Mycelial and yeast forms of P. brasiliensis were tested for several glucohydrolases. In addition to high levels of β-blucanases, low amounts of α-glucanase, chitinase and maltase were found. Tests for invertase, amylase and lactase were negative. The levels of β-1,3-glucanase were higher in the mycelial form. The shift to the mycelial phase correlated with an increase in the levels of β-1,3-glucanase. The enzyme was present in the cytoplasm, cell wall and culture medium. The extracellular enzyme was purified 42 fold by ammonium sulphate precipitation and gel filtration. Maximal activity was obtained at 60°C and pH of 5.0 acetate buffer or pH 6.0 (phosphate buffer). Its K m was 0.205 mg/ml. The cell wall-bound enzyme showed a higher temperature optimum. Optimum pH and K m were also slightly different. Following treatment of the cell walls with chitinase, β-1,3-glucanase was released into the medium.
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Abd-El-Al, A. T. H. and Phaff, H. J. 1968. Exo-β-glucanases in yeast. — Biochem. J. 109: 347–360.
Bartnicki-García, S. 1973. Fundamental aspects of hyphal morphogenesis. p. 245. In J. M. Ashworth and J. E. Smith (eds), Microbial differentiation. — The University Press, Cambridge.
Bartnicki-García, S. and Nickerson, W. J. 1962. Nutrition, growth and morphogenesis of Mucor rouxii. — J. Bacteriol. 84: 841–858.
Belcher, R., Nutten, A. J. and Smbrook, C. M. 1954. The determination of glucosamine. —Analyst. 79: 201–208.
Bergmeyer, H. U., and Bernt, E., 1962. p. 123. In H. U. Bergmeyer (ed.), Methods of enzymatic analysis. — Academic Press, New York.
Cortat, M., Matile, P. and Wiemken, A. 1972. Isolation of glucanases containing vesicles from budding yeast. — Arch. Microbiol. 82: 182–205.
Davis, B. J. 1964. Disc electrophoresis. Method and application to human serum proteins. — Ann. N.Y. Acad. Sci. 121: 404–427.
Davis, T. E., Domer, J. E. and Li, Y. T. 1977. Cell wall studies of Histoplasma capsulatum and Blastomyces dermatitidis using autologous and heterologous enzymes. — Infect. Immun. 15: 978–987.
Fleet, G. H. and Phaff, H. J. 1974. Glucanases in Schizosaccharomyces. — J. Biol. Chem. 249: 1717–1728.
Flores-Carreón, A., Reyes, E. and Ruíz-Herrera, J. 1970. Inducible cell wall-bound α-glucosidase in Mucor rouxii. — Biochim. Biophys. Acta 222: 354–360.
Holten, V. E. and Bartnicki-García, S. 1972. Intracellular β-glucanase activity of Phytophthora palmivora. — Biochim. Biophys. Acta 276: 221–227.
Johnston, I. R. 1965. The partial acid hydrolysis of a highly dextroratatory fragment of the cell wall of Aspergillum niger. Isolation of the α-(1–3)-linked dextrin series. — Biochem. J. 96: 659–664.
Kanetsuna, F. and Carbonell, L. M. 1970. Cell wall glucans of the yeast and mycelial forms of Paracoccidioides brasiliensis. — J. Bacteriol. 101: 675–680.
Kanetsuna, F., Carbonell, L. M., Azuma, I. and Yamamura, Y. 1972. Biochemical studies on the thermal dimorphism of Paracoccidioides brasiliensis. — J. Bacteriol. 110: 208–218.
Kanetsuna, F., Carbonell, L. M., Moreno, R. E. and Rodriguez, J. 1969. Cell wall composition of the yeast and mycelial forms of Paracoccicioides brasiliensis. J. Bacteriol. 97: 1036–1041.
Lingappa, Y. and Lockwood, J. L. 1961. A chitin medium for isolation, growth and maintenance of actinomycetes. Nature 189: 158–159.
Lowry, O. H., Rosebrough, N. J., Farr, A. L. and Randall, R. J. 1951. Protein measurement with the Folin phenol reagent. — J. Biol. Chem. 193: 265–275.
Mahadevan, P. R. and Mahadkar, U. R. 1970. Roles of enzymes in growth and morphology of Neurospora crassa: Cell-wall bound enzymes and their possible role in branching. — J. Bacteriol. 101: 941–947.
Notario, V., Villa, T. G., Benitez, T. and Villanueva, J. R. 1976. β-Glucanase in the yeast Cryptococcus albidus var. aerius. Production andsseparation of β-glucanases in asynchronous cultures. — Can. J. Microbiol. 22: 261–268.
Polacheck, Y. and Rosenberger, R. F. 1975. Autolytic enzymes in hyphae of Aspergillus nidulans: their action on old and newly formed walls. — J. Bacteriol. 121: 332–337.
Reese, E. T. and Mandels, M. 1959. β-D-1,3-Glucanases in fungi. — Can. J. Microbiol. 5: 173–185.
San Blas, G. and Moreno, N. 1977. β-Glucanasas periplásmicas en hongos del género Histoplasma. — Acta Cient. Venezolana 28: 338–341.
Somogyi, M. 1952. Notes on sugar determination. — J. Biol. Chem. 195: 19–23.
Srere, P. A. and Mosbach, K. 1974. Metabolic compartmentation: symbiotic, organellar, multienzymic and microenvironmental. — Ann. Rev. Microbiol. 28: 61–83.
Villanueva, J. R. and Gacto, M., 1973. Characterization of β-(1,3)-glucanases of yeasts. — Proc. Third. Int. Spec. Symp. on Yeasts. Part II. p. 261–283.
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Flores-Carreón, A., Gómez-Villanueva, A. & Blas, G.S. β-1,3-Glucanase and dimorphism in Paracoccidioides brasiliensis . Antonie van Leeuwenhoek 45, 265–274 (1979). https://doi.org/10.1007/BF00418589
- Cell Wall
- Phosphate Buffer
- Acetate Buffer
- Maximal Activity