Development of a screening method for the identification of a novel Saccharomyces cerevisiae mutant over-expressing Trichoderma reesei cellobiohydrolase II

Annals of Microbiology

Volumn 56, Issue 2, 2006, Pages 143-150

  Gundllapalli, Sarath B ^a,c   Otero, Ricardo R Cordero ^a,d   Pretorius, Isak S ^a,b  

^a STELLENBOSCH UNIVERSITY   (South Africa)

^b AUSTRALIAN WINE RESEARCH INSTITUTE   (Australia)

^c YALE UNIVERSITY SCHOOL OF MEDICINE   (United States)

^d UNIVERSITAT ROVIRA I VIRGILI   (Spain)

Author keywords

Cellobiohydrolase; Saccharomyces cerevisiae; Saccharomycopsis fibuligera; Trichoderma reesei; glucosidase

Indexed keywords

HYPOCREA JECORINA; SACCHAROMYCES CEREVISIAE; SACCHAROMYCETALES; SACCHAROMYCOPSIS FIBULIGERA;

EID: 33745863119     PISSN: 15904261     EISSN: None     Source Type: Journal    
DOI: 10.1007/BF03174996     Document Type: Article

References (25)

1. Aho S., Arffman A., Korhola M. (1996). Saccharomyces cerevisiae mutants selected for increased production of Trichoderma reesei cellulolytic enzymes. Appl. Microbiol. Biotechnol., 46: 36-45.
2. Ausubel F.M., Brent R., Kingston R.E., Moore D.D., Seidman J.G. (1994). Current Protocols in Molecular Biology. John Wiley & Sons., New York.
3. Bellstedt D.U., Human P.A., Rowland G.F., Van der Merwe K.J. (1987). Acid-treated, naked bacteria as immune carriers for protein antigens. J. Immunol. Methods, 98: 249-255.
4. Fan L.T., Lee Y.H., Beardmore D.H. (1980). Mechanism of the enzymatic hydrolysis of cellulose: effects of major structural features of cellulose on enzymatic hydrolysis. Biotechnol. Bioeng., 22: 177-199.
5. Gietz R.D., St. Jean A., Woods R.A., Schiestl R.H. (1992). Improved method for high efficiency transformation of intact yeast cells. Nucleic Acid Res., 20: 1425-1425.
6. Gundllapalli Moses S.B., Cordero Otero R.R., Pretorius I.S. (2005). Domain engineering of Saccharomyces cerevisiae exoglucanases. Biotechnol. Lett., 27: 355-362.
7. Gundllapalli Moses S.B., Cordero Otero R.R., Pretorius I.S. (2006). Effect of the cellulose-binding domain on the catalytic activity of a β-glucosidase from Saccharomycopsis fibuligera. J. Ind. Microbiol. Biotechnol., in press.
8. Karin M., Najarian R.A., Haslinger P., Valenzuela J., Welch J., Fogel S. (1984). Primary structure and transcription of an amplified genetic locus: the CUP1 locus of yeast. Proc. Natl. Acad. Sci. USA, 81: 337-341.
9. Kataeva I., Li X.L., Chen H., Choi S.K., Ljungdahl L.G. (1999). Cloning and sequence analysis of a new cellulase gene encoding CelK, a major cellulosome component of Clostridium thermocellum: evidence for gene duplication and recombination. J. Bacteriol., 181: 5288-5295.
10. Kjeldsen T. (2000). Yeast secretory expression of insulin precursors. Appl. Microbiol. Biotechnol., 54: 277-286.
11. Ko J.H., Hahm M.S., Kang H.A., Nam S.W., Chung B.H. (2002). Secretory expression and purification of Aspergillus niger glucose oxidase in Saccharomyces cerevisiae mutant deficient in PMR1 gene. Protein. Expr. Purif., 25: 488-493.
12. Laemmli U.K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227: 680-685.
13. Lymar E.S., Li B., Renganathan V. (1995). Purification and characterization of a cellulose-binding beta-glucosidase from cellulose-degrading cultures of Phanerochaete chrysosporium. Appl. Environ. Microbiol., 61: 2976-2980.
14. Lynd L.R., Cushman J.H., Nichols R.J., Wyman C.E. (1991). Fuel ethanol from cellulosic biomass. Science 251: 1318-1323.
15. Lynd L.R., Weimer P.J., van Zyl W.H., Pretorius I.S. (2002). Microbial cellulose utilization: Fundamentals and biotechnology. Microbiol. Mol. Biol. Rev., 66: 506-577.
16. Machida M., Ohtsuki I., Fukui S., Yamashita I. (1988). Nucleotide sequences of Saccharomycopsis fibuligera genes for extracellular β-glucosidases as expressed in Saccharomyces cerevisiae. Appl. Environ. Microbiol., 54: 3147-3155.
17. Okada H., Sekiya T., Yokoyama K., Tohda H., Kumagai H., Morikawa Y. (1998). Efficient secretion of Trichoderma reesei cellobiohydrolase II in Schizosaccharomyces pombe and characterization of its products. Appl. Microbiol. Biotechnol., 49: 301-308.
18. Penttilä M.E., Andre L., Lehtovaara P., Bailey M., Teeri T.T., Knowles J.K.C. (1988). Efficient secretion of two fungal cellobiohydrolases by Saccharomyces cerevisiae. Gene, 63: 103-112.
19. Sheehan J., Himmel M. (1999). Enzymes, energy, and the environment: a strategic perspective on the U.S. Department of Energy's research and development activities for bioethanol. Biotechnol. Prog., 15: 817-827.
20. Suzuki K., Ichikawa K., Jigami Y. (1989). Yeast mutants with enhanced ability to secrete human lysozyme: isolation and identification of a protease-deficient mutant. Mol. Gen. Genet., 219: 58-64.
21. Takada G., Kawaguchi T., Sumitani J., Arai M. (1998). Expression of Aspergillus aculeatus No. F-50 cellobiohydrolase I (cbh1) and β-glucosidase 1 (bgl1) genes by Saccharomyces cerevisiae. Biosci. Biotechnol. Biochem., 62: 1615-1618.
22. Towbin H., Staehelin T., Gordon J. (1979). Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA., 76: 4350-4354.
23. Väljamäe P., Sild V., Nutt A., Pettersson G., Johansson G. (1999). Acid hydrolysis of bacterial cellulose reveals different modes of synergistic action between cellobiohydrolase I and endoglucanase I. Eur. J. Biochem., 266: 327-334.
24. Van Rensburg P., Van Zyl W.H., Pretorius I.S. (1997). Over-expression of the Saccharomyces cerevisiae exo-β-1,3-glucanase gene together with the Bacillus subtilis endo-β-1,3-1,4-glucanase gene and the Butyrivibrio fibrisolvens endo-β-1,4-glucanase gene in yeast. J. Biotechnol., 55: 43-53.
25. Warren R.A.J. (1996). Microbial hydrolysis of polysaccharides. Annu. Rev. Microbiol., 50: 183-212.