@article { ISI:000282507400010,
	title = {Purification and characterization of two distinct acidic phytases with broad pH stability from aspergillus niger NCIM 563},
	journal = {World Journal of Microbiology \& Biotechnology},
	volume = {26},
	number = {11},
	year = {2010},
	month = {NOV},
	pages = {2009-2018},
	publisher = {SPRINGER},
	address = {233 SPRING ST, NEW YORK, NY 10013 USA},
	abstract = {<p>Aspergillus niger NCIM 563 produced two different extracellular phytases (Phy I and Phy II) under submerged fermentation conditions at 30A degrees C in medium containing dextrin-glucose-sodium nitrate-salts. Both the enzymes were purified to homogeneity using Rotavapor concentration, Phenyl-Sepharose column chromatography and Sephacryl S-200 gel filtration. The molecular mass of Phy I and II as determined by SDS-PAGE and gel filtration were 66, 264, 150 and 148 kDa respectively, indicating that Phy I consists of four identical subunits and Phy II is a monomer. The pI values of Phy I and II were 3.55 and 3.91, respectively. Phy I was highly acidic with optimum pH of 2.5 and was stable over a broad pH range (1.5-9.0) while Phy II showed a pH optimum of 5.0 with stability in the range of pH 3.5-9.0. Phy I exhibited very broad substrate specificity while Phy II was more specific for sodium phytate. Similarly Phy II was strongly inhibited by Ag(+), Hg(2+) (1 mM) metal ions and Phy I was partially inhibited. Peptide analysis by Mass Spectrometry (MS) MALDI-TOF also indicated that both the proteins were totally different. The K (m) for Phy I and II for sodium phytate was 2.01 and 0.145 mM while V (max) was 5,018 and 1,671 mu mol min(-1) mg(-1), respectively. The N-terminal amino acid sequences of Phy I and Phy II were FSYGAAIPQQ and GVDERFPYTG, respectively. Phy II showed no homology with Phy I and any other known phytases from the literature suggesting its unique nature. This, according to us, is the first report of two distinct novel phytases from Aspergillus niger.</p>},
	keywords = {Aspergillus niger, Phytase, Phytate, Poultry feed, Purification},
	issn = {0959-3993},
	doi = {10.1007/s11274-010-0385-8},
	author = {Soni, S. K. and Magdum, A. and Khire, Jayant Malhar}
}
