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Production of wild‐type and peptide fusion cutinases by recombinant Saccharomyces cerevisiae MM01 strains

2002-06-20Journal article Restricted access
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dc.contributor.authorCalado, Cecília
dc.contributor.authorMannesse, Maurice
dc.contributor.authorEgmond, Maarten
dc.contributor.authorCabral, Joaquim M.S.
dc.contributor.authorFonseca, Luís P. P.
dc.date.accessioned2020-10-02T10:42:35Z
dc.date.available2020-10-02T10:42:35Z
dc.date.issued2002-06-20
dc.description.abstractThis study focused on the growth of Saccha‐romyces cerevisiae MM01 recombinant strains and the respective production of three extracellular heterologous cutinases: a wild‐type cutinase and two cutinases in which the primary structure was fused with the peptides (WP)2 and (WP)4, respectively. Different cultivation and strategies were tested in a 2‐L shake flask and a 5‐L bioreactor, and the respective cell growth and cutinase production were analyzed and compared for the three yeast strains. The highest cutinase productions and productivities were obtained in the fed‐batch culture, where wild‐type cutinase was secreted up to a level of cutinase activity per dry cell weight (specific cell activity) of 4.1 Umg−1 with activity per protein broth (specific activity) of 266 Umg−1, whereas cutinase‐(WP)2 was secreted with a specific cell activity of 2.1 Umg−1 with a specific activity of 200 Umg−1, and cutinase‐(WP)4 with a specific cell activity of 0.7 Umg−1 with a specific activity of 15 Umg−1. The results indicate that the fusion of hydrophobic peptides to cutinase that changes the physical properties of the fused protein limits cutinase secretion and subsequently leads to a lower plasmid stability and lower yeast cell growth. These effects were observed under different cultivation conditions (shake flask and bioreactor) and cultivation strategies (batch culture versus fed‐batch culture).pt_PT
dc.description.versioninfo:eu-repo/semantics/publishedVersionpt_PT
dc.identifier.citationCALADO, Cecília R. C.; [et al] – Production of wild‐type and peptide fusion cutinases by recombinant Saccharomyces cerevisiae MM01 strains. Biotechnology and Bioengineering. ISSN 1097-0290. Vol. 78, N.º 6 (2002), pp. 692-698pt_PT
dc.identifier.doi10.1002/bit.10252pt_PT
dc.identifier.issn1097-0290
dc.identifier.urihttp://hdl.handle.net/10400.21/12273
dc.language.isoengpt_PT
dc.peerreviewedyespt_PT
dc.publisherWileypt_PT
dc.relation.publisherversionhttps://onlinelibrary.wiley.com/doi/epdf/10.1002/bit.10252pt_PT
dc.subjectCutinasept_PT
dc.subjectSaccharomyces cerevisiaept_PT
dc.subjectHeterologous proteinpt_PT
dc.subjectSecretionpt_PT
dc.subjectHydrophobic peptidespt_PT
dc.subjectFusion tagspt_PT
dc.titleProduction of wild‐type and peptide fusion cutinases by recombinant Saccharomyces cerevisiae MM01 strainspt_PT
dc.typejournal article
dspace.entity.typePublication
oaire.citation.endPage698pt_PT
oaire.citation.issue6pt_PT
oaire.citation.startPage692pt_PT
oaire.citation.titleBiotechnology and Bioengineeringpt_PT
oaire.citation.volume78pt_PT
person.familyNameCalado
person.familyNameCabral
person.familyNameP. Fonseca
person.givenNameCecília
person.givenNameJoaquim M.S.
person.givenNameLuis
person.identifier130332
person.identifier.ciencia-id9418-E320-3177
person.identifier.ciencia-idAB13-9ED3-C821
person.identifier.ciencia-id951D-DF38-3397
person.identifier.orcid0000-0002-5264-9755
person.identifier.orcid0000-0002-2405-5845
person.identifier.orcid0000-0001-8429-6977
person.identifier.ridE-2102-2014
person.identifier.ridG-2052-2010
person.identifier.ridA-4228-2013
person.identifier.scopus-author-id6603163260
person.identifier.scopus-author-id7201350203
person.identifier.scopus-author-id55916288400
rcaap.rightsclosedAccesspt_PT
rcaap.typearticlept_PT
relation.isAuthorOfPublicatione8577257-c64c-4481-9b2b-940fedb360cc
relation.isAuthorOfPublication596986f6-6f41-4107-a097-bc205ecdb95a
relation.isAuthorOfPublication5c533551-5113-4c0a-93f1-9c50cbd796bc
relation.isAuthorOfPublication.latestForDiscovery5c533551-5113-4c0a-93f1-9c50cbd796bc

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