02287nas a2200217   4500008004100000022001400041245014000055210006900195260005700264300001400321490000700335520143100342653002201773653001201795653002401807653002801831653002701859100002501886700002601911856013201937       2007                        eng d  a0959-399300aProduction and partial characterization of two types of phytase from aspergillus niger NCIM 563 under submerged fermentation conditions0 aProduction and partial characterization of two types of phytase   a233 SPRING ST, NEW YORK, NY 10013 USAbSPRINGERcNOV  a1585-15930 v233 a<p>Novel extracellular phytase was produced by Aspergillus niger NCIM 563 under submerged fermentation conditions at 30 degrees C in medium containing dextrin and glucose as carbon sources along with sodium nitrate as nitrogen source. Maximum phytase activity (41.47 IU/mL at pH 2.5 and 10.71 IU/mL at pH 4.0) was obtained when dextrin was used as carbon source along with glucose and sodium nitrate as nitrogen source. Nearly 13 times increase in phytase activity was observed when phosphate in the form of KH2PO4 (0.004 g/100 mL) was added in the fermentation medium. Physic-chemical properties of partially purified enzyme indicate the possibility of two distinct forms of phytases, Phy I and Phy II. Optimum pH and temperature for Phy I was 2.5 and 60 degrees C while Phy II was 4.0 and 60 degrees C, respectively. Phy I was stable in the pH range 1.5-3.5 while Phy II was stable in the wider pH range, 2.0-7.0. Molecular weight of Phy I and Phy II on Sephacryl S-200 was approximately 304 kDa and 183 kDa, respectively. Phy I activity was moderately stimulated in the presence of 1 mM Mg2+, Mn2+, Ca2+ and Fe3+ ions and inhibited by Zn2+ and Cd2+ ions while Phy II activity was moderately stimulated by Fe3+ ions and was inhibited by Hg2+, Mn2+ and Zn2+ ions at 1 mM concentration in reaction mixture. The Km for Phy I and II was 3.18 and 0.514 mM while Vmax was 331.16 and 59.47 mu mols/min/mg protein, respectively.</p>10aAspergillus niger10aPhytase10aphytate degradation10aPoultry feed supplement10aSubmerged fermentation1 aSoni, Sarvesh, Kumar1 aKhire, Jayant, Malhar  uhttps://library.ncl.res.in/content/production-and-partial-characterization-two-types-phytase-aspergillus-niger-ncim-563-under-002337nas a2200253   4500008004100000022001400041245014600055210006900201260009400270300001400364490000600378520134000384653002401724653002201748653001201770653002401782653002801806653002701834100002401861700001601885700002501901700002601926856013101952       2008                        eng d  a1684-531500aInfluence of pretreatment of agriculture residues on phytase production by aspergillus niger NCIM 563 under submerged fermentation conditions0 aInfluence of pretreatment of agriculture residues on phytase pro  aP O BOX 5170-00200 NAIROBI, VICTORIA ISLAND, LAGOS 73023, NIGERIAbACADEMIC JOURNALScAPR  a1101-11060 v73 a<p>The extracellular phytase production by Aspergillus niger NCIM 563 was evaluated in medium containing various agriculture residues under submerged fermentation conditions. Phytase production was affected by inorganic phosphate content of agriculture residues which ranged from 2.8 to 8 mg/g. The agriculture residues containing less than 4 mg/g inorganic phosphate supported phytase production with maximum activity of 68 IU/ml in medium containing 1% rice bran on 11(th) day of fermentation. Addition of glucose up to 5% in fermentation medium containing 1% rice bran, enhanced phytase production. Pretreatment of agriculture residues with water to remove excess inorganic phosphate has significantly enhanced the phytase activity in case of de-oiled rice bran, wheat bran, peanut cake (low and high oil) and coconut cake. Maximum increase of 20.3 times in phytase activity was observed in case of wheat bran as compared to de-oiled rice bran, coconut cake, peanut cake high and low oil in which the increase in phytase activity was 6.85, 6.1, 5.3 and 3.0 times, respectively. Maximum phytase activity of 68 IU/ml was produced on the 11(th) day of fermentation compared to earlier reported 41.47 IU/ml phytase activity on the 15(th) day of submerged fermentation using 5% dextrin and 2.5% glucose, thus increasing productivity.</p>10aAgriculture residue10aAspergillus niger10aPhytase10aphytate degradation10aPoultry feed supplement10aSubmerged fermentation1 aBhavsar, Kavita, P.1 aShah, Parin1 aSoni, Sarvesh, Kumar1 aKhire, Jayant, Malhar  uhttps://library.ncl.res.in/content/influence-pretreatment-agriculture-residues-phytase-production-aspergillus-niger-ncim-563-002504nas a2200253   4500008004100000022001400041245013000055210006900185260008000254300001200334490000700346520155600353653002401909653002201933653001201955653002401967653002801991653002702019100001302046700002402059700001702083700002602100856012402126       2009                        eng d  a1367-543500aStrain improvement and up scaling of phytase production by aspergillus niger NCIM 563 under submerged fermentation conditions0 aStrain improvement and up scaling of phytase production by asper  aTIERGARTENSTRASSE 17, D-69121 HEIDELBERG, GERMANYbSPRINGER HEIDELBERGcMAR  a373-3800 v363 a<p>Combination of physical and chemical mutagenesis was used to isolate hyper secretory strains of Aspergillus niger NCIM 563 for phytase production. Phytase activity of mutant N-1 and N-79 was about 17 and 47% higher than the parent strain. In shake flask the productivity of phytase in parent, mutant N-1 and N-79 was 6,181, 7,619 and 9,523 IU/L per day, respectively. Up scaling of the fermentation from shake flask to 3 and 14 L New Brunswick fermenter was studied. After optimizing various fermentation parameters like aeration, agitation and carbon source in fermentation medium the fermentation time to achieve highest phytase activity was reduced considerably from 14 days in shake flask to 8 days in 14 L fermenter. Highest phytase activity of 80 IU/ml was obtained in 1% rice bran-3.5% glucose containing medium with aeration 0.2 vvm and agitation 550 rpm at room temperature on 8th day of fermentation. Addition of either bavistin (0.1%), penicillin (0.1%), formalin (0.2%) and sodium chloride (10%) in fermented broth were effective in retaining 100% phytase activity for 8 days at room temperature while these reagents along with methanol (50%) and ethanol (50%) confer 100% stability of phytase activity at 4A degrees C till 20 days. Among various carriers used for application of phytase in feed, wheat bran and rice bran were superior to silica and calcium carbonate. Thermo stabilization studies indicate 100% protection of phytase activity in presence of 12% skim milk at 70A degrees C, which will be useful for its spray drying.</p>10aAgriculture residue10aAspergillus niger10aPhytase10aphytate degradation10aPoultry feed supplement10aSubmerged fermentation1 aShah, P.1 aBhavsar, Kavita, P.1 aSoni, S., K.1 aKhire, Jayant, Malhar  uhttps://library.ncl.res.in/content/strain-improvement-and-scaling-phytase-production-aspergillus-niger-ncim-563-under-002418nas a2200229   4500008004100000022001400041245012600055210006900181260005700250300001400307490000700321520159900328653002201927653001201949653001201961653001701973653001701990100001702007700001502024700002602039856012302065       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  uhttps://library.ncl.res.in/content/purification-and-characterization-two-distinct-acidic-phytases-broad-ph-stability-002628nas a2200229   4500008004100000022001400041245016400055210006900219260008000288300001400368490000700382520169500389653002202084653001202106653003402118653002902152653002402181100002402205700001602229700002602245856012702271       2011                        eng d  a1367-543500aHigh level phytase production by aspergillus niger NCIM 563 in solid state culture: response surface optimization, up-scaling, and its partial characterization0 aHigh level phytase production by aspergillus niger NCIM 563 in s  aTIERGARTENSTRASSE 17, D-69121 HEIDELBERG, GERMANYbSPRINGER HEIDELBERGcSEP  a1407-14170 v383 a<p>Phytase production by Aspergillus niger NCIM 563 was optimized by using wheat bran in solid state fermentation (SSF). An integrated statistical optimization approach involving the combination of Placket-Burman design (PBD) and Box-Behnken design (BBD) was employed. PBD was used to evaluate the effect of 11 variables related to phytase production, and five statistically significant variables, namely, glucose, dextrin, NaNO(3), distilled water, and MgSO(4)center dot 7H(2)O, were selected for further optimization studies. The levels of five variables for maximum phytase production were determined by a BBD. Phytase production improved from 50 IU/g dry moldy bran (DMB) to 154 IU/g DMB indicating 3.08-fold increase after optimization. A simultaneous reduction in fermentation time from 7 to 4 days shows a high productivity of 38,500 IU/kg/day. Scaling up the process in trays gave reproducible phytase production overcoming industrial constraints of practicability and economics. The culture extract also had 133.2, 41.58, and 310.34 IU/g DMB of xylanase, cellulase, and amylase activities, respectively. The partially purified phytase was optimally active at 55A degrees C and pH 6.0. The enzyme retained ca. 75% activity over a wide pH range 2.0-9.5. It also released more inorganic phosphorus from soybean meal in a broad pH range from 2.5 to 6.5 under emulated gastric conditions. Molecular weight of phytase on Sephacryl S-200 was approximately 87 kDa. The K (m) and V (max) observed were 0.156 mM and 220 mu m/min/mg. The SSF phytase from A. niger NCIM 563 offers an economical production capability and its wide pH stability shows its suitability for use in poultry feed.</p>10aAspergillus niger10aPhytase10aResponse surface optimization10aSolid state fermentation10aStatistical methods1 aBhavsar, Kavita, P.1 aKumar, Ravi1 aKhire, Jayant, Malhar  uhttps://library.ncl.res.in/content/high-level-phytase-production-aspergillus-niger-ncim-563-solid-state-culture-response-002146nas a2200229   4500008004100000022001400041245018200055210006900237260009900306300001400405490000700419520119100426653002201617653002901639653001201668653002401680653001701704100002401721700001601745700002601761856012901787       2012                        eng d  a1359-511300aDownstream processing of extracellular phytase from aspergillus niger: chromatography process vs. aqueous two phase extraction for its simultaneous partitioning and purification0 aDownstream processing of extracellular phytase from aspergillus   aTHE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, OXON, ENGLANDbELSEVIER SCI LTDcJUL  a1066-10720 v473 a<p>The application of single step aqueous two-phase extraction (ATPE) for the downstream processing of phytase from Aspergillus niger NCIM 563, produced under solid state fermentation, has been studied and compared with the traditional multi-step procedure involving salt precipitation and column chromatography. High phytase recovery (98.5%) within a short time (3 h) and improved thermostability was attained by ATPE in comparison to 20% recovery in 96 h by chromatography process.The ATPE method, therefore, seems to be an interesting alternative for simultaneous partitioning and purification of phytase. The influence of system parameters; such as, phase forming salts, polymer molecular weight and system pH on the partitioning behavior of phytase was evaluated. The ATPE system consisting of combination of polyethylene glycol (PEG) 6000 and 8000(10.5%) and sodium citrate (20.5%) resulted in one-sided partitioning of phytase in bottom phase with a purification factor of 2.5. This is the first report on phytase purification using liquid-liquid extraction and the results are likely to be beneficial in the poultry feed industry. (c) 2012 Elsevier Ltd. All rights reserved.</p>10aAspergillus niger10aliquid-liquid extraction10aPhytase10aPolyethylene glycol10aPurification1 aBhavsar, Kavita, P.1 aKumar, Ravi1 aKhire, Jayant, Malhar  uhttps://library.ncl.res.in/content/downstream-processing-extracellular-phytase-aspergillus-niger-chromatography-process-vs-002605nas a2200253   4500008004100000022001400041245018200055210006900237260005700306300001200363490000700375520164900382653001602031653002202047653001602069653001202085653002902097100002402126700001402150700001302164700001602177700002602193856013202219       2013                        eng d  a0175-759800aCombinatorial approach of statistical optimization and mutagenesis for improved production of acidic phytase by Aspergillus niger NCIM 563 under submerged fermentation condition0 aCombinatorial approach of statistical optimization and mutagenes  a233 SPRING ST, NEW YORK, NY 10013 USAbSPRINGERcJAN  a673-6790 v973 a<p>Combination of statistical optimization and mutagenesis to isolate hypersecretory strains is studied to maximize phytase production from Aspergillus niger NCIM 563 under submerged fermentation. The overall results obtained show a remarkable 5.98-fold improvement in phytase production rates when compared to that using basal medium. Optimization of culture conditions from parent strain is studied first by the Plackett-Burman technique to evaluate the effects of 11 variables for phytase production. The results showed that glucose, MgSO4, KCl, incubation period, and MnSO4 are the most significant variables affecting enzyme production. Further optimization in these variables, using a central composite design technique, resulted in 3.74-fold increase in the yield of phytase production to 254,500 U/l when compared with the activity observed with basal media (68,000 U/l) in shake flask. Our experiments show that the phytase from A. niger NCIM 563 exhibits desirable activity in simulated gastric fluid conditions with low pH and also improved thermostability when compared to commercial phytase. The improved yield demonstrates the potential applicability of phytase enzyme as a source of phytase supplement for phosphorus nutrition and environmental protection in animal feed industry. Physical and chemical mutagenesis experiments were carried out in parallel to isolate hypersecretory mutants that could possibly further enhance the enzyme production. Using optimized media conditions of the parent strain, our results show that mutant strain A. niger NCIM 1359 increased the phytase activity by another 1.6-fold to 407,200 U/l.</p>10aAnimal feed10aAspergillus niger10aMutagenesis10aPhytase10aStatistical optimization1 aBhavsar, Kavita, P.1 aGujar, P.1 aShah, P.1 aKumar, Ravi1 aKhire, Jayant, Malhar  uhttps://library.ncl.res.in/content/combinatorial-approach-statistical-optimization-and-mutagenesis-improved-production-acidic-0