@article { ISI:000258819000009,
	title = {Characterization of smallest active monomeric penicillin V acylase from new source: a yeast, rhodotorula aurantiaca (NCIM 3425)},
	journal = {Process Biochemistry},
	volume = {43},
	number = {9},
	year = {2008},
	month = {SEP},
	pages = {961-967},
	publisher = {ELSEVIER SCI LTD},
	type = {Article},
	address = {THE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, OXON, ENGLAND},
	abstract = {<p>An intracellular monomeric penicillin V acylase (PVA) of 36,000 Da exhibiting pI of 4.19, purified from newly identified yeast source, Rhodotorula aurantiaca (NCIM 3425). The enzyme was purified by hydrophobic interaction chromatography. The enzyme showed optimal activity at 45 degrees C and retained 80\% activity after incubation at 45 degrees C and pH 5.5 for I h. The enzyme showed maximum activity at pH 5.5 and was very stable between pH 5.5-6.5 with optimum stability at pH 6.0. It exhibited 50\% of its original activity after 30 min incubation at 60 degrees C. Enzyme hydrolyzed substrates with benzyl side chain but preferred penicillin V as primary substrate. N-terminally located serine supports the fact that it belongs to Ntn (N-terminal nucleophile)-hydrolase superfamily. The initial ten amino acid residues of R. aurantiaca PVA were identical to the initial sequence of NADH dehydrogenase (EC 1.6.99.3): however the enzyme lacks dehydrogenase activity. EGTA, EDTA, hexane and ethyl acetate stabilized the activity where as small chain alcohols inhibited it. 1,4-Dioxane, THF (tetrahydrofurane), phenol and benzyl alcohol severely inhibited enzyme activity while BME and DTT increased it. Tween 80 and Tween 20 highly enhanced the activity where as SIDS and Triton X-100 inhibited it. (C) 2008 Elsevier Ltd. All rights reserved.</p>},
	keywords = {Intracellular enzyme, N-terminal sequencing, Penicillin V acylase, Purification, Rhodotorula aurantiaca, Substrate specificity},
	issn = {1359-5113},
	doi = {10.1016/j.procbio.2008.04.024},
	author = {Kumar, Atul and Prabhune, Asmita and Suresh, C. G. and Pundle, Archana}
}
@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.}
}
