Abstract
Cellulases have biological and economic significance in their destructive roles in plant pathogenesis (W. Brown, 1965; Albersheim, 1969) and wood decay (Scheffer and Cowling, 1966; Liese, 1970); in their possible beneficial use in converting waste cellulose into glucose, which may then be converted into the valuable chemical ethanol (Wilkie, 1975); and in their role in cell-wall loosening in higher plants to allow cell elongation and growth (Ridge and Osborne, 1969). The cellulase enzyme system of Trichoderma reesei QM9414 was chosen for this study for two reasons. First, Trichoderma is famous for its ability to degrade highly crystalline cellulose and is one of the most efficient of the cellulolytic fungi (Mandels, 1975). Second, because Trichoderma is such a good source of cellulase, its enzyme system has been studied more extensively than that of any other cellulolytic organism. Consequently, the biochemical characterizations and activities of the various Trichoderma cellulase enzymes are well known.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Albersheim, P., 1969, Biochemistry of the cell wall in relation to infective processes. Annu. Rev. Phytopathol 7: 171.
Benziman, M., Haigler, C. H., Brown, R. M. Jr., White, A. R., Cooper, K. M., 1980, Cellulose biogenesis: Polymerization and crystallization are coupled processes in Acetobacter xylinum. Proc. Natl. Acad. Sci. U.S.A. 77: 6678.
Blackwell, J., Kolpak, F. J., 1976, Cellulose microfibrils as disordered arrays of elementary fibrils. Appl. Polym. Symp. 28: 751.
Brown, R. M. Jr., Willison, J. H. M., Richardson, C. L., 1976, Cellulose biosynthesis in Acetobacter xylinum: Visualization of the site of synthesis and direct measurement of the in vivo process. Proc. Natl. Acad. Sci. U.S.A. 73: 4565.
Brown, W., 1965, Toxins and cell wall dissolving enzymes in relation to plant disease. Annu. Rev. Phytopathol. 3: 1.
Colvin, J. R, 1972, The structure and biosynthesis of cellulose. CRC Crit. Rev. Macromol. Sci. 1: 47.
Emert, G. H., Gum, E. K. Jr., Lang, J. A., Lin, T. H., Brown, R. D. Jr., 1974, Cellulases, in: Food Related Enzymes (J. Whitaker, ed.), pp. 79–100, Advances in Chemistry Series No. 136, American Chemical Society, Washington, D.C.
Eriksson, K.-E., Rzedowski, W., 1969, Extracellular enzyme system utilized by the fungus Chrysosporium lignorum for the breakdown of cellulose. I. Studies on the enzyme production. Arch. Biochem. Biophys. 129: 683.
Fan, L. T., Lee, H. Y., 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.
Gardner, K. H., Blackwell, J., 1974, The structure of native cellulose. Biopolymers 13: 1975.
Grassmann, W., Zechmeister, L., Toth, G., Stadler, R., 1933, Uber den enzymatischen Abban der Cellulose und ihrer Spaltproduckte. Justus Liebigs Ann. Chem. 503: 167.
Green, N. M., Valentine, R. C., Wrigley, N. C., Ahmad, F., Jacobson, B., Wood, H. G., 1972, Transcarbamylase. XI. Electron microscopy and subunit structure. J. Biol. Chem. 247: 6284.
Gregory, D. W., Pirie, B. J. S., 1973, Wetting agents for biological electron microscopy. I. General considerations and negative staining. J. Microsc. (Oxford) 99: 251.
Gritzali, M., Brown, R. D. Jr., 1979, The cellulase system of Trichoderma: Relationships between purified extracellular enzymes from induced or cellulose-grown cells, in: Hydrolysis of Cellulose: Mechanisms of Enzymatic and Acid Catalysis (R. D. Brown, Jr., L. Jurasek, eds.), pp. 237–260, Advances in Chemistry Series, No. 181, American Chemical Society, Washington, D.C.
Gum, E. K. Jr., Brown, R. D. Jr., 1976, Structural characterization of a glycoprotein cellulase, l,4-β-D-glucan cellobiohydrolase C from Trichoderma viride. Biochim. Biophys. Acta 446: 371.
Gum, E. K. Jr., Brown, R. D. Jr., 1977a, Comparison of four purified extracellular 1,4-β-d- glucan cellobiohydrolase enzymes from Trichoderma viride. Biochim. Biophys. Acta 492: 225.
Gum, E. K. Jr., Brown, R. D. Jr., 1977b, Two alternative HPLC separation methods for reduced and normal cellooligosaccharides. Anal. Biochem. 82: 372.
Haigler, C. H., Brown, R. M. Jr., Benziman, M., 1980, Calcofluor White ST alters the in vivo assembly of cellulose microfibrils. Science 210: 903.
Halliwell, G., Griffin, M., 1973, The nature and mode of action of the cellulolytic component C of Trichoderma koningii on native cellulose. Biochem. J. 135: 587.
Hestrin, S., Schramm, M., 1954, Synthesis of cellulose by Acetobacter xylinum. 2. Preparation of freeze-dried cells capable of polymerizing glucose to cellulose. Biochem. J. 58: 345.
Home, R. W., 1978, Special specimen preparation methods for image processing in transmission electron microscopy: A review. J. Microsc. 113: 241.
Iwasaki, T., Hayashi, K., Funatsu, M., 1964, Purification and characterization of two types of cellulase from Trichoderma koningii. J. Biochem. (Tokyo) 55: 209.
Josephs, R., 1971, Electron microscopic studies on glutamic dehydrogenase: Subunit structure of individual molecules and linear associates. J. Mol. Biol. 55: 147.
Keegstra, K., Talmadge. K. W., Bauer, W. D., Albersheim. P., 1973, The structure of plant cell walls. III. A model of the walls of suspension-cultured sycamore cells based on the interconnections of the macromolecular components. Plant Physiol. 51: 188.
Lake, J. A., 1979, Practical aspects of immune electron microscopy. Methods Enzymol. 61: 250.
Li, L. H., Flora, R. M., King, K. W., 1965, Individual roles of cellulase components derived from Trichoderma viride. Arch. Biochem. Biophys. 111: 439.
Liese, W., 1970, Ultrastructural aspects of woody tissue degradation. Annu. Rev. Phytopathol. 8: 231.
Mandels, M., 1975, Microbial sources of cellulase. Biotechnol. Bioeng. Symp. 5: 81.
Massover, W. H., 1978, The ultrastructure of ferritin macromolecules. III. Mineralized iron in ferritin is attached to the protein shell. J. Mol. Biol 123: 721.
Montezinos, D., Brown, R. M. Jr., 1976, Surface architecture of the plant cell: Biogenesis of the cell wall, with special emphasis on the role of the plasma membrane in cellulose biosynthesis. J. Supramol. Struct. 5: 277 (229).
Ohtsuki, M., Isaacson, M. S., Crewe, A. V., 1979, Dark field imaging of biological macromolecules with the scanning transmission electron microscope. Proc. Natl. Acad. Sci. U.S.A. 76: 1228.
Ottensmeyer, F. P., Whiting, R. F., Schmidt, E. E., Clemens, R. S., 1975, Electron microtephroscopy of proteins, A close look at the ashes of myokinase and protamine. J. Ultrastruct. Res. 52: 193.
Ottensmeyer, F. Prew J. W., Bazett-Jones, D. P., Chau, A. S. K., Hewitt, J., 1977, Signal to noise enhancement in dark field electron micrographs of vasopressin: Filtering of arrays of images in reciprocal space. J. Microsc. (Oxford) 109: 259.
Pease, D. C., 1975, Micronets for electron microscopy. Micron 6: 85.
Pringsheim, H., 1912, Uber den fermentativen Abban der Zellulose. Z. Physiol. Chem. 78: 266.
Reese, E. T., 1956, A microbiological process report: Enzymatic hydrolysis of cellulose, Appl. Microbiol. 4: 39.
Reese, E. T., 1975a, Polysaccharases and the hydrolysis of insoluble substrates, in: Biological Transformation of Wood ( W. Liese, ed.), pp. 165–181, Springer-Verlag, Berlin.
Reese, E. T., 1975b, Summary statement on the enzyme system. Biotechnol. Bioeng. Symp. 5: 77.
Reese, E. T., Levinson, H. S., 1952, A comparative study of the breakdown of cellulose by microorganisms. Physiol. Plant. 5: 345.
Reese, E. T., Siu, R. G., Levinson, H. S., 1950, The biological degradation of soluble cellulose derivatives and its relationship to the mechanism of cellulose hydrolysis. J. Bacteriol. 59: 485.
Ridge, I., Osborne, D. J., 1969, Cell growth and cellulases: Regulation by ethylene and indole-3- acetic acid in shoots oiPisum sativum. Nature (London) 223: 318.
Romanovicz, D. K., Brown, R. M. Jr., 1976, Biogenesis and structure of Golgi-derived cellulosic scales in Pleurochrysis. II. Scale composition and supramolecular structure. Appl. Polym. Symp. 28: 587.
Rowland, S. P., 1975, Selected aspects of the structure and accessibility of cellulose as they relate to hydrolysis. Biotechnol. Bioeng. Symp. 5: 183.
Rowland, S. P., Roberts, E. J., 1972, The nature of accessible surfaces in the microstructure of cotton cellulose. J. Polym. Sci. Polym. Chem. Ed. 10: 2447.
Scheffer, T. C., Cowling, E. B., 1966, Natural resistance of wood to microbial deterioration. Annu. Rev. Phytopathol. 4: 147.
Seilliere, G., 1905, Sur la digestion de cellulose. C. R. Seances Soc. Biol. Ses Fil. 58: 409.
Selby, K., Maitland, C. C., 1967, The cellulase of Trichoderma viride: Separation of the components involved in the solubilization of cotton. Biochem. J. 104: 716.
Shoemaker, S. P., Brown, R. D. Jr., 1978a, Enzymic activities of endo-1,4-β-d-glucanases purified from Trichoderma viride. Biochim. Biophys. Acta 523: 133.
Shoemaker, S. P., Brown, R. D. Jr., 1978b, Characterization of en do- 1,4-O-D-glucanases purified from Trichoderma viride. Biochim. Biophys. Acta 523: 147.
Ward, H. M., 1888, A lily-disease. Ann. Bot. (London) 2: 319.
Ward, H. M., 1898, Penicillium as a wood-destroying fungus. Ann. Bot. (London) 12: 565.
White, A. R., Brown, R. M. Jr., 1981, Enzymatic hydrolysis of cellulose: Visual characterization of the process. Proc. Natl. Acad. Sci. U.S.A. 78: 1047.
Whiting, R. F., Ottensmeyer, F. P., 1972, Heavy atoms in model compounds and nucleic acids imaged by darkfield transmission electron microscopy. J. Mol. Biol. 67: 173.
Wilkie, C. R. (ed.), 1975, Cellulose as a Chemical and Energy Source, John Wiley, New York.
Willison, J. H. M., Brown, R. M. Jr., 1978, Cell wall structure and deposition in Glaucocystis. J. Cell Biol. 77: 103.
Wood, T. M., 1968, Cellulolytic enzyme system of Trichoderma koningii: Separation of components attacking native cotton. Biochem. J. 109: 217.
Wood, T. M., McCrae, S. I., 1972, The purification and properties of the C, component of Trichoderma koningii cellulase. Biochem. J. 128: 1183.
Wood, T. M., McCrae, S. I., 1978, Purification and properties of some endoglucanase components with special reference to their action on cellulose when acting along and in synergism with the cellobiohydrolase. Biochem. J. 171: 61.
Zaar, K., 1979, Visualization of pores (export sites) correlated with cellulose production in the envelope of the gram negative bacterium A. xylinum. J. Cell Biol. 80: 773.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1982 Plenum Press, New York
About this chapter
Cite this chapter
White, A.R. (1982). Visualization of Cellulases and Cellulose Degradation. In: Brown, R.M. (eds) Cellulose and Other Natural Polymer Systems. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-1116-4_23
Download citation
DOI: https://doi.org/10.1007/978-1-4684-1116-4_23
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4684-1118-8
Online ISBN: 978-1-4684-1116-4
eBook Packages: Springer Book Archive