02628nas 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-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-0