Summary
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1.
Mycelial extracts and culture filtrates of two species of Trametes have been assayed for various enzymatic activities. The tests performed after 3 and 10 days of mycelial growth on 3% malt extract have revealed that the spectra of external enzymes secreted by both strains differ markedly from their intracellular equivalents. A great part of the external isozyme bands, shown in disc electrophoresis and isoelectric focusing, have no equivalent acting within the cell.
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2.
These findings are discussed on the basis of special functional properties which have to be attributed to external enzymes. It is concluded that a great number of them are not simply internal enzymes which happen to be active outside the cell but that they are synthesized or at least modified especially for extracellular action under these special conditions.
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3.
A comparison between the two species of Trametes has shown that both produce enzymes with identical function. This indicates their strong relationship, though the electrophoretic mobility of most of the enzymes is not comparable. The consequences of these findings for chemical taxonomy are discussed.
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References
Ahlgren, E., Eriksson, K. E.: Characterization of cellulases and related enzymes by isoelectric focusing, gel filtration and zone electrophoresis. II. Studies on Stereum sanguinolentum, Fomes annosus and Chrysosporium lignorum enzymes. Acta chem. scand. 21, 1193–1199 (1967).
Amano, T., Takeuchi, T., Yoshii, H.: Studies on antiseptics for use in soy sauce: X. Properties of n-butyl p-hydroxybenzoate esterase produced by Aspergillus sojae. J. Ferment. Technol. 47, 610–616 (1969).
Blaich, R.: Störungen bei der isoelektrischen Fokussierung von Proteinen durch anorganische Ionen. Naturwissenschaften 58, 55–56 (1971).
Cheung, D. S. M., Marshall, K. C.: Antigenic similarity between isolates of Trametes versicolor (Linneaeus ex Fries). Lloyd and other related species. Arch. Mikrobiol. 57, 232–238 (1967).
——: Antigenic and some kinetic properties of three p-diphenol oxidase isozymes of Trametes versicolor. Biochim. biophys. Acta (Amst.) 178, 177–180 (1969).
Eriksson, K. E., Rzedowski, W.: Extracellular enzyme system utilized by the fungus Chrysosporium lignorum for the breakdown of cellulose. I. Studies on the enzyme production. Arch. Biochem. 129, 683–688 (1969).
Esser, K.: Die Phenoloxydasen des Ascomyceten Podospora anserina. I. Identifizierung von Laccase und Tyrosinase beim Wildstamm. Arch. Mikrobiol. 46, 217–226 (1963).
Eylar, E. H.: On the biological role of glycoproteins. J. theoret. Biol. 10, 89–113 (1965).
Feniksova, R. V., Ermoshina, G. K.: Acid resistance of α-amylases of different origin. Priklad Biokhim. Mikrobiol. 5, 137–140 (1969).
Folk, J. E., Burstone, M. S.: Chromgenetic leucyl substrates for aminopeptidase and papain. Proc. Soc. exp. Biol. (N. Y.) 89, 473–476 (1955).
Gascon, S., Neumann, N. P., Lampen, J. O.: Comparative study of the properties of the purified internal and external invertases from yeast (Saccharomyces strains). J. biol. Chem. 243, 1573–1577 (1968).
Glynn, A. N., Reid, J.: Electrophoretic patterns of soluble fungal proteins and their possible use as taxonomic criteria in the genus Fusarium. Canad. J. Bot. 47, 1823–1831 (1969).
Grabbe, K., Koenig, R., Haider, K.: Die Bildung der Phenoloxydase und die Stoffwechselbeeinflussung durch Phenole bei Polystictus versicolor. Arch. Mikrobiol. 63, 133–153 (1968).
Haglund, H.: Isoelectric focusing in natural pH gradients—a technique of growing importance for fractionation and characterization of proteins. Sci. Tools 14, 17–23 (1967).
Hubby, J. L., Lewontin, R. C.: A molecular approach to the study of genic heteroxygosity in natural population. I. The number of alleles at different loci in Drosophila pseudoobscura. Genetics 54, 577–594 (1966).
Jonsson, M., Pettersson, E., Reinhammar, B.: Isoelectric fractionation, analysis and characterization of ampholytes in natural pH gradients. VII. The isoelectric spectra of fungal laccase A and B. Acta chem. scand. 22, 2135–2140 (1968).
Lillie, R. D., Burtner, H. J.: Stable sudanophilia of human neutrophil leucocytes in relation to peroxidase and oxidase. J. Histochem. Cytochem. 1, 8–26 (1953).
Meyer, J. A., Renard, J. L.: Protein and esterase patterns of two formae speciales of Fusarium oxysporum. Phytopathology 59, 1409–1411 (1969).
Nealson, K. H., Garber, E. D.: An electrophoretic survey of esterases, phosphatases and leucine aminopeptidases in mycelial extracts of species of Aspergillus. Mycologia (N. Y.) 59, 330–336 (1967).
Pazur, J. H., Simpson, D. L., Knull, H. R.: Biosynthesis of glucohydrolase I, a glycoenzyme from Aspergillus niger. Biochem. biophys. Res. Commun. 36, 394–400 (1969).
Peberdy, J. F., Turner, M.: The esterases of Mortierella ramanniana in relation to taxonomy. J. gen. Microbiol. 51, 303–312 (1968).
Reese, E. T., Maguire, A., Parrish, F. W.: Benzoyl esterases of fungi. Canad. J. Biochem. 47, 511–516 (1969).
Reiss, J.: Cytochemischer Nachweis von Hydrolasen in Pilzzellen. I. Glykosidasen. Histochemie 18, 12–23 (1969).
Rösch, R., Liese, W., Berndt, H.: Untersuchungen über die Enzyme von Bläuepilzen: I. Cellulase-, Polygalakturonase-, Pektinesterase- und Laccase-Aktivität. Arch. Mikrobiol. 67, 28–50 (1969).
Rutenburg, A. M., Seligmann, A. M.: The histochemical demonstration of acid phosphatase by a post incubation coupling technique. J. Histochem. Cytochem. 3, 455–470 (1955).
Steward, F. C., Barber, J. T.: The use of acrylamide gel electrophoresis in the investigation of the soluble proteins of plants. Ann. N. Y. Acad. Sci. 121, 225–231 (1964).
Strumeyer, D. H., Malin, M. J.: Resistance of extracellular yeast invertase and other glycoproteins to denaturation by tannins. Biochem. J. 118, 899–900 (1970).
Vasu, S.: Pectolytic enzymes of Aspergillus niger. II. Intracellular distribution of polygalacturonases, pectinmethylesterases and pectintranseliminases. Rev. Roum. Biochim. 4, 67–74 (1967).
Wrigley, C. W.: Gel-electrofocusing—a technique for analyzing multiple protein samples by isoelectric focusing. Sci. Tools 15, 17–23 (1968).
Yamadea, H., Adachi, O., Watanabe, M., Ogata, K.: Tannase (tannin acyl hydrolase), a typical serine esterase (from Aspergillus, Penicillium). Agr. Biol. Chem. 32, 257–258 (1968).
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With support of the Deutsche Forschungsemeinschaft (Bad Godesberg).
Supported by a fellowship of the Humboldt-Stiftung (Bad Godesberg).
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Scháněl, L., Blaich, R. & Esser, K. Function of enzymes in wood decaying fungi. Archiv. Mikrobiol. 77, 140–150 (1971). https://doi.org/10.1007/BF00408606
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DOI: https://doi.org/10.1007/BF00408606