Applied Microbiology and Biotechnology

, Volume 39, Issue 1, pp 99–103

Hydrolytic enzymes secreted by Paecilomyces lilacinus cultured on sclerotia of Aspergillus flavus

  • Subhash C. Gupta
  • Timothy D. Leathers
  • Donald T. Wicklow
Applied Microbial and Cell Physiology


Sclerotia, the survival stage of Aspergillus flavus, are compact masses of mycelia capable of with-standing harsh climatic conditions. Six strains of Paecilomyces lilacinus, originally isolated from sclerotia of A. flavus var. flavus or A. flavus var. parasiticus, were also able to colonize the sclerotia from four different strains of A. flavus under laboratory conditions. P. lilacinus strains did not differ significantly in their colonization ability, but host susceptibility appeared to be an important factor. P. lilacinus strains were cultured in vitro for 96 h on a basal salt medium containing either ground sclerotia of A. flavus or glucose plus asparagine. Activities of hydrolytic enzymes such as polysaccharidases, proteases, and chitinases were determined in the culture supernatants. Supernatants from fungal cultures grown in the basal medium containing glucose plus aspargine medium showed very little or no enzyme activity, whereas fungi grown on ground sclerotia produced a variety of enzymes. Specifically, all strains produced chitinases (endochitinase and N-acetyl glucosaminidase), β-1,3-glucanase, chymoelastase and chymotrypsin, suggesting that these enzymes may be required for colonization of sclerotia. Production of β-1,4-glucanase, dextranase, cellulase, and trypsin was strain variable, suggesting that these enzymes may not be required.


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  1. Bojovic-Cvetic D, Vujicic R (1988) Polysaccharide cytochemistry in maturing Aspergillus flavus sclerotia. Trans Br Mycol Soc 91:619–624Google Scholar
  2. Bradford M (1976) A rapid and sensitive method for the quantification of microgram quantities of proteins utilizing the principle of protein-dye-binding. Anal Biochem 72:248–254Google Scholar
  3. Diener UL, Cole RJ, Sanders GA, Payne GA, Lee LS, Klich MA (1987) Epidemiology of aflatoxin formation by Aspergillus flavus. Annu Rev Phytopathol 25:249–270Google Scholar
  4. Domsch KH, Gams W, Anderson TH (1980) Paecilomyces. In: Compendium of soil fungi. Academic Press, London, pp 530–532Google Scholar
  5. Galvez-Mariscal A, Lopez-Munguia A (1991) Production and characterization of a dextranase from an isolated Paecilomyces lilacinus strain. Appl Microbiol Biotechnol 36:327–331Google Scholar
  6. Gomez-Miranda B, Leal JA (1981) Extracellular and cell wall polysaccharides of Aspergillus alliaceus. Trans Br Mycol Soc 76:249–253Google Scholar
  7. Gupta SC, Leathers TD, El-Sayed GN, Ignoffo CM (1991) Production of degradative enzymes by Metarhizium anisopliae during growth on defined media and insect cuticle. Exp Mycol 15:310–315Google Scholar
  8. Jain S, Parriche M, Durand H, Tiraby G (1990) Production of polysaccharides by a cellulase-pectinase hyperproducing mutant (Pol6) of Penicillium occitanis. Enzyme Microb Technol 12:691–696Google Scholar
  9. Karhuvaara L (1960) On the parasites of the sclerotia of some fungi. Acta Agric Scand 10:127–134Google Scholar
  10. Kelly CT, O'Mahony MR, Fogarty WM (1989) Extracellular xylanolytic enzymes of Paecilomyces varioti. Biotechnol Lett 11:885–890Google Scholar
  11. Leathers TD (1986) Color variants of Aureobasidium overproduce xylanase with extremely high specific activity. Appl Environ Microbiol 52:1026–1030Google Scholar
  12. Makkonen R, Pohjakallio O (1960) On the parasites attacking the sclerotia of some fungi pathogenic to higher plants and on the resistance of these sclerotia to their parasites. Acta Agric Scand 10:105–126Google Scholar
  13. Saksirirat W, Hoppe HH (1990) Verticillium psalliotae an effective mycoparasite of the soybean rust fungus Phakopsora pachyrhizi Syd. Z Pflanzenkr Pflanzenschutz 97:622–633Google Scholar
  14. Saksirirat W, Hoppe HH (1991a) Secretion of extracellular enzymes by Verticillium psalliotae Treschow and Verticillium lecanii Zimm. Viegas during growth on uredospores of the soybean rust fungus Phakopsora pachyrhizi Syd. in liquid cultures. J Phytopathol 131:161–173Google Scholar
  15. Saksirirat W, Hoppe HH (1991b) Degradation of uredospores of the soybean rust fungus Phakopsora pachyrhizi Syd. by cell-free culture filtrates of mycoparasite Verticillium psalliotae Treschow. J Phytopathol 132:33–45Google Scholar
  16. Shotwell OL (dy1977) Aflatoxin in corn. J Am Oil Chem Soc 54:216A–224AGoogle Scholar
  17. Sun J, Cheng X, Zhang Y, Yan Z, Zhang S (1988) A strain of Paecilomyces lilacinus producing high quality dextranase. Ann N Y Acad Sci 542:192–194Google Scholar
  18. Wicklow DT (1987) Survival of Aspergillus flavus sclerotia in soil. Trans Br Mycol Soc 89:131–134Google Scholar
  19. Wicklow DT (1984) Sporogenic germination of sclerotia of Aspergillus flavus and Aspergillus parasiticus. Trans Br Mycol Soc 82:621–624Google Scholar
  20. Wicklow DT, Shotwell OL, Adams GL (1981) Use of aflatoxin-producing ability medium to distinguish aflatoxin-producing strains of Aspergillus flavus. Appl Environ Microbiol 4:697–699Google Scholar
  21. Wicklow DT, Wilson DM (1990) Paecilomyces lilacinus, a colonist of Aspergillus flavus sclerotia buried in soil in Illinois and Georgia. Mycologia 82:393–395Google Scholar

Copyright information

© Springer-Verlag 1993

Authors and Affiliations

  • Subhash C. Gupta
    • 1
  • Timothy D. Leathers
    • 1
  • Donald T. Wicklow
    • 2
  1. 1.Biopolymer Research Unit, National Center for Agricultural Utilization ResearchUSDA, ARSPeoriaUSA
  2. 2.Mycotoxin Research Unit, National Center for Agricultural Utilization ResearchUSDA, ARSPeoriaUSA

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