01692nas a2200193 4500008004100000022001400041245010400055210006900159260007100228300001400299490000700313520095300320100001801273700002401291700002301315700001901338700001401357856012701371 2006 eng d a8756-793800aPreparation and characterization of urea-formaldehyde-pepsin bioconjugate: a new biocatalyst system0 aPreparation and characterization of ureaformaldehydepepsin bioco a1155 16TH ST, NW, WASHINGTON, DC 20036 USAbAMER CHEMICAL SOCcDEC a1585-15900 v223 a

This study describes the synthesis of urea formaldehyde (UF) microspheres by a dispersion polycondensation polymerization method. These microspheres with proper F/U molar ratio can provide highly reactive groups, capable of further condensation with the amino acid residues of enzyme/proteins. Presence of methylols groups in UF microspheres was confirmed by C-13 NMR study. Pepsin, a proteolytic enzyme, was immobilized on the UF microspheres to form bioconjugate system. As compared to the free enzyme in solution, the pepsin in the bioconjugate system exhibited significantly enhanced pH and temperature stability. The urea-formaldehydepepsin bioconjugate system also exhibited excellent proteolytic activity over eight successive reuse cycles with more than 50% of initial activity. A highlight of this new biocatalyst is the ease with which separation of this biocatalyst from the reaction medium may be achieved by mild centrifugation.

1 aVinod, V., P.1 aShinde, Sudhirkumar1 aD'Britto, Virginia1 aShukla, P., G.1 aRao, Mala uhttp://library.ncl.res.in/content/preparation-and-characterization-urea-formaldehyde-pepsin-bioconjugate-new-biocatalyst-001498nas a2200205 4500008004100000022001400041245013100055210006900186260007300255300001200328490000700340520067200347653003401019653002801053653002701081100002101108700002501129700001401154856012401168 2008 eng d a0141-813000apH Induced structural alterations in an aspartic protease from Vigna radiata indicating an alkali induced molten globule state0 apH Induced structural alterations in an aspartic protease from V aPO BOX 211, 1000 AE AMSTERDAM, NETHERLANDSbELSEVIER SCIENCE BVcNOV a373-3760 v433 a

pH-dependent transitions in secondary and tertiary structure are described for a plant aspartic protease from Vigna radiata. The enzyme was pH stable with pH optima of 3.0. The Lineweaver Burk analysis at various pH yielded pK(a) values of 3.3 and 4.29 indicating acidic amino acids at the active site of the enzyme. The structural changes exemplified compact secondary structure collapsed tertiary structure and exposure of hydrophobic patches at pH 10. The changes at pH 10 are typical of a molten globule state. This alkali induced molten globule is novel since acid induced molten globule state is more reported. (C) 2008 Elsevier B.V. All rights reserved.

10aAlkali induced molten globule10aPlant aspartic protease10aStructural transitions1 aKulkarni, Aarohi1 aGaikwad, Sushama, M.1 aRao, Mala uhttp://library.ncl.res.in/content/ph-induced-structural-alterations-aspartic-protease-vigna-radiata-indicating-alkali-001495nas a2200229 4500008004100000022001400041245010300055210006900158260010200227300001400329490000600343520060500349653002400954653001800978653003300996653002901029653001301058100001401071700002301085700002601108856013101134 2010 eng d a1930-212600aProduction of single cell protein, essential amino acids, and xylanase by penicillium janthinellum0 aProduction of single cell protein essential amino acids and xyla aCAMPUS BOX 8005, RALEIGH, NC 27695-8005 USAbNORTH CAROLINA STATE UNIV DEPT WOOD & PAPER SCIcOCT a2470-24770 v53 a

Microbial biomass having 46% crude protein content and enriched with essential amino acids as well as extracellular xylanase activity (100-150 IU/ml) was produced by an efficient fungal strain, Penicillium janthinellum (NCIM St-F-3b). Optimization studies for maximum xylanase and biomass production showed that the fungus required a simple medium containing bagasse hemicellulose as carbon source and ammonium sulphate as the nitrogen source. Therefore bagasse, which is a waste product of the sugar industry, can be efficiently used in microbioal biomass protein preparation for animal feed.

10aBagasse hydrolysate10aCrude protein10aMicrobial biomass production10aPenicillium janthinellum10aXylanase1 aRao, Mala1 aVarma, Anjanikumar1 aDeshmukh, Sumedha, S. uhttp://library.ncl.res.in/content/production-single-cell-protein-essential-amino-acids-and-xylanase-penicillium-janthinellum-001854nas a2200217 4500008004100000022001400041245009400055210006900149260009900218300001200317490000700329520104200336653002201378653002401400653001701424653002201441100001801463700001401481700002501495856011601520 2011 eng d a1359-511300aPurification and characterization of an alkaline protease by a new strain of Beauveria sp0 aPurification and characterization of an alkaline protease by a n aTHE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, OXON, ENGLANDbELSEVIER SCI LTDcFEB a579-5850 v463 a

A fungal culture isolated from animal dung was identified as a new strain of Beauveria sp MTCC 5184 based on 18S rDNA and ITS nucleotide sequence homology. The fungal isolate secretes alkaline protease active at pH 9 and 50 degrees C. The alkaline protease from Beauveria sp (BAP) was purified to homogeneity with 10.2-folds increase in specific activity and 38.6% recovery. The molecular mass and isoelectric point of the protease were found to be 29 kDa and 9.3, respectively. The N-terminal sequence of the BAP showed only partial homology with subtilisin like proteases from other fungi. The enzyme was stable up to 40 degrees C and pH 3-11. The protease was inhibited by Cd(2+), Hg(2+) and Mn(2+). The activity was totally lost in the presence of 1 mM PMSF suggesting it to be a serine protease. The protease showed maximum activity with casein followed by haemoglobin and BSA. The purified protease is able to separate the endothelial cells and can be used in animal cell culture. (C) 2010 Elsevier Ltd. All rights reserved.

10aAlkaline Protease10aAnimal cell culture10aBeauveria sp10aSequence homology1 aShankar, Shiv1 aRao, Mala1 aLaxman, Ryali, Seeta uhttp://library.ncl.res.in/content/purification-and-characterization-alkaline-protease-new-strain-beauveria-sp-002490nas a2200253 4500008004100000022001400041245010500055210006900160260007900229300001200308490000800320520154900328653002101877653002101898653003301919653001701952653002001969100002101989700002702010700002602037700001402063700002802077856013102105 2012 eng d a0273-228900aProduction, purification, and characterization of a beta-glucosidase of penicillium funiculosum NCL10 aProduction purification and characterization of a betaglucosidas a999 RIVERVIEW DRIVE SUITE 208, TOTOWA, NJ 07512 USAbHUMANA PRESS INCcJUL a959-9720 v1673 a

Penicillium funiculosum NCL1, a filamentous fungus, produced significantly higher levels of beta-glucosidase. The effect of initial pH, incubation temperature, and different carbon sources on extracellular beta-glucosidase production was studied in submerged fermentation. At 30 A degrees C with initial pH 5.0, enzyme production was increased by 48-fold upon induction with paper mill waste, as compared to commercial cellulose powder. In zymogram analysis, four isoforms of beta-glucosidases were observed with wheat bran whereas a minimum of one isoform was observed with other carbon sources. A major beta-glucosidase (Bgl3A) with the apparent molecular weight of similar to 120 kDa, induced by paper mill waste, was purified 19-fold to homogeneity, with a specific activity of 1,796 U/mg. Bgl3A was a monomeric glycoprotein with 29% of neutral carbohydrate content. It showed optimum activity at pH 4.0 and 5.0, optimum temperature at 60 A degrees C, and exhibited a half-life of 1 h at 60 A degrees C. K (m) of Bgl3A was found to be 0.057 mM with p-nitrophenyl beta-d-glucoside and V (max) was 1,920 U/mg. The purified enzyme exhibited glucose tolerance with a K (i) of 1.5 mM. Bgl3A readily hydrolyzed glucosides with beta-linkage. Bgl3A activity was enhanced (156%) by Zn2+ and was not affected by other metal cations and reagents. The supplementation of Bgl3A (5 U/mg) with Trichoderma reesei cellulase complex (5 FPU/mg) resulted in about 70% of enhanced glucose production, which emphasizes the industrial importance of Bgl3A.

10abeta-Glucosidase10aPaper mill waste10aPenicillium funiculosum NCL110aPurification10aThermostability1 aRamani, Gurusamy1 aMeera, Balasubramanian1 aVanitha, Chinnathambi1 aRao, Mala1 aGunasekaran, Paramasamy uhttp://library.ncl.res.in/content/production-purification-and-characterization-beta-glucosidase-penicillium-funiculosum-ncl1-002493nas a2200229 4500008004100000022001400041245010100055210006900156260011000225300001200335490000700347520160200354653002701956653002801983653001802011653003302029653001702062100001602079700002502095700001402120856012902134 2012 eng d a0301-120800aPurification and biochemical characterization of endoglucanase from Penicillium pinophilum MS 200 aPurification and biochemical characterization of endoglucanase f aDR K S KRISHNAN MARG, PUSA CAMPUS, NEW DELHI 110 012, INDIAbNATL INST SCIENCE COMMUNICATION-NISCAIRcJUN a189-1940 v493 a

Cellulases find increasing prominence in sustainable production of fuel and feedstock from lignocellulosic biomass. The purification and biochemical characterization of individual components of cellulase complex is important to understand the mechanism of their action for the solubilization of crystalline cellulose. In this study, an extra-cellular endoglucanase isolated from culture filtrate of Penicillium pinophilum MS 20 was purified to homogeneity by ammonium sulphate precipitation, ion-exchange chromatography and gel filtration. The purified endoglucanase (specific activity 69 U/mg) was a monomeric protein with molecular mass of 42 kDa, as determined by SDS-PAGE. The endoglucanase was active over a broad range of pH (4-7) with maximum activity at pH 5 and showed optimum temperature of 50 degrees C. It retained 100% activity at 50 degrees C for 6 h and half- lives of 4 h and 3 h at 60 degrees C and 70 degrees C, respectively. The kinetic constants for the endoglucanase determined with carboxymethyl cellulose as substrate were V-max of 72.5 U/mg and apparent K-m of 4.8 mg/ml. The enzyme also showed moderate activity towards H3PO4 swollen cellulose and p-nitrophenyl beta-D-glucoside, but no activity towards filter paper, Avicel and oat spelt xylan. The activity was positively modulated by 47, 32 and 25% in the presence of Co2+, Zn2+ and Mg2+, respectively to the reaction mixture. The wide pH stability (4-7) and temperature stability up to 50 degrees C of endoglucanase makes the enzyme suitable for use in cellulose saccharification at moderate temperature and pH.

10aBiochemical properties10aCarboxymethyl cellulose10aEndoglucanase10aPenicillium pinophilum MS 2010aPurification1 aPol, Dipali1 aLaxman, Ryali, Seeta1 aRao, Mala uhttp://library.ncl.res.in/content/purification-and-biochemical-characterization-endoglucanase-penicillium-pinophilum-ms-20-0