Enzyme activity of extracellular protein induced in Trichoderma asperellum and T. longibrachiatum by substrates based on Agaricus bisporus and Phymatotrichopsis omnivora

Fungal Biol. 2014 Feb;118(2):211-21. doi: 10.1016/j.funbio.2013.11.012. Epub 2013 Dec 11.

Abstract

Antagonistic Trichoderma spp. are used throughout the world for the biological control of soil-borne plant diseases. This approach has stimulated an on-going search for more efficient mycoparasitic strains with a high potential for producing extracellular lytic enzymes. This study compares the production of lytic enzymes by native strains of Trichoderma asperellum and Trichoderma longibrachiatum on substrates of differing complexity. The quantity of protein induced by Agaricus bisporus-based medium was higher than that induced by Phymatotrichopsis omnivora-based medium. In P. omnivora medium, T. asperellum exhibited higher chitinolytic and β-1,3-glucanolytic activities than T. longibrachiatum. The enzyme profile was related to the previously reported ability of these strains to inhibit the growth of several soil-borne plant pathogens. NAGase production was similar among the tested indigenous strains of T. longibrachiatum; T479 and T359 produced more endochitinase, T479 produced more glucanase, and T341 and T359 produced more β-1,3-glucanase. The detected variations in glucanase and β-1,3-glucanase activities suggest that the production of these enzymes is strongly influenced by the substrate. Strains T397 and T359 exhibited xylanase activity, which triggers defence mechanisms in plants. Thus, these strains may utilise an additional mechanism of biocontrol.

Keywords: Endochitinase; Mycoparasitism; NAGase; Xylanase; β-1,3-Glucanase.

MeSH terms

  • Agaricus / chemistry*
  • Ascomycota / chemistry*
  • Cell Extracts / isolation & purification
  • Culture Media / chemistry
  • Fungal Proteins / metabolism*
  • Glycoside Hydrolases / metabolism*
  • Trichoderma / drug effects*
  • Trichoderma / enzymology

Substances

  • Cell Extracts
  • Culture Media
  • Fungal Proteins
  • Glycoside Hydrolases