Please use this identifier to cite or link to this item: https://hdl.handle.net/2440/55074
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dc.contributor.authorEksteen, J.-
dc.contributor.authorvan Rensburg, P.-
dc.contributor.authorCordero Otero, R.-
dc.contributor.authorPretorius, I.-
dc.date.issued2003-
dc.identifier.citationBiotechnology and Bioengineering, 2003; 84(6):639-646-
dc.identifier.issn0006-3592-
dc.identifier.issn1097-0290-
dc.identifier.urihttp://hdl.handle.net/2440/55074-
dc.description.abstract<jats:title>Abstract</jats:title><jats:p><jats:italic>Lipomyces kononenkoae</jats:italic> and <jats:italic>Saccharomycopsis fibuligera</jats:italic> possess highly efficient α‐amylase and/or glucoamylase activities that enable both of these yeasts to utilize raw starch as a carbon source. Eight constructs containing the <jats:italic>L. kononenkoae </jats:italic>α‐amylase genes (<jats:italic>LKA1</jats:italic> and <jats:italic>LKA2</jats:italic>), and the <jats:italic>S. fibuligera</jats:italic> α‐amylase (<jats:italic>SFA1</jats:italic>) and glucoamylase (<jats:italic>SFG1</jats:italic>) genes were prepared. The first set of constructs comprised four single gene cassettes each containing one of the individual amylase coding sequences (<jats:italic>LKA1, LKA2, SFA1</jats:italic> or <jats:italic>SFG1</jats:italic>) under the control of the phosphoglycerate kinase gene (<jats:italic>PGK1</jats:italic>) promoter and terminator, while the second set comprised two single cassettes containing <jats:italic>SFA1</jats:italic> and <jats:italic>SFG1</jats:italic> linked to their respective native promoters and terminators. The third set of constructs consisted of two double‐gene cassettes, one containing <jats:italic>LKA1</jats:italic> plus <jats:italic>LKA2 </jats:italic>under the control of the <jats:italic>PGK1</jats:italic> promoter and terminator, and the other <jats:italic>SFA1</jats:italic> plus <jats:italic>SFG1</jats:italic> controlled by their respective native promoters and terminators. These constructs were transformed into a laboratory strain <jats:italic>Saccharomyces cerevisiae</jats:italic> (Σ1278b). Southern‐blot analysis confirmed the stable integration of the different gene constructs into the <jats:italic>S. cerevisiae</jats:italic> genome and plate assays revealed amylolytic activity. The strain expressing <jats:italic>LKA1</jats:italic> and <jats:italic>LKA2</jats:italic> resulted in the highest levels of α‐amylase activity in liquid media. This strain was also the most efficient at starch utilization in batch fermentations, utilizing 80% of the available starch and producing 0.61g/100 mL of ethanol after 6 days of fermentation. The strain expressing <jats:italic>SFG1</jats:italic> under the control of the <jats:italic>PGK1</jats:italic> expression cassette gave the highest levels of glucoamylase activity. It was shown that the co‐expression of these heterologous α‐amylase and glucoamylase genes enhance starch degradation additively in <jats:italic>S. cerevisiae</jats:italic>. This study has resulted in progress towards laying the foundation for the possible development of efficient starch‐degrading <jats:italic>S.</jats:italic> cerevisiae strains that could eventually be used in consolidated bioprocessing, and in the brewing, whisky, and biofuel industries. © 2003 Wiley Periodicals, Inc. <jats:italic>Biotechnol Bioeng</jats:italic> <jats:bold>84:</jats:bold> 639–646, 2003.</jats:p>-
dc.description.statementofresponsibilityJ.M. Eksteen, P. van Rensburg , R.R. Cordero Otero and I.S. Pretorius-
dc.language.isoen-
dc.publisherJohn Wiley & Sons Inc-
dc.source.urihttp://dx.doi.org/10.1002/bit.10797-
dc.subjectα-amylase-
dc.subjectglucoamylase-
dc.subjectstarch fermentation-
dc.subjectyeast-
dc.titleStarch fermentation by recombinant Saccharomyces cerevisiae strains expressing the alpha-amylase and glucoamylase genes from lipomyces kononenkoae and saccharomycopsis fibuligera-
dc.typeJournal article-
dc.identifier.doi10.1002/bit.10797-
pubs.publication-statusPublished-
Appears in Collections:Agriculture, Food and Wine publications
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