@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:000382535600016,
	title = {Purification and partial characterization of novel penicillin V acylase from Acinetobacter sp AP24 isolated from loktak lake, an indo-burma biodiversity hotspot},
	journal = {Preparative Biochemistry \& Biotechnology},
	volume = {46},
	number = {5},
	year = {2016},
	month = {OCT},
	pages = {524-530},
	publisher = {TAYLOR \& FRANCIS INC},
	address = {530 WALNUT STREET, STE 850, PHILADELPHIA, PA 19106 USA},
	abstract = {<p>Members of the bacterial genus Acinetobacter have attracted great attention over the past few decades, on account of their various biotechnological applications and clinical implications. In this study, we are reporting the first experimental penicillin V acylase (PVA) activity from this genus. Penicillin acylases are pharmaceutically important enzymes widely used in the synthesis of semisynthetic beta-lactam antibiotics. The bacterium, identified as Acinetobacter sp. AP24, was isolated from the water of Loktak Lake (Manipur, India), an Indo-Burma biodiversity hotspot. PVA production was increased threefold in an optimized medium with 0.2\% sodium glutamate and 1\% glucose as nitrogen and carbon sources respectively, after 24hr of fermentation at 28 degrees C and pH 7.0 with shaking at 180rpm. The enzyme was purified to homogeneity by cation-exchange chromatography using SP-sepharose resin. The PVA is a homotetramer with subunit molecular mass of 34 kD. The enzyme was highly specific toward penicillin V with optimal hydrolytic activity at 40 degrees C and pH 7.5. The enzyme was stable from pH 5.0 to 9.0 at 25 degrees C for 2hr. The enzyme retained 75\% activity after 1hr of incubation at 40 degrees C at pH 7.5.</p>},
	keywords = {6-APA, Acinetobacter, Loktak Lake, Penicillin V acylase},
	issn = {1082-6068},
	doi = {10.1080/10826068.2015.1084636},
	author = {Philem, Pushparani Devi and Sonalkar, Vidya V. and Dharne, Mahesh S. and Prabhune, Asmita}
}
