02417nas a2200229   4500008004100000022001400041245012600055210006900181260005700250300001400307490000700321520159900328653002201927653001201949653001201961653001701973653001701990100001702007700001502024700002602039856012202065       2010                        eng d  a0959-399300aPurification and characterization of two distinct acidic phytases with broad pH stability from aspergillus niger NCIM 5630 aPurification and characterization of two distinct acidic phytase  a233 SPRING ST, NEW YORK, NY 10013 USAbSPRINGERcNOV  a2009-20180 v263 a<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>10aAspergillus niger10aPhytase10aPhytate10aPoultry feed10aPurification1 aSoni, S., K.1 aMagdum, A.1 aKhire, Jayant, Malhar  uhttp://library.ncl.res.in/content/purification-and-characterization-two-distinct-acidic-phytases-broad-ph-stability-001975nas a2200277   4500008004100000020001400041245012200055210006900177260000800246300001100254490000700265520107900272653001501351653001201366653001701378653002901395100002501424700002901449700002401478700002301502700002901525700002601554700002201580700002301602856007201625       2021                        eng d  a1878-818100aPerformance of Aspergillus niger (NCIM 563) phytase based feed supplement for broiler growth and phosphorus excretion0 aPerformance of Aspergillus niger NCIM 563 phytase based feed sup  cJAN  a1018870 v313 aDespite 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.10aPhosphorus10aPhytase10aPoultry feed10aSolid state fermentation1 aPuppala, Kumar, Raja1 aBuddhiwant, Priyanka, G.1 aAgawane, Sachin, B.1 aKadam, Avinash, S.1 aMote, Chandrashekhar, S.1 aLonkar, Vijaysinh, D.1 aKhire, Jayant, M.1 aDharne, Mahesh, S.  uhttps://www.sciencedirect.com/science/article/pii/S1878818120319186