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Possible Correlation Between Bile Salt Hydrolysis and AHL Deamidation: Staphylococcus epidermidis RM1, a Potent Quorum Quencher and Bile Salt Hydrolase Producer

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Abstract

The aim of the present work was to isolate a bile salt hydrolase (BSH) producer from fermented soy curd and explore the ability of the BSH produced to cleave bacterial quorum sensing signals. Bacterial isolates with possible ability to deconjugate bile salts were enriched and isolated on De Man, Rogosa and Sharpe (MRS) medium containing 0.2 % bile salts. BSH-producing positive isolate with orange-pink-pigmented colonies was isolated and was identified as a strain of Staphylococcus epidermidis using biochemical and phylogenetic tools. S. epidermidis RM1 was shown to possess both potent BSH and N-acyl homoserine lactone (AHL) cleavage activity. Genetic basis of this dual-enzyme activity was explored by means of specific primers designed using S. epidermidis ATCC 12228 genome as template. It was observed that a single enzyme was not responsible for both the activity. Two different genetic elements corresponding to each of the enzymatic activity were successfully amplified from the genomic DNA of the isolate.

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Acknowledgments

RM wishes to thank the University Grants Commission for the  PhD fellowship.

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Authors declare no conflicts of interest.

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Authors and Affiliations

  1. Division of Biochemical Sciences, National Chemical Laboratory, Pune, 411008, India

    Ruchira Mukherji &  Asmita Prabhune

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  1. Ruchira Mukherji
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  2. Asmita Prabhune
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Correspondence to Asmita Prabhune.

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Ruchira Mukherji, holds an M.Sc degree from the University of Mumbai and is currently pursuing her doctoral studies in National Chemical Laboratory.

Asmita Prabhune holds a PhD degree, National Chemical Laboratory.

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Mukherji, R., Prabhune, A. Possible Correlation Between Bile Salt Hydrolysis and AHL Deamidation: Staphylococcus epidermidis RM1, a Potent Quorum Quencher and Bile Salt Hydrolase Producer. Appl Biochem Biotechnol 176, 140–150 (2015). https://doi.org/10.1007/s12010-015-1563-9

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  • DOI: https://doi.org/10.1007/s12010-015-1563-9

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