@article { ISI:000271494300030, title = {Cellulases from penicillium janthinellum mutants: solid-state production and their stability in ionic liquids}, journal = {Bioresources}, volume = {4}, number = {4}, year = {2009}, month = {AUG}, pages = {1670-1681}, publisher = {NORTH CAROLINA STATE UNIV DEPT WOOD \& PAPER SCI}, address = {CAMPUS BOX 8005, RALEIGH, NC 27695-8005 USA}, abstract = {

The cellulase production by P. janthinellum mutants on lignocellulosic material such as cellulose or steam exploded bagasse (SEB) in combination with wheat bran was studied in solid state fermentation (SSF). One of the mutants, EU2D21, produced the highest levels of endoglucanase (3710 IU g(-1) carbon source) and beta-glucosidase (155 IU g(-1) carbon source). Ionic liquids are so-called green solvents that have become attractive for biocatalysis. Stability of mutant cellulases was tested in 10-50\% of the ionic liquid 1-butyl-3-methylimidazolium chloride ([bmim]Cl). FPA and CMCase were significantly stable in 10\% ionic liquid after 5h. beta-glucosidase showed 85\% of its original activity after 5 h incubation in 30\% ionic liquid and retained 55\% of its activity after 24 h. This enzyme preparation hydrolyzed ionic-liquid-treated SEB completely in 15 h in the presence of 20\% ionic liquid. These studies revealed that there is no need of regenerating cellulose after ionic liquid treatment, since cellulase of mutant strain was found to be significantly stable in the ionic liquid.

}, keywords = {Cellulase stability, Ionic liquid, Mutant cellulase, Solid state fermentation}, issn = {1930-2126}, author = {Adsul, Mukund G. and Terwadkar, Asawari P. and Varma, Anjanikumar and Gokhale, Digambar V.} } @article { ISI:000291194800029, title = {Comparative production of cellulases by mutants of penicillium janthinellum NCIM 1171 and its application in hydrolysis of avicel and cellulose}, journal = {Bioresource Technology}, volume = {102}, number = {11}, year = {2011}, month = {JUN}, pages = {6569-6572}, publisher = {ELSEVIER SCI LTD}, address = {THE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, OXON, ENGLAND}, abstract = {

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.

}, keywords = {beta-Glucosidase thermostability, Mutant EU2D-21, Solid state fermentation, Submerged fermentation}, issn = {0960-8524}, doi = {10.1016/j.biortech.2011.01.014}, author = {Singhvi, M. S. and Adsul, Mukund G. and Gokhale, D. V.} } @article { ISI:000294225100030, title = {High level phytase production by aspergillus niger NCIM 563 in solid state culture: response surface optimization, up-scaling, and its partial characterization}, journal = {Journal of Industrial Microbiology \& Biotechnology}, volume = {38}, number = {9}, year = {2011}, month = {SEP}, pages = {1407-1417}, publisher = {SPRINGER HEIDELBERG}, address = {TIERGARTENSTRASSE 17, D-69121 HEIDELBERG, GERMANY}, abstract = {

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.

}, keywords = {Aspergillus niger, Phytase, Response surface optimization, Solid state fermentation, Statistical methods}, issn = {1367-5435}, doi = {10.1007/s10295-010-0926-z}, author = {Bhavsar, Kavita P. and Kumar, V. Ravi and Khire, Jayant Malhar} } @article { ISI:000327920600003, title = {Phytase isozymes from aspergillus niger NCIM 563 under solid state fermentation: biochemical characterization and their correlation with submerged phytases}, journal = {Process Biochemistry}, volume = {48}, number = {11}, year = {2013}, month = {NOV}, pages = {1618-1625}, publisher = {ELSEVIER SCI LTD}, address = {THE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, OXON, ENGLAND}, abstract = {

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.

}, keywords = {A. niger, Isozymes, Phytase, Solid state fermentation, Submerged fermentation}, issn = {1359-5113}, doi = {10.1016/j.procbio.2013.08.001}, author = {Bhavsar, Kavita P. and Buddhiwant, Priyanka and Soni, Sarvesh K. and Depan, Dilip and Sarkar, Sampa 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.} }