Purification and antibiofilm activity of ahl-lactonase from endophytic enterobacter aerogenes vt66

Rajesh, P. S. and Rai, V. R. (2015) Purification and antibiofilm activity of ahl-lactonase from endophytic enterobacter aerogenes vt66. International Journal of Biological Macromolecules, 81. pp. 1046-1052. ISSN 0141-8130

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Official URL: http://doi.org/0.1016/j.ijbiomac.2015.09.048

Abstract

The opportunistic pathogen Pseudomonas aeruginosa uses biofilm lifestyle to resist antibiotic treatment. In our study, endophytic bacterium Enterobacter aerogenes VT66 quenched the N-acyl homoserine lactone (AHL) molecules produced by P. aeruginosa PAO1. The quorum quenching activity was attributed to the presence of AHL-Iactonase. The AHL-Iactonase was purified using column chromatography and purified AHL-lactonase was applied for the control of biofilm formation in P. aeruginosa PAO1. The results showed that purified AHL-lactonase obtained with a molecular weight about 30kDa was able to inhibit more than 70% of biofilm in P. aeruginosa PAO1 (P<0.001). Antibiofilm activity of AHL-lactonase was correlated well with results from staining technique used to determine inhibition of biomass and viable cell activity. Therefore, results unambiguously confirm that the AHL-lactonase from E. aerogenes VT66 could be used as antibiofilm therapeutics in P. aeruginosa associated biomedical applications. (C) 2015 Elsevier B.V. All rights reserved.

Item Type: Article
Uncontrolled Keywords: Quorum quenching; AHL-Iactonase; Antibiofilm
Subjects: B Life Science > Microbiology
Divisions: Department of > Microbiology
Depositing User: Shrirekha N
Date Deposited: 29 May 2019 11:26
Last Modified: 17 Sep 2019 10:29
URI: http://eprints.uni-mysore.ac.in/id/eprint/651

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