Advanced SearchSearch Tips
Characterization and Antifungal Activity from Soilborne Streptomyces sp. AM50 towards Major Plant Pathogens
facebook(new window)  Pirnt(new window) E-mail(new window) Excel Download
 Title & Authors
Characterization and Antifungal Activity from Soilborne Streptomyces sp. AM50 towards Major Plant Pathogens
Jang, Jong-Ok; Lee, Jung-Bok; Kim, Beam-Soo; Kang, Sun-Chul; Hwang, Cher-Won; Shin, Kee-Sun; Kwon, Gi-Seok;
  PDF(new window)
BACKGROUND: Chemical fungicides not only may pollute the ecosystem but also can be environmentally hazardous, as the chemicals accumulate in soil. Biological control is a frequently-used environment-friendly alternative to chemical pesticides in phytopathogen management. However, the use of microbial products as fungicides has limitations. This study isolated and characterized a three-antifungal-enzyme (chitinase, cellulase, and -1,3-glucanase)-producing bacterium, and examined the conditions required to optimize the production of the antifungal enzymes. METHOD AND RESULTS: The antifungal enzymes chitinase, cellulase, and -1,3-glucanase were produced by bacteria isolated from an sawmill in Korea. Based on the 16S ribosomal DNA sequence analysis, the bacterial strain AM50 was identical to Streptomyces sp. And their antifungal activity was optimized when Streptomyces sp. AM50 was grown aerobically in a medium composed of 0.4% chitin, 0.4% starch, 0.2% ammonium sulfate, 0.11% , 0.07% , 0.0001% , and 0.0001% at . A culture broth of Streptomyces sp. AM50 showed antifungal activity towards the hyphae of plant pathogenic fungi, including hyphae swelling and lysis in P. capsici, factors that may contribute to its suppression of plant pathogenic fungi. CONCLUSION(S): This study demonstrated the multiantifungal enzyme production by Streptomyces sp. AM50 for the biological control of major plant pathogens. Further studies will investigate the synergistic effect, to the growth regulations by biogenic amines and antifungal enzyme gene promoter.
Antifungal activity;Biological control;Biogenic amines;Chitinase;Cellulase;Streptomyces sp.;
 Cited by
Akihiro, O., Takashi,A., Makoto,S., 1993. Production of the antifungal peptide antibiotic, Iturin by Bacillus subtilis NB22 in solid state fermentation, J. Ferm. Bioeng. 75, 23-27. crossref(new window)

Akihiro, S., Takeshi, F., Tadakatsu, Y., Kiyotaka, M., 1998. glk A Is involved in glucose repression of chitinase production in Streptomyces lividans, J. Biotechnol. 11, 2911-2914.

Chang, H.L., Wong, X.Z., Hong,L., Ren, X.T., 2001. Antifungal activity of Artemisia annua endophyte cultures against phytopathogenic fungi, J. Biotechnol. 88, 277-282. crossref(new window)

Chernin, L., Chet, I., 2002. Microbial enzymes in biocontrol of plant pathogens and pests, p. 171-225. In R. G. Burns and R.P. Dick (Eds.), Enzymes in the environment: Activity, Ecology, and Applications, Marcel Dekker, New York.

Daulagala, P.W.H.K.P., Allan, E.J., 2003. L-form bacteria of Pseudomonas syringae pV. phaseolicola induce chitinase and enhance resistance to Botrytis cinerea infection in Chinese cabbage, Physiological and Molecular Plant Pathology. 62, 253-263. crossref(new window)

Elad, Y.,Chet, I., Hensis, Y., 1982. Degradation of plant pathogenic fungi by Trichoderma harzianum, Can. J. Microbiol. 28, 719-725. crossref(new window)

Endo, A., Okada, S., 2005. Lactobacillus satsumensis sp. nov. isolated from mashes of shochu, a traditional Japanese distilled spirit made from fermented rice and other starchy materials, Int. J. Syst. Evol. Microbiol. 55, 83-85. crossref(new window)

Felsenstein, J., 1993. PHYLIP (phylogeny inference package), version 3.5c. Distributed by the author. Department of Genome Sciences, University of Washington, Seattle, USA.

Hassane, A.L., Andres, S., Manuel, R., Jesus, D.L.C., Enriaue, M., Antonio,L., 2001. An antifungal exo-$\alpha$-1,3-glucanase (ANG13.1) from the biocontrol fungus Trichoderma harzianum, Appl. Microbiol. Biotechnol. 67, 5833-5839.

Johnson, L.F., Cirl, E.A., 1972. Methods for research on the ecology of soil-borne plant pathogens, p.241. Burgess Publishing Company, Minnesota.

Jukes, T.H., Cantor, C.R., 1969. Evolution of protein molecules. In Mammalian Protein Metabolism, vol. 3, p. 21-132. Edited by H. N. Munro, Academic Press, New York.

Kim, K., Ji, H.S., 2001. Effect of chitin sources on production of chitinase and chitosanase by Streptomyces griseus HUT 6037, Biotechnol. Bioprocess Eng. 6, 18-24. crossref(new window)

Kitamoto, Y., Mori, N., Yamamoto, M., Ohiwa, T., Ichiwaka, Y., 1998. A simple method for protoplast formation and generation from various fungi, Appl. Microbiol. Biotechnol. 28, 445-450.

Kiyotaka, M., Takeshi, F., Akihiro, S., 2000. Induction and response to various carbon sources, Biosci. Biotechnol. Biochem. 64, 39-43. crossref(new window)

Kwakman, J.H.J.M., Postma, P.W., 1994. Glucose kinase has a regulatory role in carbon catabolite repression in Streptomyces coelicolor, J. Bacteriol. 176, 2694-2698. crossref(new window)

Marrianne, B., Buurlage, S., Ponstein, A.S.,. BresVloemans, S.A, Melchers, L.S., van den Elzen, P.J.M., Cornelissen, B.J.C., 1993. Only specific tobacco (Nicotiana tabacum) chitinase and $\beta$-1,3-glucan ase exhibit antifungal activity, Plant Physiol. 101, 857-863. crossref(new window)

Merav, K., Marianna, O., Ilan, C., Leonid, C., 2003. Soil-borne strain IC14 of Serratiaplymuthica with multiple mechanisms of antifungal activity provides biocontrol of Botrytis cinerea and Sclerotinia sclerotiorum diseases, Soil boil. Biochem. 35, 323-331. crossref(new window)

Miller, G.L., 1959. Use of the dinitrosalicylic acid reagent for the determination of reducing sugars, Anal. Chem. 31, 426-428. crossref(new window)

Phae, G.C., Shoda, M., Kita, N., Nakano, M., Ushiyama. K., 1992. Biological control of crown and root and bacterial wilt of tomato by Bacillus subtilis NB22, Ann. Phytopathol. Soc. Jpn. 58, 329-339. crossref(new window)

Sachslehner, A., Nidetzky, B., Kulbe, K.D., Haltrich, D., 1998. Induction of mannose, xylanase, and endoglucanase activities in Sclerotium rolfsii, Enzyme Microb. Technol. 64, 594-600.

Sindhu, S.S., Dadarwal, K.R., 2001. Chitinolytic and cellulolytic Pseudomonas sp. antagonistic to fungal pathogens enhances nodulation by Mesorhizobium sp. Cicer in chickpea, Microbiol. Res. 156, 353-358. crossref(new window)

Takahashi, M., Tsukiyama, T., Suzuki, T., 1993. Purification and some properties of chitinase produced by Vibrio sp., J. Ferment. Bioeng. 75, 457-459. crossref(new window)

Thompson, J.D., Gibson, T.J., Plewniak, F., Jeanmougin, F., Higgins, D.G., 1997. The CLUSTAL_X Windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools, Nucleic Acids Res. 25, 4876-4882. crossref(new window)

Wang, S.L., Shih, I.L., Wang, C.H., Tseng, K.C., Chang, W.T., Twu, Y.K., Ro, J.J., Wang., C.L., 2002. Production of antifungal compounds from chitin by Bacillus subtilis, Enzyme Microb. Technol. 31, 321-328. crossref(new window)

Wang, S.L., Yieh, T.C., Shih, I.L., 1999. Production of antifungal compounds by Pseudomonas aeruginosa K-187 using shrimp and crab shell powder as a carbon source, Enzyme Microb. Technol. 25, 142-148. crossref(new window)

Wang, S.L., Yen, Y.H., Tsiao, W.J., Chang, W.T., Wang, C.L., 2002. Production of antimicrobial compounds by Monascus purpureus CCRC31499 using shrimp and crab shell powder as a carbon source, Enzyme Microb. Technol. 31, 337-344. crossref(new window)

Wichitra, L., Pranom, S., Souwalak, P., 2005. Purification, characterization and synergistic activity of $\beta$-1,3-glucanase and antibiotic extract from an antagonistic Bacillus subtilis NSRS 89-24 against rice blast and sheath blight, Enzyme Microb. Technol. 38, 990-997.

Wietse, B., Paulien, J.A.K.G., Petrar, L., Janse, J.D., Spit, B.E., Woldendorp, J.W., 1998. Anti-fungal properties of chitinolytic dune soil bacteria, Soil Biol. Biochem. 2, 193-203.