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Inactivation of virginiamycin by Aureobasidium pullulans.
Timothy D Leathers1, Joseph O Rich2, Melinda S Nunnally2
1Renewable Product Technology Research Unit, Agricultural Research Service, US Department of Agriculture, National Center for Agricultural Utilization Research, 1815 North University Street, Peoria, IL, 61604, USA. Tim.Leathers@ars.usda.gov.
Biotechnology Letters
|October 18, 2017
Summary
Aureobasidium pullulans, a fungus, can break down the antibiotic virginiamycin using its laccase enzyme. This finding shows potential for bioremediation of contaminated animal feed.
Area of Science:
- Microbiology
- Enzymology
- Bioremediation
Background:
- Virginiamycin is an antibiotic used in animal feed.
- Contamination of animal feed with virginiamycin is a concern.
- Aureobasidium pullulans is a fungus known to produce enzymes like laccase.
Purpose of the Study:
- To investigate the ability of Aureobasidium pullulans to inactivate virginiamycin.
- To determine if laccase produced by A. pullulans is responsible for virginiamycin inactivation.
Main Methods:
- Screening of A. pullulans strains for laccase production.
- Comparing virginiamycin inactivation by laccase-induced supernatants from different A. pullulans clades.
- Utilizing High-Performance Liquid Chromatography (HPLC) to quantify virginiamycin degradation.
Main Results:
- Fourteen strains of A. pullulans from phylogenetic clade 7 were assessed for laccase activity.
- Laccase-induced supernatants from clade 7 strains demonstrated greater virginiamycin inactivation compared to clade 5 strains.
- Strain NRRL Y-2567 from clade 7 inactivated 6 µg/ml of virginiamycin within 24 hours at 50°C.
- HPLC analysis confirmed the degradation of virginiamycin by A. pullulans.
Conclusions:
- Aureobasidium pullulans possesses the capability to degrade virginiamycin.
- The fungus shows promise for the bioremediation of virginiamycin-contaminated materials.
- Potential applications include the treatment of distiller's dry grains with solubles (DDGS) in animal feed production.