Binding mechanism of patulin to heat-treated yeast cell

Lett Appl Microbiol. 2012 Dec;55(6):453-9. doi: 10.1111/j.1472-765x.2012.03314.x. Epub 2012 Oct 15.

Abstract

Aims: This study aims to assess the removal mechanism of patulin using heat-treated Saccharomyces cerevisiae cells and identify the role of different cell wall components in the binding process.

Methods and results: In order to understand the binding mechanism, viable cells, heat-treated cells, cell wall and intracellular extract were performed to assess their ability to remove patulin. Additionally, the effects of chemical and enzymatic treatments of yeast on the binding ability were tested. The results showed that there was no significant difference between viable (53·28%) and heat-treated yeast cells (51·71%) in patulin binding. In addition, the cell wall fraction decreased patulin by 35·05%, and the cell extract nearly failed to bind patulin. Treatments with protease E, methanol, formaldehyde, periodate or urea significantly decreased (P < 0·05) the ability of heat-treated cells to remove patulin. Fourier transform infrared (FTIR) analysis indicated that more functional groups were involved in the binding process of heat-treated cells.

Conclusions: Polysaccharides and protein are important components of yeast cell wall involved in patulin removal. In addition, hydrophobic interactions play a major role in binding processes.

Significance and impact of the study: Heat-treated S. cerevisiae cells could be used to control patulin contamination in the apple juice industry. Also, our results proof that the patulin removal process is based mainly on the adsorption not degradation.

Keywords: Saccharomyces cerevisiae; cell wall; patulin; polysaccharide; protein.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adsorption
  • Beverages*
  • Cell Wall / chemistry*
  • Decontamination / methods*
  • Formaldehyde / chemistry
  • Hot Temperature
  • Malus / chemistry*
  • Methanol / chemistry
  • Patulin / chemistry*
  • Periodic Acid / chemistry
  • Saccharomyces cerevisiae / metabolism*
  • Serine Endopeptidases / metabolism
  • Spectroscopy, Fourier Transform Infrared
  • Urea / chemistry

Substances

  • Periodic Acid
  • Formaldehyde
  • Urea
  • Patulin
  • metaperiodate
  • Serine Endopeptidases
  • protease E
  • Methanol