2.50
Hdl Handle:
http://hdl.handle.net/10033/235575
Title:
Inclusion bodies of fuculose-1-phosphate aldolase as stable and reusable biocatalysts.
Authors:
Sans, Cristina; García-Fruitós, Elena; Ferraz, Rosa M; González-Montalbán, Núria; Rinas, Ursula; López-Santín, Josep; Villaverde, Antonio; Álvaro, Gregorio
Abstract:
Fuculose-1-phosphate aldolase (FucA) has been produced in Escherichia coli as active inclusion bodies (IBs) in batch cultures. The activity of insoluble FucA has been modulated by a proper selection of producing strain, culture media, and process conditions. In some cases, when an optimized defined medium was used, FucA IBs were more active (in terms of specific activity) than the soluble protein version obtained in the same process with a conventional defined medium, supporting the concept that solubility and conformational quality are independent protein parameters. FucA IBs have been tested as biocatalysts, either directly or immobilized into Lentikat beads, in an aldolic reaction between DHAP and (S)-Cbz-alaninal, obtaining product yields ranging from 65 to 76%. The production of an active aldolase as IBs, the possibility of tailoring IBs properties by both genetic and process approaches, and the reusability of IBs by further entrapment in appropriate matrices fully support the principle of using self-assembled enzymatic clusters as tunable mechanically stable and functional biocatalysts.
Affiliation:
Dept. d'Enginyeria Química, Escola d'Enginyeria, Unitat de Biocatàlisi Aplicada Associada al IQAC (CSIC), Universitat Autònoma de Barcelona, Edifici Q, 08193 Bellaterra, Spain.
Citation:
Inclusion bodies of fuculose-1-phosphate aldolase as stable and reusable biocatalysts., 28 (2):421-7 Biotechnol. Prog.
Journal:
Biotechnology progress
Issue Date:
24-Jul-2012
URI:
http://hdl.handle.net/10033/235575
DOI:
10.1002/btpr.1518
PubMed ID:
22275283
Type:
Article
Language:
en
ISSN:
1520-6033
Appears in Collections:
Publications of the RG Rekombinante Proteinexpression (RPEX)

Full metadata record

DC FieldValue Language
dc.contributor.authorSans, Cristinaen_GB
dc.contributor.authorGarcía-Fruitós, Elenaen_GB
dc.contributor.authorFerraz, Rosa Men_GB
dc.contributor.authorGonzález-Montalbán, Núriaen_GB
dc.contributor.authorRinas, Ursulaen_GB
dc.contributor.authorLópez-Santín, Josepen_GB
dc.contributor.authorVillaverde, Antonioen_GB
dc.contributor.authorÁlvaro, Gregorioen_GB
dc.date.accessioned2012-07-24T14:43:28Z-
dc.date.available2012-07-24T14:43:28Z-
dc.date.issued2012-07-24-
dc.identifier.citationInclusion bodies of fuculose-1-phosphate aldolase as stable and reusable biocatalysts., 28 (2):421-7 Biotechnol. Prog.en_GB
dc.identifier.issn1520-6033-
dc.identifier.pmid22275283-
dc.identifier.doi10.1002/btpr.1518-
dc.identifier.urihttp://hdl.handle.net/10033/235575-
dc.description.abstractFuculose-1-phosphate aldolase (FucA) has been produced in Escherichia coli as active inclusion bodies (IBs) in batch cultures. The activity of insoluble FucA has been modulated by a proper selection of producing strain, culture media, and process conditions. In some cases, when an optimized defined medium was used, FucA IBs were more active (in terms of specific activity) than the soluble protein version obtained in the same process with a conventional defined medium, supporting the concept that solubility and conformational quality are independent protein parameters. FucA IBs have been tested as biocatalysts, either directly or immobilized into Lentikat beads, in an aldolic reaction between DHAP and (S)-Cbz-alaninal, obtaining product yields ranging from 65 to 76%. The production of an active aldolase as IBs, the possibility of tailoring IBs properties by both genetic and process approaches, and the reusability of IBs by further entrapment in appropriate matrices fully support the principle of using self-assembled enzymatic clusters as tunable mechanically stable and functional biocatalysts.en_GB
dc.language.isoenen
dc.rightsArchived with thanks to Biotechnology progressen_GB
dc.titleInclusion bodies of fuculose-1-phosphate aldolase as stable and reusable biocatalysts.en
dc.typeArticleen
dc.contributor.departmentDept. d'Enginyeria Química, Escola d'Enginyeria, Unitat de Biocatàlisi Aplicada Associada al IQAC (CSIC), Universitat Autònoma de Barcelona, Edifici Q, 08193 Bellaterra, Spain.en_GB
dc.identifier.journalBiotechnology progressen_GB
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