@article { ISI:000334485400001,
	title = {New role for penicillin acylases: degradation of acyl homoserine lactone quorum sensing signals by Kluyvera citrophila penicillin G acylase},
	journal = {Enzyme and Microbial Technology },
	volume = {56},
	year = {2014},
	month = {MAR},
	pages = {1-7},
	publisher = {ELSEVIER SCIENCE INC},
	type = {Article},
	address = {360 PARK AVE SOUTH, NEW YORK, NY 10010-1710 USA},
	abstract = {<p>Use of penicillin acylases for the production of semi-synthetic penicillins is well-known. Escherichia coli penicillin G acylase (EcPGA) has been extensively used for this purpose; however, Kluyvera citrophila penicillin G acylase (KcPGA) is assumed to be a better substitute, owing to its increased resilience to extreme pH conditions and ease of immobilization. In the present article we report a new dimension for the amidase activity of KcPGA by demonstrating its ability to cleave bacterial quorum sensing signal molecules, acyl homoserine lactones (AHL) with acyl chain length of 6-8 with or without oxo-substitution at third carbon position. Initial evidence of AHL degrading capability of KcPGA was obtained using CV026 based bioassay method. Kinetic studies performed at pH 8.0 and 50 degrees C revealed 3-oxo-C6 HSL to be the best substrate for the enzyme with V-max and K-m values of 21.37+0.85 mM/h/mg of protein and 0.1+0.01 mM, respectively. C6 HSL was found to be the second best substrate with V-max. and K-m value of 10.06+0.27 mM/h/mg of protein and 0.28+0.02 mM, respectively. Molecular modeling and docking studies performed on the active site of the enzyme support these findings by showing the fitting of AHLs perfectly within the hydrophobic pocket of the enzyme active site. (c) 2013 Elsevier Inc. All rights reserved.</p>},
	keywords = {Acyl homoserine lactones, CV026, KcPGA, Quorum quenching},
	issn = {0141-0229},
	doi = {10.1016/j.enzmictec.2013.12.010},
	author = {Mukherji, Ruchira and Varshney, Nishant Kumar and Panigrahi, Priyabrata and Suresh, C. G. and Prabhune, Asmita}
}
@article { ISI:000354991500013,
	title = {Possible correlation between bile salt hydrolysis and ahl deamidation: staphylococcus epidermidis RM1, a potent quorum quencher and bile salt hydrolase producer},
	journal = {Applied Biochemistry and Biotechnology},
	volume = {176},
	number = {1},
	year = {2015},
	month = {MAY},
	pages = {140-150},
	publisher = {HUMANA PRESS INC},
	address = {999 RIVERVIEW DRIVE SUITE 208, TOTOWA, NJ 07512 USA},
	abstract = {<p>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.</p>},
	keywords = {AHL acylase, Bile salt hydrolase, CV026, Quorum quenching, Staphylococcus epidermidis},
	issn = {0273-2289},
	doi = {10.1007/s12010-015-1563-9},
	author = {Mukherji, Ruchira and Prabhune, Asmita}
}
