@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}
}
@article {47778,
	title = {Performance of Aspergillus niger (NCIM 563) phytase based feed supplement for broiler growth and phosphorus excretion},
	journal = {Biocatalysis and Agricultural Biotechnology},
	volume = {31},
	year = {2021},
	month = {JAN},
	pages = {101887},
	type = {Article},
	abstract = {Despite availability of commercial enzymes, the phytase produced from relatively inexpensive systems with high yields are gaining global attention in the feed industries in post-antibiotic era. We studied A. niger NCIM 563 Phytase produced in solid state fermentation (SSF) derived Koji powder and evaluated its utility in the poultry feed for broiler growth performance and phosphorous (P) excretion. The ability of phytase in the dried powder was estimated to dephytinize the poultry feed under simulated gastric conditions. Poultry feed was formulated using A. niger NCIM 563 phytase followed by a 42 days feed trial on broilers. After supplementation of phytase to the diet, there was a reduction of dietary P, maintained growth performance, skeletal development of broilers and reduced levels of phytic acid and available P in the litter. Extracellular phytase was able to replace up to 0.1\% P in poultry feed. Minimal downstream processing a low-cost feed supplement with significant phytase activity could provide added advantage for anti-nutrition free poultry feed.},
	keywords = {Phosphorus, Phytase, Poultry feed, Solid state fermentation},
	isbn = {1878-8181},
	doi = {10.1016/j.bcab.2020.101887},
	url = {https://www.sciencedirect.com/science/article/pii/S1878818120319186},
	author = {Puppala, Kumar Raja and Buddhiwant, Priyanka G. and Agawane, Sachin B. and Kadam, Avinash S. and Mote, Chandrashekhar S. and Lonkar, Vijaysinh D. and Khire, Jayant M. and Dharne, Mahesh S.}
}
