Engineering yeast for efficient cellulose degradation

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dc.contributor.authorVan Rensburg P.
dc.contributor.authorVan Zyl W.H.
dc.contributor.authorPretorius I.S.
dc.date.accessioned2011-05-15T16:05:35Z
dc.date.available2011-05-15T16:05:35Z
dc.date.issued1998
dc.description.abstractSaccharomyces cerevisiae produces several β-1,3-glucanases, but lacks the multicomponent cellulase complexes that hydrolyse the β-1,4-linked glucose polymers present in cellulose-rich biomass as well as in haze-forming glucans in certain wines and beers. We have introduced into S. cerevisiae a functional cellulase complex for efficient cellulose degradation by cloning the Endomyces fibuliger cellobiase (BGL1) gene and co-expressing it with the Butyrivibrio fibrisolvens endo-β-1,4-glucanase (END1), the Phanerochaete chrysosporium cellobiohydrolase (CBH1) and the Ruminococcus flavefaciens cellodextrinase (CEL1) gene constructs in this yeast. The END1, CBH1 and CEL1 genes were inserted into yeast expression/secretion cassettes. Expression of END1, CBH1 and CEL1 was directed by the promoter sequences derived from the alcohol dehydrogenase II (ADH2), the phosphoglycerate kinase I(PKG1) and the alcohol dehydrogenase I (ADH1) genes, respectively. In contrast, BGL1 was expressed under the control of its native promoter. Secretion of End1p and Cel1p was directed by the signal sequence of the yeast mating pheromone α-factor (MFα1), whereas Cbh1p and Bgl1p were secreted using their authentic leader peptides. The construction of a fur1 ura3 S. cerevisiae strain allowed for the autoselection of this multicopy URA3-based plasmid in rich medium. S. cerevisiae transformants secreting biologically active endo-β-1,4-glucanase, cellobiohydrolase, cellodextrinase and cellobiase were able to degrade various substrates including carboxymethylcellulose, hydroxyethylcellulose, laminarin, barley glucan, cellobiose, polypectate, birchwood xylan and methyl-β-D-glucopyranoside. This study could lead to the development of industrial strains of S. cerevisiae capable of converting cellulose in a one-step process into commercially important commodities.
dc.description.versionArticle
dc.identifier.citationYeast
dc.identifier.citation14
dc.identifier.citation1
dc.identifier.issn0749503X
dc.identifier.other10.1002/(SICI)1097-0061(19980115)14:1<67::AID-YEA200>3.0.CO;2-T
dc.identifier.urihttp://hdl.handle.net/10019.1/13197
dc.subjectbeta glucosidase
dc.subjectcellulase
dc.subjectcellulose
dc.subjectcellulose 1,4 beta cellobiosidase
dc.subjectarticle
dc.subjectbioengineering
dc.subjectcontrolled study
dc.subjectdegradation
dc.subjectgene construct
dc.subjectgene expression regulation
dc.subjectmolecular cloning
dc.subjectnonhuman
dc.subjectphanerochaete
dc.subjectpriority journal
dc.subjectpromoter region
dc.subjectsaccharomyces cerevisiae
dc.subjectyeast
dc.subjectBacterial Proteins
dc.subjectbeta-Glucosidase
dc.subjectBlotting, Northern
dc.subjectBlotting, Southern
dc.subjectCellulase
dc.subjectCellulose
dc.subjectCellulose 1,4-beta-Cellobiosidase
dc.subjectCloning, Molecular
dc.subjectGene Expression Regulation, Fungal
dc.subjectGenes, Fungal
dc.subjectPlasmids
dc.subjectRecombinant Proteins
dc.subjectSaccharomyces cerevisiae
dc.subjectTransformation, Genetic
dc.subjectButyrivibrio fibrisolvens
dc.subjectChrysosporium
dc.subjectEndomyces
dc.subjectHordeum vulgare subsp. vulgare
dc.subjectPhanerochaete
dc.subjectPhanerochaete chrysosporium
dc.subjectRuminococcus flavefaciens
dc.subjectSaccharomyces cerevisiae
dc.subjectSaccharomycopsis fibuligera
dc.titleEngineering yeast for efficient cellulose degradation
dc.typeArticle
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