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Updated: Jan 29, 2026

Analysis of Yersinia enterocolitica Effector Translocation into Host Cells Using Beta-lactamase Effector Fusions
Published on: October 13, 2015
Exploring antibiotic degradation mechanisms: Molecular docking analysis of beta-lactamase enzymes from Pseudomonas
Pratibha T1, Subash Vetri Selvi2, Uyen Khanh Pham3
1Department of Biotechnology, School of Life Sciences, Vels Institute of Science, Technology and Advanced Studies (VISTAS), Pallavaram, Chennai - 600 117, India.
Abstract:
This study investigates the potential of Pseudomonas songnenensis (P. songnenensis) in degrading β-lactam antibiotics through enzymatic hydrolysis by β-lactamase. Faecal soil samples were collected from ten poultry farms in Tamil Nadu, India, between June and July 2023. Each farm houses 10,000-50,000 birds and routinely administers antibiotics. Among the bacterial isolates obtained, strain 18 showed the highest degradation activity. Molecular docking analysis revealed stable enzyme-antibiotic interactions, with Amoxicillin showing the strongest binding affinity due to multiple hydrogen bonds. The β-lactamase enzyme effectively hydrolyses the β-lactam ring, breaking the amide bond and rendering antibiotics inactive. This stepwise degradation mechanism contributes to reducing antibiotic persistence in the environment and offers insights into microbial-driven bioremediation strategies. The findings highlight the novelty of using P. songnenensis for antibiotic degradation and emphasise its potential application in mitigating antibiotic pollution in livestock farming and food production systems.
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