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

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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 http://hdl.handle.net/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


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