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Fungal Biotransformation of a β-Lactam Antibiotic Ampicillin under Laccase-Induced Conditions

Preprints.org 2024 4 citations ? Citation count from OpenAlex, updated daily. May differ slightly from the publisher's own count. Score: 45 ? 0–100 AI score estimating relevance to the microplastics field. Papers below 30 are filtered from public browse.
Bouthaina Ghariani, Bouthaina Ghariani, Abdulrahman H. Alessa, Imen Ben Atitallah, Ibtihel Louati, Ibtihel Louati, Ahmad A. Alsaigh, Tahar Mechichi, Héla Zouari-Mechichi

Summary

Researchers studied how the white-rot fungus Coriolopsis gallica biotransforms the antibiotic ampicillin under laccase-induced conditions, identifying degradation pathways and transformation products that may reduce the drug's persistence and ecotoxicity in aquatic environments.

The over use of pharmaceutical compounds, essentially antibiotics, led to an increase of their concentrations in aquatic ecosystems. In this study, the white-rot fungus Coriolopsis gallica (high-laccase-producing fungus) was investigated for the biodegradation of ampicillin (AMP) under different cultivation conditions. The biotransformation of the antibiotic was confirmed by means of high-performance liquid chromatography (HPLC), and the antibacterial activity was evaluated via the bacterial growth inhibition agar well diffusion method using Escherichia coli as an ampicillin-sensitive test strain. The results showed that AMP (50 mg L-1) was totally removed by C. gallica after 6 days of incubation in a liquid medium. The antibiotic removal rate was maximal with a fungal culture aged 9 days. Such a culture achieved the removal of a higher concentration of up to 500 mg L-1 of ampicillin in 3 days. This higher antibiotic removal rate was concomitant with the maximal laccase production in culture supernatant. In addition, four consecutive doses of 500 mg L-1 of ampicillin were transformed by the same fungal culture in 24 days. After that, the fungus was unable to remove the antibiotic. The measurement of ligninolytic enzyme activity showed that laccase of C. gallica might participate in the biotransformation of AMP.

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