Applied Microbiology and Biotechnology

, Volume 39, Issue 1, pp 99–103

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

Authors

  • Subhash C. Gupta
    • Biopolymer Research Unit, National Center for Agricultural Utilization ResearchUSDA, ARS
  • Timothy D. Leathers
    • Biopolymer Research Unit, National Center for Agricultural Utilization ResearchUSDA, ARS
  • Donald T. Wicklow
    • Mycotoxin Research Unit, National Center for Agricultural Utilization ResearchUSDA, ARS
Applied Microbial and Cell Physiology

DOI: 10.1007/BF00166856

Cite this article as:
Gupta, S.C., Leathers, T.D. & Wicklow, D.T. Appl Microbiol Biotechnol (1993) 39: 99. doi:10.1007/BF00166856

Abstract

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.

Copyright information

© Springer-Verlag 1993