Expression of the Ruminococcus flavefaciens cellodextrinase gene in Saccharomyces cerevisiae

Rensburg, Pierre van; Zyl, Willem H. van; Pretorius, Isak S.

doi:10.1007/bf00132014

Cited by 11 publications

(6 citation statements)

References 14 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…From the restriction maps, nucleotide sequences, and chromosomal map positions it can be concluded that EXG1 is identical to BGL1 and that SSG1 is identical to SPR1. The chromosomal location of these four ␤-1,3-glucanase genes in S. cerevisiae is as follows: EXG1/ BGL1 on chromosome XII, EXG2 on chromosome IV, BGL2 on chromosome IV, and SSG1/SPR1 on chromosome XV (120,702). The EXG1 (BGL1) gene encodes a protein whose differential glycosylation accounts for the two main extracellular exo-1,3-␤-glucanases (EXGI and EXGII), present in the culture medium of vegetatively growing cells (181,371,482).…”

Section: Heterologous Cellulase Expression In Bacteriamentioning

confidence: 99%

“…Native secretion sequences have been found sufficient to effect proper posttranslational processing and secretion of functional proteins in the case of genes originating from fungal sources, including EgI, EgII, and Xyn2 of T. reesei (367,368,521); XynC, XlnA, and Man1 of Aspergillus (129,398,611); and a glucoamylase gene. In-frame fusions to the yeast MF␣1 S secretion sequence have been used to express in S. cerevisiae saccharolytic genes from bacteria, including the end1 gene of B. fibrosolvens, the cel1 gene of R. flavefaciens, the beg1 gene of B. subtilis, and the xlnD gene of A. niger (367,368,701,702,703). Although these proteins were often extensively glycosylated, they were still efficiently secreted through the yeast cell wall into the medium (367,368).…”

Section: Heterologous Cellulase Expression In Bacteriamentioning

confidence: 99%

See 1 more Smart Citation

Microbial Cellulose Utilization: Fundamentals and Biotechnology

Lynd

Weimer

Zyl³

et al. 2002

Microbiol Mol Biol Rev

Self Cite

4,006

2,868

View full text Add to dashboard Cite

Fundamental features of microbial cellulose utilization are examined at successively higher levels of aggregation encompassing the structure and composition of cellulosic biomass, taxonomic diversity, cellulase enzyme systems, molecular biology of cellulase enzymes, physiology of cellulolytic microorganisms, ecological aspects of cellulase-degrading communities, and rate-limiting factors in nature. The methodological basis for studying microbial cellulose utilization is considered relative to quantification of cells and enzymes in the presence of solid substrates as well as apparatus and analysis for cellulose-grown continuous cultures. Quantitative description of cellulose hydrolysis is addressed with respect to adsorption of cellulase enzymes, rates of enzymatic hydrolysis, bioenergetics of microbial cellulose utilization, kinetics of microbial cellulose utilization, and contrasting features compared to soluble substrate kinetics. A biological perspective on processing cellulosic biomass is presented, including features of pretreated substrates and alternative process configurations. Organism development is considered for “consolidated bioprocessing” (CBP), in which the production of cellulolytic enzymes, hydrolysis of biomass, and fermentation of resulting sugars to desired products occur in one step. Two organism development strategies for CBP are examined: (i) improve product yield and tolerance in microorganisms able to utilize cellulose, or (ii) express a heterologous system for cellulose hydrolysis and utilization in microorganisms that exhibit high product yield and tolerance. A concluding discussion identifies unresolved issues pertaining to microbial cellulose utilization, suggests approaches by which such issues might be resolved, and contrasts a microbially oriented cellulose hydrolysis paradigm to the more conventional enzymatically oriented paradigm in both fundamental and applied contexts

show abstract

Section: Heterologous Cellulase Expression In Bacteriamentioning

confidence: 99%

Section: Heterologous Cellulase Expression In Bacteriamentioning

confidence: 99%

Microbial Cellulose Utilization: Fundamentals and Biotechnology

Lynd

Weimer

Zyl³

et al. 2002

Microbiol Mol Biol Rev

Self Cite

4,006

2,868

View full text Add to dashboard Cite

show abstract

“…The pectinase gene cassette, consisting of ADH1 P ‐MFα1 S ‐pelE‐ADH1 T (designated PEL5 ) and ADH1 P ‐MFα1 S ‐peh1‐ADH1 T (designated PEH1 ) enabled wine yeast strains of S. cerevisiae to degrade polypectate efficiently87. Likewise, our laboratory has also constructed a glucanase gene cassette comprising the Butyrivibrio fibrisolvens endo‐β‐1,4‐glucanase gene ( END1 ), the Bacillus subtilis endo‐β‐1,3‐1,4‐glucanase gene ( BEG1 ), the Ruminococcus flavefaciens cellodextrinase gene ( CEL1 ), the Phanerochaete chrysosporium cellobiohydrolase gene ( CBH1 ) and the Saccharomycopsis fibuligera cellobiase gene ( BGL1 )162, 163, 164, 165, 166. Upon introduction of this glucanase gene cassette, S. cerevisiae transformants were able to degrade glucans efficiently.…”

Section: Targets For Wine Yeast Strain Developmentmentioning

confidence: 99%

Tailoring wine yeast for the new millennium: novel approaches to the ancient art of winemaking

Pretorius

2000

Yeast

Self Cite

962

406

View full text Add to dashboard Cite

Yeasts are predominant in the ancient and complex process of winemaking. In spontaneous fermentations, there is a progressive growth pattern of indigenous yeasts, with the ®nal stages invariably being dominated by the alcohol-tolerant strains of Saccharomyces cerevisiae. This species is universally known as the `wine yeast' and is widely preferred for initiating wine fermentations. The primary role of wine yeast is to catalyze the rapid, complete and ef®cient conversion of grape sugars to ethanol, carbon dioxide and other minor, but important, metabolites without the development of off-¯avours. However, due to the demanding nature of modern winemaking practices and sophisticated wine markets, there is an ever-growing quest for specialized wine yeast strains possessing a wide range of optimized, improved or novel oenological properties. This review highlights the wealth of untapped indigenous yeasts with oenological potential, the complexity of wine yeasts' genetic features and the genetic techniques often used in strain development. The current status of genetically improved wine yeasts and potential targets for further strain development are outlined. In light of the limited knowledge of industrial wine yeasts' complex genomes and the daunting challenges to comply with strict statutory regulations and consumer demands regarding the future use of genetically modi®ed strains, this review cautions against unrealistic expectations over the short term. However, the staggering potential advantages of improved wine yeasts to both the winemaker and consumer in the third millennium are pointed out.

show abstract

“…Previously, we have constructed plasmid pEND, pCBH and pPR4 ( van Rensburg et al, 1995), respectively. Plasmid pEFB19 containing the BLG1 gene was linearized with BamHI and the protruding ends were filled in with DNA polymerase I (Klenow fragment).…”

Section: Construction Of Recombinant E Coli-s Cerevisiae Shuttle Plmentioning

confidence: 99%