@article { ISI:000307537300043,
	title = {Characterization of a new bacillus cereus ATUAVP1846 strain producing penicillin V acylase, and optimization of fermentation parameters},
	journal = {Annals of Microbiology},
	volume = {62},
	number = {3},
	year = {2012},
	month = {SEP},
	pages = {1287-1293},
	publisher = {SPRINGER},
	address = {233 SPRING ST, NEW YORK, NY 10013 USA},
	abstract = {<p>Penicillin acylases are involved chiefly in the industrial production of semisynthetic penicillins, which remain the most widely used group of antibiotics. We have isolated a new bacterial strain ATUAVP1846 that produces penicillin V acylase (PVA). Phylogenetic analysis using 16S rRNA sequencing showed 99.37\% homology with Bacillus cereus. Maximum PVA production was observed with B. cereus ATUAVP1846 at 30A degrees C, pH 7 after 24 h fermentation time under submerged conditions. Highest enzyme productivity was achieved using sucrose as carbon source, and tryptone and ammonium hydrogen phosphate as nitrogen sources. Minimal medium containing 0.4\% glucose and 0.3\% ammonium hydrogen phosphate was found to be optimal for maximum PVA production from B. cereus ATUAVP1846. The crude enzyme from B. cereus ATUAVP1846 was partially purified using ammonium sulfate fractionation and showed highest enzymatic activity in the hydrolysis of penicillin V at 40A degrees C and pH 6. The crude enzyme preparation also showed unique substrate specificity, preferring ampicillin and cephalexin over penicillin V.</p>},
	keywords = {16S rRNA, Bacillus cereus, isolation, Ntn hydrolase, Optimization, Penicillin acylase},
	issn = {1590-4261},
	doi = {10.1007/s13213-011-0374-7},
	author = {Sunder, Avinash Vellore and Kumar, Atul and Naik, Neha and Pundle, Archana V.}
}
@article {45766,
	title = {Penicillin V acylases from gram-negative bacteria degrade N-acylhomoserine lactones and attenuate virulence in Pseudomonas aeruginosa},
	journal = {Applied Microbiology and Biotechnology},
	volume = {101},
	year = {2017},
	month = {MAR},
	pages = {2383-2395},
	type = {Article},
	abstract = {<p>Virulence pathways in gram-negative pathogenic bacteria are regulated by quorum sensing mechanisms, through the production and sensing of N-acylhomoserine lactone (AHL) signal molecules. Enzymatic degradation of AHLs leading to attenuation of virulence (quorum quenching) could pave the way for the development of new antibacterials. Penicillin V acylases (PVAs) belong to the Ntn hydrolase superfamily, together with AHL acylases. PVAs are exploited widely in the pharmaceutical industry, but their role in the natural physiology of their native microbes is not clearly understood. This report details the characterization of AHL degradation activity by homotetrameric PVAs from two gram-negative plant pathogenic bacteria, Pectobacterium atrosepticum (PaPVA) and Agrobacterium tumefaciens (AtPVA). Both the PVAs exhibited substrate specificity for degrading long-chain AHLs. Exogenous addition of these enzymes into Pseudomonas aeruginosa greatly diminished the production of elastase and pyocyanin and biofilm formation and increased the survival rate in an insect model of acute infection. Subtle structural differences in the PVA active site that regulate specificity for acyl chain length have been characterized, which could reflect the evolution of AHL-degrading acylases in relation to the environment of the bacteria that produce them and also provide strategies for enzyme engineering. The potential for using these enzymes as therapeutic agents in clinical applications and a few ideas about their possible significance in microbial physiology have also been discussed.</p>},
	keywords = {N-acylhomoserine lactone acylase, Ntn hydrolase, pathogenesis, Penicillin Vacylase, Quorum quenching},
	issn = {0175-7598},
	doi = {10.1007/s00253-016-8031-5},
	author = {Sunder, Avinash Vellore and Utari, Putri Dwi and Ramasamy, Sureshkumar and van Merkerk, Ronald and Quax, Wim and Pundle, Archana}
}
