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Screening and Engineering Yeast Transporters to Improve Cellobiose Fermentation by Recombinant Saccharomyces cerevisiae

2024-09Journal article Open access
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dc.contributor.authorKretzer, Leonardo
dc.contributor.authorKnychala, Marília
dc.contributor.authorSilva, Lucca C.
dc.contributor.authorFontoura, Isadora C.C.
dc.contributor.authorLeandro, Maria José
dc.contributor.authorFonseca, César
dc.contributor.authorVerstrepen, Kevin J.
dc.contributor.authorStambuk, Boris
dc.date.accessioned2024-11-13T11:42:11Z
dc.date.available2024-11-13T11:42:11Z
dc.date.issued2024-09
dc.description.abstractABSTRACT: Developing recombinant Saccharomyces cerevisiae strains capable of transporting and fermenting cellobiose directly is a promising strategy for second-generation ethanol production from lignocellulosic biomass. In this study, we cloned and expressed in the S. cerevisiae CEN.PK2-1C strain an intracellular beta-glucosidase (SpBGL7) from Spathaspora passalidarum and co-expressed the cellobiose transporter SiHXT2.4 from Scheffersomyces illinoinensis, and two putative transporters, one from Candida tropicalis (CtCBT1 gene), and one from Meyerozyma guilliermondii (MgCBT2 gene). While all three transporters allowed cell growth on cellobiose, only the MgCBT2 permease allowed cellobiose fermentation, although cellobiose consumption was incomplete. The analysis of the beta-glucosidase and transport activities revealed that the cells stopped consuming cellobiose due to a drop in the transport activity. Since ubiquitinylation of lysine residues at the N- or C-terminal domains of the permease are involved in the endocytosis and degradation of sugar transporters, we constructed truncated versions of the permease lacking lysine residues at the C-terminal domain (MgCBT2 Delta C), and at both the C- and N-terminal domain (MgCBT2 Delta N Delta C) and co-expressed these permeases with the SpBGL7 beta-glucosidase in an industrial strain. While the strain harboring the MgCBT2 Delta C transporter continued to produce incomplete cellobiose fermentations as the wild-type MgCBT2 permease, the strain with the MgCBT2 Delta N Delta C permease was able to consume and ferment all the cellobiose present in the medium. Thus, our results highlight the importance of expressing cellobiose transporters lacking lysine at the N- and C-terminal domains for efficient cellobiose fermentation by recombinant S. cerevisiae.pt_PT
dc.description.versioninfo:eu-repo/semantics/publishedVersionpt_PT
dc.identifier.citationKretzer, L.G., Knychala, M.M., Silva, L.C., Fontoura, I.C.C., Leandro, M.J., Fonseca, C., Verstrepen, K.J. & Stambuk, B.U. (2024) Screening and Engineering Yeast Transporters to Improve Cellobiose Fermentation by Recombinant Saccharomyces cerevisiae. In: Fermentation, 2024, vol. 10 (9), article nº 490. https://doi.org/10.3390/fermentation10090490pt_PT
dc.identifier.doi10.3390/fermentation10090490pt_PT
dc.identifier.eissn2311-5637
dc.identifier.urihttp://hdl.handle.net/10400.9/4382
dc.language.isoengpt_PT
dc.peerreviewedyespt_PT
dc.publisherMDPIpt_PT
dc.relation.publisherversionhttps://doi.org/10.3390/fermentation10090490pt_PT
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/pt_PT
dc.subjectSaccharomyces cerevisiaept_PT
dc.subjectYeastspt_PT
dc.subjectFermentationpt_PT
dc.subjectEthanolpt_PT
dc.titleScreening and Engineering Yeast Transporters to Improve Cellobiose Fermentation by Recombinant Saccharomyces cerevisiaept_PT
dc.typejournal article
dspace.entity.typePublication
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/OE/SFRH%2FBPD%2F102803%2F2014/PT
oaire.citation.titleFermentationpt_PT
oaire.citation.volume10pt_PT
oaire.fundingStreamOE
person.familyNameKretzer
person.familyNameKnychala
person.familyNameTravassos Leandro
person.familyNameFonseca
person.familyNameVerstrepen
person.familyNameStambuk
person.givenNameLeonardo
person.givenNameMarília
person.givenNameMaria José
person.givenNameCésar
person.givenNameKevin
person.givenNameBoris
person.identifier2013922
person.identifier2018724
person.identifierK-5461-2015
person.identifier284260
person.identifier464730
person.identifier.ciencia-idE91B-D158-3535
person.identifier.orcid0000-0002-6547-1239
person.identifier.orcid0000-0001-6803-5670
person.identifier.orcid0000-0002-2254-4610
person.identifier.orcid0000-0003-2448-7063
person.identifier.orcid0000-0002-3077-6219
person.identifier.orcid0000-0001-7507-1020
person.identifier.ridA-6757-2010
person.identifier.ridLEN-0758-2024
person.identifier.scopus-author-id36854236300
person.identifier.scopus-author-id55955425000
person.identifier.scopus-author-id7004417604
project.funder.identifierhttp://doi.org/10.13039/501100001871
project.funder.nameFundação para a Ciência e a Tecnologia
rcaap.rightsopenAccesspt_PT
rcaap.typearticlept_PT
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