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Expression of the β-1,3-Glucanase Gene in Yeast Hansenula Polymorpha

  • Shi-Hsiang Shen
  • Lison Bastien

Abstract

The yeast cell wall is composed mainly of glucan, mannoprotein and chitin (1). In most yeasts, the polysaccharide glucan is predominantly β-1,3-linked with some branching via (3-1,6- linkages (2). The glucan network in the yeast cell wall, due to its rigidity, is an essential structure in preventing lysis of the protoplast in a hypotonic environment. Several microorganisms have been reported to produce extracellular enzymes capable of lysing yeast cells (3,4). Analysis of the constituents of these lytic enzyme preparations revealed the presence, among other activities, of β-1,3-glucanases (3,5). When combinedwith athiol reagent, β-1,3-glucanase alone was found to be able to lyse the yeast cell (6). Currently, the most common-used enzyme for digestion of yeast cell walls is an enzyme preparation called Zymolyase, produced from Oerskovia xanthineolytica (5). We have isolated the glucanase gene from this organism and completely determined its sequence (7).

Keywords

Yeast Cell Glucanase Activity Yeast Cell Wall Periplasmic Protein Glucanase Gene 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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References

  1. 1.
    Ballau, C.E.(1982) in The Molecular Biology of the Yeast Saccharomyces(Strathern J.N., Jones, E.W., and Broach, J.R.,eds)pp. 335–360, Cold Sping HarborGoogle Scholar
  2. 2.
    Manners, D.L. Masson, A.J.,and Patterson, J.C.(1973) Biochem. J. 135,19–31PubMedGoogle Scholar
  3. 3.
    Doi, K., Doi, A., and Fukui, T. (1971) J. Biochem. 70,711–714PubMedGoogle Scholar
  4. 4.
    Kitamura, K., KaneKo, T., and Yamamoto, Y.(1971) Arch. Biochem. Biophys. 145, 402–404PubMedCrossRefGoogle Scholar
  5. 5.
    Katamura, K., Kaneko, T., and Yamamoto, Y. (1974) J. Gen. Appl. Microbiol. 20, 323–344Google Scholar
  6. 6.
    Scott, J., and Schekman, R. (1980) J. Bacteriol. 142, 414–423PubMedGoogle Scholar
  7. 7.
    Shen S.H., Chretien, P., Bastien, L, and Slilaty, S.N. (1991) J. Biol. Chem. 286, 1056–1063Google Scholar
  8. 8.
    Shen, S.H., Bastien, L., Nguyen, T., Fung, M., and Slilaty. S.N. (1990) Gene 84, 303–309Google Scholar
  9. 9.
    Esmon, P.C., Esmon, S.E., Schauer, I.E., Taylor, A., and Schekman, R. (1987) J. Biol. Chem. 282:4387–4334Google Scholar
  10. 10.
    Emr, S.D., Schauer, I., Hansen, N., Esmon, P., and Schekman, R. (1984) Mol. Cell. Biol. 4:2347–2355PubMedGoogle Scholar

Copyright information

© Plenum Press, New York 1992

Authors and Affiliations

  • Shi-Hsiang Shen
    • 1
  • Lison Bastien
    • 1
  1. 1.Biotechnology Research InstituteNational Research Council of CanadaMontrealCanada

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