Purification and identification of a novel antifungal protein from Bacillus subtilis XB-1

World J Microbiol Biotechnol. 2019 Sep 23;35(10):150. doi: 10.1007/s11274-019-2726-6.

Abstract

This study aimed to characterize a powerful antifungal component from bacteria. Bacillus subtilis strain XB-1, which showed maximal inhibition of Monilinia fructicola, was isolated and identified, and an antifungal protein was obtained from it. Ammonium sulfate precipitation, ion exchange chromatography, and sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) were used to purify and identify the proteins secreted by B. subtilis XB-1. Analyses revealed that purified fraction V had the strongest antifungal effect, with the largest pathogen inhibition zone diameter of 4.15 cm after 4 days (P < 0.05). This fraction showed a single band with a molecular weight of approximately 43 kDa in SDS-PAGE. Results from SDS-PAGE and liquid chromatography electrospray ionization tandem mass spectrometry analyses demonstrated that fraction V was likely a member of the chitosanase family. These results suggest that B. subtilis XB-1 and its antifungal protein may be useful in potential biocontrol applications.

Keywords: Antifungal protein; Bacillus subtilis; Chitosanase; Monilinia fructicola.

MeSH terms

  • Antifungal Agents / chemistry
  • Antifungal Agents / isolation & purification*
  • Antifungal Agents / pharmacology*
  • Ascomycota / drug effects
  • Ascomycota / growth & development
  • Bacillus subtilis / chemistry*
  • Bacillus subtilis / metabolism
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / isolation & purification*
  • Bacterial Proteins / pharmacology*
  • Chromatography, Ion Exchange
  • Electrophoresis, Polyacrylamide Gel
  • Glycoside Hydrolases / chemistry
  • Glycoside Hydrolases / isolation & purification*
  • Glycoside Hydrolases / pharmacology*
  • Molecular Weight

Substances

  • Antifungal Agents
  • Bacterial Proteins
  • Glycoside Hydrolases
  • chitosanase