Production of Hormoconis resinae glucoamylase P by a stable industrial strain of Saccharomyces cerevisiae

Vainio, Arja E. I.; Lantto, Raija; Parkkinen, Elke; Torkkeli, Helena T.

doi:10.1007/bf00166081

Cited by 8 publications

(2 citation statements)

References 12 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In fermentation processes, raw starch is first gelatinized by cooking, then liquefied with α‐amylase and finally saccharified to glucose by glucoamylase, since S. cerevisiae lacks the enzymes necessary for starch utilization. This limitation is now relieved by heterologous expression of amylolytic enzymes in this organism [4–8].…”

Section: Introductionmentioning

confidence: 99%

Efficient utilization of starch by a recombinant strain of Saccharomyces cerevisiae producing glucoamylase and isoamylase

Lin

Chien

et al. 2000

Biotech and App Biochem

View full text Add to dashboard Cite

Two plasmids, designated pRTI and pTI, were constructed to allow the integration of a bacterial isoamylase gene (iso) into Saccharomyces cerevisiae G23-8 chromosome. The integrative plasmid pRTI comprises the iso gene from Pseudomonas amyloderamosa, a portion of S. cerevisiae ribosomal DNA (rDNA), S. cerevisiae trp1 gene deficient in promoter and the bacterial vector pSP72. The structure of plasmid pTI is similar to that of pRTI, except that it lacks an rDNA segment. The Aspergillus awamori glucoamylase and P. amyloderamosa isoamylase genes were expressed in the recombinant strain of S. cerevisiae under the control of the yeast alcohol dehydrogenase gene (adh1) promoter. Southern-blot analysis showed that these plasmids were integrated into the yeast chromosome in tandem repeat and dispersion copies. The recombinant strains could assimilate starch more efficiently than the recipient strain with a conversion rate of greater than 95%.

show abstract

Section: Introductionmentioning

confidence: 99%

Efficient utilization of starch by a recombinant strain of Saccharomyces cerevisiae producing glucoamylase and isoamylase

Lin

Chien

et al. 2000

Biotech and App Biochem

View full text Add to dashboard Cite

show abstract

“…Furthermore, by utilizing yeast proteins secretion systems, foreign peptides can be secreted to the external medium. In this respect, by utilizing yeast secretion systems, such as ␣-factor signal peptide, attempts were made to produce several recombinant proteins (Kilonzo et al, 2008;Gorgens et al, 2001;Bannister and Wittrup, 2000;Shiba et al, 1994;Vainio et al, 1994;Chau et al, 2000;Chen et al, 2006;Ekino et al, 2002).…”

Section: Introductionmentioning

confidence: 99%