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
Full text not available from this repository. (Request a copy)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 |
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Uncontrolled Keywords: | Quorum quenching; AHL-Iactonase; Antibiofilm |
Subjects: | B Life Science > Microbiology |
Divisions: | Department of > Microbiology |
Depositing User: | Users 19 not found. |
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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