Properties of catechol 1,2-dioxygenase from Pseudomonas putida immobilized in calcium alginate hydrogels
| 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 | 2015-11-24T16:33:40Z | |
| dc.date.available | 2015-11-24T16:33:40Z | |
| dc.identifier.issn | 0141-0229 | - |
| dc.identifier.uri | https://olympias.lib.uoi.gr/jspui/handle/123456789/7692 | |
| dc.rights | Default Licence | - |
| dc.subject | catechol 1,2-dioxygenase | en |
| dc.subject | immobilization | en |
| dc.subject | alginate | en |
| dc.subject | hydrogel | en |
| dc.subject | epr spectroscopy | en |
| dc.subject | mass transfer | en |
| dc.subject | pseudomonas putida | en |
| dc.subject | acinetobacter-radioresistens s13 | en |
| dc.subject | multimeric enzymes | en |
| dc.subject | ampicillin synthesis | en |
| dc.subject | organic-solvents | en |
| dc.subject | meta-pathway | en |
| dc.subject | stabilization | en |
| dc.subject | stability | en |
| dc.subject | diox | en |
| dc.title | Properties of catechol 1,2-dioxygenase from Pseudomonas putida immobilized in calcium alginate hydrogels | 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.access | campus | - |
| heal.fullTextAvailability | TRUE | - |
| heal.identifier.primary | DOI 10.1016/j.enzmictec.2006.02.026 | - |
| heal.identifier.secondary | <Go to ISI>://000239694500022 | - |
| heal.identifier.secondary | http://ac.els-cdn.com/S0141022906001232/1-s2.0-S0141022906001232-main.pdf?_tid=1ca75659a27f202d59c7388f2acab842&acdnat=1335510864_a7e94fe8a2756363431557c35b2f5d0c | - |
| heal.journalName | Enzyme and Microbial Technology | en |
| heal.journalType | peer reviewed | - |
| heal.language | en | - |
| heal.publicationDate | 2006 | - |
| heal.recordProvider | Πανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών και Τεχνολογιών. Τμήμα Βιολογικών Εφαρμογών και Τεχνολογιών | el |
| heal.type | journalArticle | - |
| heal.type.el | Άρθρο Περιοδικού | el |
| heal.type.en | Journal article | en |
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