02093nas a2200169   4500008004100000245016100041210006900202260000800271300001200279490000700291520141100298100002501709700002001734700001601754700002201770856013101792       2016                        eng d00aPhytase production by solid-state fermentation of groundnut oil cake by Aspergillus niger: A bioprocess optimization study for animal feedstock applications0 aPhytase production by solidstate fermentation of groundnut oil c  cJUL  a531-5380 v463 aThis investigation deals with the use of agro-industrial waste, namely groundnut oil cake (GOC), for phytase production by the fungi Aspergillus niger NCIM 563. Plackett-Burman design (PBD) was used to evaluate the effect of 11 process variables and studies here showed that phytase production was significantly influenced by glucose, dextrin, distilled water, and MgSO4 center dot 7H(2)O. The use of response surface methodology (RSM) by Box-Behnken design (BBD) of experiments further enhanced the production by a remarkable 36.67-fold from the original finding of 15 IU/gds (grams of dry substrate) to 550 IU/gds. This is the highest solid-state fermentation (SSF) phytase production reported when compared to other microorganisms and in fact betters the best known by a factor of 2. Experiments carried out using dried fermented koji for phosphorus and mineral release and also thermal stability have shown the phytase to be as efficient as the liquid enzyme extract. Also, the enzyme, while exhibiting optimal activity under acidic conditions, was found to have significant activity in a broad range of pH values (1.5-6.5). The studies suggest the suitability of the koji supplemented with phytase produced in an SSF process by the "generally regarded as safe" (GRAS) microorganism A. niger as a cost-effective value-added livestock feed when compared to that obtained by submerged fermentation (SmF).1 aBuddhiwant, Priyanka1 aBhavsar, Kavita1 aKumar, Ravi1 aKhire, Jayant, M.  uhttps://library.ncl.res.in/content/phytase-production-solid-state-fermentation-groundnut-oil-cake-aspergillus-niger-bioprocess02274nas a2200169   4500008004100000245011600041210006900157260000800226300002300234490000600257520163200263100002001895700001601915700002301931700002201954856012801976       2017                        eng d00aPhytase production by aspergillus niger NCIM 563 for a novel application to degrade organophosphorus pesticides0 aPhytase production by aspergillus niger NCIM 563 for a novel app  cMAR  aArticle Number: 660 v73 aThe production of phytase using Aspergillus niger NCIM 563 under submerged fermentation conditions was studied using protein rich chickpea flour as substrate. Employing a hybrid statistical media optimization strategy of Plackett-Burman and Box-Behnken experimental designs in shake-flasks gave an increased phytase activity from an initial 66 IU/mL in 216 h to 160 IU/mL in a reduced time of 132 h. Productivity, thus increased by 3.97 times from 7.3 to 29 IU/mL/day. Using the optimized media, the production was successfully scaled-up further and improved up to 164 IU/mL in 96 h by studies carried out employing 2 and 10-L fermenters. The enzyme supernatant was recovered using centrifugal separation of biomass and the stability of the produced phytase was tested for animal feed applications under gastric conditions. In vitro degradation studies of water soluble monocrotophos, methyl parathion and water insoluble chlorpyrifos, pesticides used extensively in agriculture was carried out. It was observed by HPLC analysis that phytase could degrade 72% of chlorpyrifos at pH 7.0, 35 degrees C. Comparable results were obtained with monocrotophos and methyl parathion. With chlorpyrifos at higher temperature 50 degrees C as much as 91% degradation could be obtained. The degradation of chlorpyrifos was further validated by spraying phytase on harvested green chilli ( Capsicum annuum L) under normal conditions of pH 7.0, 35 degrees C and the degradation products obtained analyzed by LCMS. Thus, the present study brings out a potentially novel application of phytase for biodegradation of organophosphorus pesticides.1 aShah, Parin, C.1 aKumar, Ravi1 aDastager, Syed, G.1 aKhire, Jayant, M.  uhttps://library.ncl.res.in/content/phytase-production-aspergillus-niger-ncim-563-novel-application-degrade-organophosphorus00543nas a2200157   4500008004100000022001400041245007700055210006900132260000800201300000700209490000700216100002200223700001600245700001600261856010800277       2022                        eng d  a0003-021X00aProcess optimization for biodiesel production using agro-waste substrate0 aProcess optimization for biodiesel production using agrowaste su  cOCT  a440 v991 aRaviKumar, Ameeta1 aBed, Rashmi1 aKumar, Ravi  uhttps://library.ncl.res.in/content/process-optimization-biodiesel-production-using-agro-waste-substrate02156nas a2200229   4500008004100000022001400041245010800055210006900163260000900232300000700241490000700248520134100255653002701596653001701623653003401640653003301674653002401707100002601731700001601757700002401773856012901797       2023                        eng d  a2191-085500aPotential of Y. lipolytica epoxide hydrolase for efficient production of enantiopure (R)-1,2-octanediol0 aPotential of Y lipolytica epoxide hydrolase for efficient produc  cJUL   a770 v133 a<p>
	The recombinant Yleh from a tropical marine yeast Yarrowia lipolytica NCIM 3589 exhibited a high epoxide hydrolase activity of 9.34 +/- 1.80 mu mol min(-1) mg(-1) protein towards 1,2-epoxyoctane (EO), at pH 8.0 and 30 degrees C. The reaction product was identified as 1,2-Octanediol (OD) by GC-MS using EO and H2O18 as substrate, affirming the functionality of Yleh as an epoxide hydrolase. For EO, the K-m, V-max, and k(cat)/K-m values were 0.43 +/- 0.017 mM, 0.042 +/- 0.003 mM min(-1), and 467.17 +/- 39.43 mM(-1) min(-1), respectively. To optimize the reaction conditions for conversion of racemic EO by Yleh catalyst to enantiopure (R)-1,2-octanediol, initially, Response Surface Methodology was employed. Under optimized reaction conditions of 15 mM EO, 150 mu g purified Yleh at 30 degrees C a maximal diol production of 7.11 mM was attained in a short span of 65 min with a yield of 47.4%. Green technology using deep eutectic solvents for the hydrophobic substrate (EO) were tested as co-solvents in Yleh catalyzed EO hydrolysis. Choline chloride-Glycerol, produced 9.08 mM OD with an increased OD yield of 60.5%. Thus, results showed that deep eutectic solvents could be a promising solvent for Yleh-catalyzed reactions making Yleh a potential biocatalyst for the biosynthesis of enantiopure synthons. [GRAPHICS] .</p>
10aDeep Eutectic solvents10aOptimization10aRecombinant epoxide hydrolase10aResponse surface methodology10aYarrowia lipolytica1 aGodase, Vijaya, P. P.1 aKumar, Ravi1 aKumar, Ameeta, Ravi  uhttps://library.ncl.res.in/content/potential-y-lipolytica-epoxide-hydrolase-efficient-production-enantiopure-r-12-octanediol