@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:000302770700013,
	title = {Characterization of smallest active monomeric lipase from novel rhizopus strain: application in transesterification},
	journal = {Applied Biochemistry and Biotechnology},
	volume = {166},
	number = {7},
	year = {2012},
	month = {APR},
	pages = {1769-1780},
	publisher = {HUMANA PRESS INC},
	address = {999 RIVERVIEW DRIVE SUITE 208, TOTOWA, NJ 07512 USA},
	abstract = {<p>An extracellular lipase-producing fungus was isolated from oil-rich soil. This fungus belongs to the genus Rhizopus and clades with Rhizopus oryzae. Lipase was purified to homogeneity from this novel fungal source using ammonium sulphate precipitation followed by Q-Sepharose chromatography. The extracellular lipase was purified 8.6-fold, and enzymatic properties were studied. The molecular mass of the purified enzyme was estimated to be 17 kD by sodium dodecyl sulphate-polyacrylamide gel electrophoresis and 16.25 kD by matrix-assisted laser desorption ionization/time-of-flight analysis. The native molecular mass was estimated to be 17.5 kD by gel filtration, indicating the protein to be monomer. The optimum pH and temperature for the enzyme catalysis were 7.0 A degrees C and 40 A degrees C, respectively. Enzyme was stable in pH range 6.0-7.0 and retains 95-100\% activity when incubated at 50 A degrees C for 1 h. The pI of the purified lipase was 4.2. Enzyme was stable in the organic solvents such as ethanol, hexane and methanol for 2 h. Purified enzyme was used for transesterification of oleic acid in the presence of ethanol for production of oleic acid ethyl ester with a conversion efficiency of 66\% after 24 h at 30 A degrees C.</p>},
	keywords = {Lipase, Low molecular weight, Purification, Rhizopus, transesterification},
	issn = {0273-2289},
	doi = {10.1007/s12010-012-9584-0},
	author = {Kantak, Jayshree B. and Prabhune, Asmita}
}
