369
Views
24
CrossRef citations to date
0
Altmetric
Original Articles

Purification and Characterization of Laminaran Hydrolases from Trichoderma viride

, , , , &
Pages 1349-1357 | Received 16 Jan 2003, Accepted 15 Mar 2003, Published online: 22 May 2014

  • 1) Howell, C. R., The role of antibiosis in biocontrol. In “Trichoderma and Gliocladium: Enzymes, Biological Control and Commercial Applications” vol. 2, eds. Harman, G. E., and Kubicek, C. P., Taylor and Francis, London, pp. 174-184 (1998).
  • 2) Toyama, N., and Ogawa, K., Purification and properties of Trichoderma viride mycolytic enzyme. J. Ferment. Technol., 46, 626-633 (1968).
  • 3) de la Cruz, J., Rey, M., Lora, J. M., Hidalgo-Gallego, A., Dominguez, F., Pintor-Toro, J. A., Llobell, A., and Benitez, T., Carbon source control on β-glucanase, chitobiase and chitinase from Trichoderma harzianum. Arch. Microbiol., 159, 316-322 (1993).
  • 4) de la Cruz, J., Pintor-Toro, J. A., Benitez, T., Llobell, A., and Romero, L. C., A novel endo-β-1,3-glucanase, BGN13.1, involved in the mycoparasitism of Trichoderma harzianum. J. Bacteriol., 177, 6937-6945 (1995).
  • 5) Elad, Y., Chet, I., and Henis, Y., Degradation of plant pathogenic fungi by Trichoderma harzianum. Can. J. Microbiol., 28, 719-725 (1982).
  • 6) Cohen-Kupiec, R., Broglie, K. E., Friesem, D., Broglie, R. M., and Chet, I., Molecular characterization of a novel β-1,3-exoglucanase related to mycoparasitism of Trichoderma harzianum. Gene, 226, 147-154 (1999).
  • 7) Manners, D. J., Masson, A. J., Patterson, J. C., Bjorndal, H., and Lindberg, B., The structure of a β-(1→6)-D-glucan from yeast cell walls. Biochem. J., 135, 31-36 (1973).
  • 8) Shida, M., Ushioda, Y., Nakajima, T., and Matsuda, K., Structure of the alkali-insoluble skeletal glucan of Lentinus edodes. J. Biochem. (Tokyo), 90, 1093-1100 (1981).
  • 9) Shiota, M., Nakajima, T., Satoh, A., Shida, M., and Matsuda, K., Comparison of β-glucan structures in a cell wall mutant of Saccharomyces cerevisiae and the wild type. J. Biochem. (Tokyo), 98, 1301-1307 (1985).
  • 10) Henrissatt, B., A classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem. J., 280, 309-316 (1991).
  • 11) Coutinho, P. M., and Henrissat, B., Carbohydrate-Active Enzymes server at URL: http://afmb.cnrs-mrs.fr/~cazy/CAZY/index.html (1999).
  • 12) Pitson, S. M., Seviour, R. J., and McDougall, B. M., Noncellulolytic fungal β-glucanase: their physiology and regulation. Enzyme Microb. Technol., 15, 178-192 (1993).
  • 13) McCreath, K. J., and Gooday, G. W., A rapid and sensitive microassay for determination of chitinolytic activity. J. Microbiol. Methods, 14, 229-237 (1992).
  • 14) Noronha, E. F., and Ulhoa, C. J., Purification and characterization of an endo-β-1,3-glucanase from Trichoderma harzianum. Can. J. Microbiol., 42, 1039-1044 (1996).
  • 15) Noronha, E. F., and Ulhoa, C. J., Characterization of a 29-kDa β-1,3-glucanase from Trichoderma harzianum. FEMS Microbiol. Lett., 183, 119-123 (2000).
  • 16) Vazquez-Garciduenas, S., Leal-Morales, C. A., and Herrera-Estrella, A., Analysis of the β-1,3-glucanolytic system of the biocontrol agent Trichoderma harzianum. Appl. Environ. Microbiol., 64, 1442-1446 (1998).
  • 17) Ogawa, K., Toyama, N., and Sugita, K., Purification and some properties of β-1,3-glucanase from Trichoderma viride. J. Ferment. Technol., 66, 385-392 (1988).
  • 18) Ogawa, K., Ito, M., Tazaki, S., and Nakatsu, S., Breeding and interspecific protoplast fusion of Koji-molds, Aspergillus awamori var. kawachi and Aspergillus usamii mut. shirousamii. J. Ferment. Bioeng., 70, 63-65 (1990).
  • 19) Ogawa, K., Tsuchimori, M., Taniguchi, K., and Nakatsu, S., Interspecific hybridization of Aspergillus usamii mut. shirousamii and Aspergillus niger by protoplast fusion. Agric. Biol. Chem., 53, 2873-2880 (1990).
  • 20) Ogawa, K., Approaches to hybridization and applied genetics by protoplast fusion: Koji-molds and mushrooms. In “Recombinant Microbes for Industrial and Agricultural Applications”, eds. Murooka, Y., and Imanaka, T., Marcel Dekker, Inc., New York, pp. 581-603 (1994).
  • 21) Sibata, Y., and Fujimbara, T., A β-1,6-glucan 6-glucanohydrolase from Gibberella fujikuroi. J. Ferment. Techonol., 51, 216-226 (1973).
  • 22) Yamamoto, S., Kobayashi, R., and Nagasaki, S., Purification and properties of an endo-β-1,6-glucanases from Rhizopus chinesis R-69. Agric. Biol. Chem., 38, 1493-1500 (1974).
  • 23) Wasser, S. P., and Weis, A. L., Therapeutic effects of substances occurring in higher Basidiomycetes mushrooms: a modern perspective. Crit. Rev. Immunol., 19, 65-96 (1999).
  • 24) Ooi, V. E., and Liu, F., Immunomodulation and anti-cancer activity of polysaccharide-protein complexes. Curr. Med. Chem., 7, 715-729 (2000).
  • 25) Omumasaba, C. A., Yoshida, N., and Ogawa, K., Purification and characterization of a chitinase from Trichoderma viride. J. Gen. Appl. Microbiol., 47, 53-61 (2001).
  • 26) Jeuniax, C., Chitinase. Methods Enzymol., 8, 644-650 (1966).
  • 27) Somogyi, M., Notes in sugar determination. J. Biol. Chem., 195, 19-23 (1952).
  • 28) Nelson, N. J., Colorimetric analysis of sugar. Methods Enzymol., 3, 85-86 (1955).
  • 29) Lowry, O. H., Rosebrough, N. J., Farr, A. L., and Randall, R. J., Protein measurement with the Folin reagent. J. Biol. Chem., 193, 265-267 (1951).
  • 30) Laemmli, U. K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London), 227, 680-685 (1970).
  • 31) Doner, L. W., High-performance thin-layer chromatography of starch, cellulose, xylan, and chitin hydrolyzates. Methods Enzymol., 160, 176-180 (1988).
  • 32) Katohda, S., Suzuki, F., Katsuki, S., and Sato, T., Purification and some properties of endo-β-1,6-glucanase from Acinetobacter sp. Agric. Biol. Chem., 43, 2029-2034 (1979).
  • 33) Peat, S., Whelan, W. J., and Lawley, H. G., The structure of laminatin. Part II. The minor structural features. J. Chem. Soc., 729-737 (1958).
  • 34) Maeda, M., and Nisizawa, K., Fine structure of Laminaran of Eisenia bicyclis. J. Biochem., 63, 199-206 (1968).
  • 35) Usui, T., Toriyama, T., and Mizuno, T., Structural investigation of laminaran of Eisenia bicyclis. Agric. Biol. Chem., 43, 603-611 (1979).
  • 36) Aono, R., Hammura, M., Yamamoto, M., and Asano, T., Isolation of extracellular 28- and 42-kilodalton β-1,3-glucanases and comparison of three β-1,3-glucanase produced by Bacillus circulans IAM1165. Appl. Environ. Microbiol., 61, 122-129 (1995).
  • 37) Hrmova, M., and Fincher, G. B., Purification and properties of three (1→3)- β-D-glucanase ioenzymes from young leaves of barley (Hordeum vulgare). Biochem. J., 289, 453-461 (1993).
  • 38) Kim, D. J., Baek, J. M., Uribe, P., Kenerley, C. M., and Cook, D. R., Cloning and characterization of multiple glycosyl hydrolase genes from Trichoderma virens. Curr. Genet., 40, 374-384 (2002).
  • 39) Pitson, S. M., Seviour, R. J., McDougall, B. M., Stone, B. A., and Sadek, M., Purification and characterization of an extracellular (1→6)-β-glucanase from the filamentous fungus Acremonium persicinum. Biochem. J., 316, 841-846 (1996).
  • 40) Rombouts, F. M., and Phaff, H. J., Lysis of yeast cell walls. Lytic β-(1→6)-glucanase from Bacillus circulans WL-12. Eur. J. Biochem., 63, 109-120 (1976).
  • 41) Schep, G. P., Shepherd, M. G., and Sullivan, P. A., Purification and properties of a β-1,6-glucanase from Penicillium brefeldianum. Biochem. J., 223, 707-714 (1984).
  • 42) Miyazaki, T., and Oikawa, N., An endo-(1→6)-β-D-glucanase from Mucor hiemalis. Carbohydr. Res., 48, 209-216 (1976).
  • 43) de la Cruz, J., Pintor-Toro, J. A., Benitez, T., and Llobell, A., Purification and characterization of an endo-β-1,6-glucanase from Trichoderma harzianum that is related to its mycoparasitism. J. Bacteriol., 177, 1864-1871 (1995).
  • 44) de la Cruz, J., and Llobell, A., Purification and properties of a basic endo-β-1,6-glucanase (BGN16.1) from the antagonistic fungus Trichoderma harzianum. Eur. J. Biochem., 265, 145-151 (1999).

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.