Publicação
Optimization in the immobilization of penicillin G acylase by entrapment in xerogel particles with magnetic properties
| dc.contributor.author | Bernardino, Susana | |
| dc.contributor.author | Estrela, Nídia | |
| dc.contributor.author | Ochoa-Mendes, Vanessa | |
| dc.contributor.author | Fernandes, Pedro | |
| dc.contributor.author | Fonseca, Luís P. | |
| dc.date.accessioned | 2025-12-09T14:33:00Z | |
| dc.date.available | 2025-12-09T14:33:00Z | |
| dc.date.issued | 2011-02-24 | |
| dc.description.abstract | Biocatalysis presents a sound alternative to chemical synthesis in the field of drug production, given the highly selective nature of biological catalysts. Penicillin G Acylase (PGA) from E. coli is currently used to hydrolyze penicillin G (PG) and catalyzes the synthesis of β-lactam antibiotics. In this work, particular emphasis is given to recent developments in penicillin G acylase immobilization, by entrapment simultaneously with nano-magnetic particles in a silica matrix. The sol-gel biocatalytic particles were prepared either by a conventional method (crushed powder) or by a more recent approach, based in an emulsion system using 150 mM AOT/isooctane, which allowed for the formation of spherical micro- and nanobeads. The effects on PGA activity of different sol-gel precursors, additives, enzyme concentration, aging, drying conditions and mechanical stability were evaluated. After these optimization studies, a mechanically stable carrier based on porous xerogels silica matrixes, starting from tetramethoxysilane (TMOS) with 65-67% PGA activity yield in these carriers allowed an immobilization yield of 74 mg protein g dry sol-gel -1 and 930 Ug dry sol-gel -1 for specific activity were obtained. | eng |
| dc.description.sponsorship | S. M. S. A. Bernardino, N. I. Estrela and P. Fernandes acknowledge Fundação para a Ciência e a Tecnologia (Portugal) for financial support in the form of the PhD grants SFRH/BD/30632/2006, SFRH/BD/18639/2004 and for a contract under Program Ciência 2007, respectively. | |
| dc.identifier.citation | Bernardino S., Estrela N., Ochoa-Mendes V., Fernandes P., Fonseca L.P., Optimization in the immobilization of penicillin G acylase by entrapment in xerogel particles with magnetic properties (2011) Journal of Sol-Gel Science and Technology, 58 (2), pp. 545 - 556, Cited 22 times. DOI: 10.1007/s10971-011-2426-7 | |
| dc.identifier.doi | 10.1007/s10971-011-2426-7 | |
| dc.identifier.issn | 0928-0707 | |
| dc.identifier.issn | 1573-4846 | |
| dc.identifier.uri | http://hdl.handle.net/10400.8/14957 | |
| dc.language.iso | eng | |
| dc.peerreviewed | yes | |
| dc.publisher | Springer Science and Business Media LLC | |
| dc.relation.hasversion | https://www.scopus.com/pages/publications/79958784144 | |
| dc.relation.ispartof | Journal of Sol-Gel Science and Technology | |
| dc.rights.uri | http://creativecommons.org/licenses/by-nc-nd/4.0/ | |
| dc.subject | Entrapment | |
| dc.subject | Enzyme immobilization | |
| dc.subject | Magnetic particles | |
| dc.subject | Micro-emulsion | |
| dc.subject | Penicillin G acylase | |
| dc.subject | Sol-gel | |
| dc.title | Optimization in the immobilization of penicillin G acylase by entrapment in xerogel particles with magnetic properties | eng |
| dc.type | journal article | |
| dspace.entity.type | Publication | |
| oaire.citation.endPage | 556 | |
| oaire.citation.issue | 2 | |
| oaire.citation.startPage | 545 | |
| oaire.citation.title | Journal of Sol-Gel Science and Technology | |
| oaire.citation.volume | 58 | |
| oaire.version | http://purl.org/coar/version/c_970fb48d4fbd8a85 | |
| person.familyName | Bernardino | |
| person.givenName | Susana | |
| person.identifier.ciencia-id | E418-2945-9EB6 | |
| person.identifier.orcid | 0000-0001-9454-3281 | |
| person.identifier.scopus-author-id | 14824775000 | |
| relation.isAuthorOfPublication | 9d6614e3-975b-431b-bb0a-00179588eca2 | |
| relation.isAuthorOfPublication.latestForDiscovery | 9d6614e3-975b-431b-bb0a-00179588eca2 |