.enzmictec.2006.02.026	en
heal.identifier.secondary	http://dx.doi.org/10.1016/j.enzmictec.2006.02.026	en
heal.language	English	en
heal.publicationDate	2006	en
heal.abstract	Catechol 1,2-dioxygenase from Pseudomonas putida was isolated and immobilized in calcium alginate hydrogels. The gel matrix could effectively entrap the enzyme, with high retention of activity. Following immobilization, catechol 1,2-dioxygenase exhibited improved storage stability and activity in the presence of organic solvents, and performed better at higher incubation temperatures. In addition, the enzyme retained most of its catalytic efficiency after successive operational cycles. The hypothesis that enhancement of enzyme stability after immobilization is related to the stabilization of its multimeric structure has been investigated. Electron paramagnetic resonance (EPR) spectroscopy indicates that the environment of the non-heme iron center was not affected during the immobilization process and the ability for the substrate (catechol) binding at the metal center was retained. Catalytic constants for free and immobilized enzyme were practically equivalent. The influence of internal and external mass-transfer limitations on the initial reaction rates of dioxygenase-catalyzed oxidation reactions has been investigated. (c) 2006 Elsevier Inc. All rights reserved.	en
heal.publisher	ELSEVIER SCIENCE INC	en
heal.journalName	Enzyme and Microbial Technology	en
dc.identifier.doi	10.1016/j.enzmictec.2006.02.026	en
dc.identifier.isi	ISI:000239694500022	en
dc.identifier.volume	39	en
dc.identifier.issue	5	en
dc.identifier.spage	1113	en
dc.identifier.epage	1121	en