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Microbiological activity in stored olive oil.

G Ciafardini1, B A Zullo

  • 1Department of Animal, Plant, and Environmental Sciences, Agriculture Faculty, University of Molise, Campobasso, Italy. ciafardi@unimol.it

International Journal of Food Microbiology
|May 10, 2002
PubMed
Summary

Yeast beta-glucosidase enzymes from Saccharomyces cerevisiae and Candida wickerhamii can hydrolyze oleuropein, reducing bitterness in olive oil. This finding offers new insights into olive oil quality improvement during storage.

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Area of Science:

  • Food Science
  • Enzymology
  • Microbiology

Background:

  • Olive oil bitterness is primarily caused by the secoiridoid compound oleuropein.
  • Oleuropein hydrolysis, reducing bitterness, is traditionally attributed to olive-derived beta-glucosidase during storage.

Purpose of the Study:

  • To investigate the potential of yeast beta-glucosidase in hydrolyzing oleuropein in olive oil.
  • To determine if Saccharomyces cerevisiae and Candida wickerhamii possess beta-glucosidase activity capable of modifying oleuropein.

Main Methods:

  • Enzymatic analyses were performed directly on untreated and sterilized olive oil.
  • Olive oil was inoculated with Saccharomyces cerevisiae and Candida wickerhamii.
  • Beta-glucosidase activity was assessed using the synthetic substrate p-nitrophenyl-beta-D-glucopyranoside (PNPG) and oleuropein.

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Main Results:

  • Demonstrated that beta-glucosidase from Saccharomyces cerevisiae and Candida wickerhamii can effectively hydrolyze oleuropein in olive oil.
  • Confirmed beta-glucosidase activity by observing the hydrolysis of both PNPG and oleuropein.
  • Found no significant lipase activity in the isolated yeasts, indicating no alteration to triglyceride composition.

Conclusions:

  • Yeast beta-glucosidases, specifically from S. cerevisiae and C. wickerhamii, can contribute to the debittering of olive oil.
  • These yeasts offer a novel avenue for improving the organoleptic quality of olive oil without negatively impacting its fundamental triglyceride structure.