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-001852nas a2200217   4500008004100000022001400041245014800055210006900203260009900272300001400371490000800385520094100393653003701334653001901371653002901390653002701419100002001446700002201466700002001488856012601508       2011                        eng d  a0960-852400aComparative production of cellulases by mutants of penicillium janthinellum NCIM 1171 and its application in hydrolysis of avicel and cellulose0 aComparative production of cellulases by mutants of penicillium j  aTHE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, OXON, ENGLANDbELSEVIER SCI LTDcJUN  a6569-65720 v1023 a<p>Mutants of Penicillium janthinellum NCIM 1171 were evaluated for cellulase production using both submerged fermentation (SmF) and solid state fermentation (SSF). Mutant EU2D-21 gave highest yields of cellulases in both SmF and SSF. Hydrolysis of Avicel and cellulose were compared using SmF and SSF derived enzyme preparations obtained from EU2D-21. Surprisingly, the use of SSF derived preparation gave less hydrolysis compared to SmF derived enzymes. This may be due to inactivation of beta-glucosidase at 50 degrees C in SSF derived enzyme preparations. SmF derived enzyme preparations contained both thermostable and thermosensitive beta-glucosidases where as SSF derived enzyme preparations contained predominantly thermosensitive beta-glucosidase. This is the first report on less thermostability of SSF derived p-glucosidase which is the main reason for getting less hydrolysis. (C) 2011 Elsevier Ltd. All rights reserved.</p>10abeta-Glucosidase thermostability10aMutant EU2D-2110aSolid state fermentation10aSubmerged fermentation1 aSinghvi, M., S.1 aAdsul, Mukund, G.1 aGokhale, D., V.  uhttps://library.ncl.res.in/content/comparative-production-cellulases-mutants-penicillium-janthinellum-ncim-1171-and-its-002293nas a2200265   4500008004100000022001400041245016000055210006900215260009900284300001400383490000700397520126900404653001301673653001301686653001201699653002901711653002701740100002401767700002501791700002201816700001701838700001801855700002601873856012801899       2013                        eng d  a1359-511300aPhytase isozymes from aspergillus niger NCIM 563 under solid state fermentation: biochemical characterization and their correlation with submerged phytases0 aPhytase isozymes from aspergillus niger NCIM 563 under solid sta  aTHE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, OXON, ENGLANDbELSEVIER SCI LTDcNOV  a1618-16250 v483 a<p>Aspergillus niger NCIM 563 produces dissimilar phytase isozymes under solid state and submerged fermentation conditions. Biochemical characterization and applications of phytase Phy III and Phy IV in SSF and their comparison with submerged fermentation Phy I and Phy III were studied. SSF phytases have a higher metabolic potential as compared to SmF. Phy I is tetramer and Phy II, III and IV are monomers. Phy I and IV have pH optima of 2.5 and Phy II and III have pH optima of 5.0 and 5.6, respectively. Phy I, III and IV exhibited very broad substrate specificity while Phy II was more specific for sodium phytate. SSF phytase is less thermostable as compared to SmF phytase. Phy land II show homology with other known phytases while Phy III and IV show no homology with SmF phytases and any other known phytases from the literature suggesting their unique nature. This is the first report about differences among phytase produced under SSF and SmF by A. niger and this study provides basis for explanation of the stability and catalytic differences observed for these enzymes. Exclusive biochemical characteristics and multilevel application of SSF native phytases determine their efficacy and is exceptional. (C) 2013 Elsevier Ltd. All rights reserved.</p>10aA. niger10aIsozymes10aPhytase10aSolid state fermentation10aSubmerged fermentation1 aBhavsar, Kavita, P.1 aBuddhiwant, Priyanka1 aSoni, Sarvesh, K.1 aDepan, Dilip1 aSarkar, Sampa1 aKhire, Jayant, Malhar  uhttps://library.ncl.res.in/content/phytase-isozymes-aspergillus-niger-ncim-563-under-solid-state-fermentation-biochemical-002841nas a2200241   4500008004100000022001400041245015000055210006900205260000800274300001200282490000700294520195200301653001402253653002802267653002802295653003302323653002702356653001302383100002502396700002302421700002302444856013202467       2024                        eng d  a0972-152500aBioprocess optimization of penicillium funiculosum NCIM 1228 for improved production and hydrolytic efficiency of cellulases on sugarcane bagasse0 aBioprocess optimization of penicillium funiculosum NCIM 1228 for  cFEB  a215-2330 v263 a<p>The cellulase enzyme is currently the world's third largest commercial enzyme. Because of its requirement in various industries like textiles, food, waste management, pharmaceuticals, agriculture, pulp paper, biofuels, and others, its demand curve has increased sharply. The response surface methodology (RSM) approach was employed to optimize media components and process parameters in the current investigation, which successfully increased the cellulase production from Penicillium funiculosum NCIM 1228. Statistical optimization for the hyperproduction of cellulases was conducted using RSM. The Plackett-Burman design (PBD) approach was used to investigate the critical factors of the cellulase production medium. Subsequently, the Box-Behnken design (BBD) method was used to statistically estimate optimum values and conditions that substantially impacted cellulase production. The estimated optimal combinations of parameters for cellulase production were urea (0.2%), CaCl2 (0.2%), MgSO4 (0.05%), peptone (1.5%), microcrystalline cellulose (5.0%), wheat bran (2.5%), corn steep liquor (CSL) (2.5%), KH2PO4 (0.15%), inoculum (10.65%), agitation (157 rpm), pH (5.88), and temperature (29.84 C-degrees). Conclusively, experimental validation under optimal conditions detected an increased production of 3.82- and 3.61-fold in filter paper assay (FPase) and beta-glucosidase, respectively. Additionally, 1.66- and 1.57-fold enhancement in FPase and beta-glucosidase specific activity was observed where an xylanase activity was enhanced by 3.29-fold. Furthermore, the enzyme showed 51.30 per cent hydrolysis efficiency on sugarcane bagasse lignocellulosic biomass (LCB), at a dose of 7 FPase units per g of cellulose. P. funiculosum NCIM 1228 offers the benefit of producing cellulase with an entire cellulolytic system of enzymes that can be synthesized extracellularly, thus acting as a promising biocatalyst for biofuel industries.</p>
10aCellulase10aLignocellulosic biomass10aPenicillium funiculosum10aResponse surface methodology10aSubmerged fermentation10aXylanase1 aChavan, Sambhaji, B.1 aShete, Ashvini, M.1 aDharne, Mahesh, S.  uhttps://library.ncl.res.in/content/bioprocess-optimization-penicillium-funiculosum-ncim-1228-improved-production-and-hydrolytic