01924nas a2200229   4500008004100000022001400041245016800055210006900223260009900292300001400391490000700405520100500412653001901417653001501436653003001451653001701481653000901498100002001507700001801527700002001545856012901565       2006                        eng d  a0960-852400aOptimization of anaerobically digested distillery molasses spent wash decolorization using soil as inoculum in the absence of additional carbon and nitrogen source0 aOptimization of anaerobically digested distillery molasses spent  aTHE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, OXON, ENGLANDbELSEVIER SCI LTDcNOV  a2131-21350 v973 a<p>The aim of this study was to achieve maximum decolorization of molasses spent wash (MSW) in absence of any additional carbon or nitrogen source using soil as inoculum. Soil samples were collected from the MSW disposal site. Colored soil samples exhibited higher pH, sugar and protein as compare to less colored samples. A decolorization of 69% was obtained using 10% (w/v) soil and 12.5% (v/v) MSW after 7 days incubation. Optimized parameters including days-6 days, pH-6, MSW-12.5% and soil concentration-40%, were obtained for maximum decolorization. A decolorization of 81% was achieved using 10% soil and 12.5% MSW after 18 days incubation in absence of any media supplement. Nearly 12% reduction in decolorization activity of the soil sample was observed over a period of 12 months when stored at 6 degrees C. It could be concluded that the decolorization of MSW might be achieved using soil as inoculum without addition of chemical amendments. (c) 2005 Elsevier Ltd. All rights reserved.</p>10aDecolorization10amelanoidin10amolasses spent wash (MSW)10aOptimization10asoil1 aAdikane, H., V.1 aDange, M., N.1 aSelvakumari, K.  uhttps://library.ncl.res.in/content/optimization-anaerobically-digested-distillery-molasses-spent-wash-decolorization-using-002379nas a2200253   4500008004100000022001400041245012000055210006900175260009900244300001400343490000700357520141500364653001401779653001901793653005001812653002401862653002001886653002801906100001301934700002001947700001601967700001301983856012901996       2008                        eng d  a0142-961200aProtection of oligo deoxynucleotides against nuclease degradation through association with self-assembling peptides0 aProtection of oligo deoxynucleotides against nuclease degradatio  aTHE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, OXON, ENGLANDbELSEVIER SCI LTDcMAR  a1099-11080 v293 a<p>Aggregates of the self-assembling peptide EAK16II or EAK16IV and oligodeoxynucleotides (ODNs) were prepared, and their stability upon diluting the solution was investigated by UV-vis spectroscopy. The aggregates prepared at pH 4 and pH 7 did not dissociate after the solution was diluted 5- and 10-fold. The resistance against Escherichia coli exonuclease I of the ODN located in the EAK-ODN aggregates was studied by fluorescence resonance energy transfer (FRET) after the ODN had aggregated with EAK 16II or EAK 16IV at pH 4 or pH 7. The effect that the peptide sequence, peptide concentration, pH, and centrifugation had on protecting the aggregated ODN against nuclease degradation was investigated. Significant nuclease resistance was obtained after the EAK-ODN aggregates had been prepared at pH 4, with an EAK16IV concentration greater than a threshold value, and ensuring that the solution was not centrifuged immediately after sample preparation. Centrifuging the EAK16IV-ODN solution immediately after sample preparation resulted in the loss of this nuclease protection. However, if the solution of EAK-ODN aggregates was centrifuged 24h after sample preparation, the nuclease protection afforded by the EAK16IV-ODN aggregates to the ODN was maintained even after being subject to a 10-fold dilution and up to 4 rounds of centrifugation over 4 days. (c) 2007 Elsevier Ltd. All rights reserved.</p>10aaggregate10acentrifugation10aFluorescence resonance energy transfer (FRET)10anuclease resistance10aoligonucleotide10aself-assembling peptide1 aWang, M.1 aAdikane, H., V.1 aDuhamel, J.1 aChen, P.  uhttps://library.ncl.res.in/content/protection-oligo-deoxynucleotides-against-nuclease-degradation-through-association-self-002135nas a2200217   4500008004100000022001400041245012700055210006900182260005700251300001200308490000700320520132400327653001901651653001801670653002401688653002101712653001901733100002001752700001801772856012701790       2009                        eng d  a0923-982000aEffect of different operational conditions on the decolorization of molasses spent wash using once developed soil inoculum0 aEffect of different operational conditions on the decolorization  a233 SPRING ST, NEW YORK, NY 10013 USAbSPRINGERcNOV  a867-8740 v203 a<p>A stirred vessel coupled with membrane unit containing cellulose acetate (0.45 mu m) membrane was used to study the decolorization of anaerobically digested molasses spent wash (MSW). The soil collected from the MSW disposal site was used as inoculum to study the decolorization without addition of any additives. The same inoculum was used over a period of 163 days at room temperature to study the decolorization of 12.5-50% (v/v) MSW using different operational conditions. The reactor was entered in to the inhibition mode after the feeding of 50% MSW, which was restored 100% without changing any operational condition. The maximum decolorization obtained for 12.5% (v/v) MSW was 77.22 +/- A 0.13%. The decolorization achieved for 25, 37.5, and 50% (v/v) MSW was 70.41 +/- A 0.12, 56.47 +/- A 0.17, and 48.78 +/- A 0.09%, respectively. Increase in the utilization of protein and reducing sugar was observed up to 25% MSW whereas, higher concentration showed decrease in the utilization. Results indicate 63% removal of chemical oxygen demand for 12.5% (v/v) MSW. Membrane flux which was significantly reduced after the feeding of 50% MSW was regenerated without changing the washing procedure, however, 35% decrease in sample flux was observed over the continuous use of membrane for the period of 198 days.</p>10aDecolorization10aMembrane flux10aMolasses spent wash10aSoil as inoculum10astirred vessel1 aAdikane, H., V.1 aDixit, J., N.  uhttps://library.ncl.res.in/content/effect-different-operational-conditions-decolorization-molasses-spent-wash-using-once-002125nas a2200217   4500008004100000022001400041245010600055210006900161260007900230300001400309490000800323520130700331653002001638653001901658653002501677653002301702653001201725100002001737700001901757856013101776       2010                        eng d  a0273-228900aStudies of penicillin G acylase immobilization using highly porous cellulose-based polymeric membrane0 aStudies of penicillin G acylase immobilization using highly poro  a999 RIVERVIEW DRIVE SUITE 208, TOTOWA, NJ 07512 USAbHUMANA PRESS INCcFEB  a1130-11450 v1603 a<p>The different ionic molecules/compounds were used as a ligand for the immobilization of penicillin G acylase on the highly porous cellulose-based polymeric membrane having buffer flux 1,746 LMH (L m(-2) h(-1)) at 0.5 bar pressure. The immobilized enzyme activity around 250 U-App was obtained with the ligand such as proline, tryptophan, casein acid hydrolysate, and brilliant green. Comparatively, proline showed less IMY% (percentage immobilization yield-58) but higher RTA% (percentage of activity retention-71) and specific activity (145 U-App g(-1)). However, the crosslinked preparation of brilliant green obtained using glutaraldehyde showed 82 +/- 2.7% immobilized enzyme activity after the completion of successive five cycles. In comparison with the free enzyme, the enzyme immobilized on the brilliant green coupled membrane showed around 2.4-fold increase in K-m value (47.4 mM) as well as similar optimum pH (7.2) and temperature (40 degrees C). The immobilized enzyme retained almost 50% activity after 107 days and 50 cycles of operation. Almost 50% decrease in buffer flux after enzyme immobilization was observed. At the end of the 30 cycles, flux pattern shows around 38% decrease in buffer flux however, after 16 cycles of operation flux moves closer towards the steady state.</p>10aBrilliant green10aImmobilization10aPenicillin G acylase10aPolymeric membrane10aProline1 aAdikane, H., V.1 aThakar, D., M.  uhttps://library.ncl.res.in/content/studies-penicillin-g-acylase-immobilization-using-highly-porous-cellulose-based-polymeric-002211nas a2200229   4500008004100000022001400041245011500055210006900170260007900239300001400318490000800332520136100340653002701701653002001728653001901748653002101767653002101788653001401809100002001823700001701843856012101860       2013                        eng d  a0273-228900aChemical modification of ethyl cellulose-based highly porous membrane for the purification of immunoglobulin G0 aChemical modification of ethyl cellulosebased highly porous memb  a999 RIVERVIEW DRIVE SUITE 208, TOTOWA, NJ 07512 USAbHUMANA PRESS INCcFEB  a1026-10380 v1693 a<p>The chemical modification of developed ethyl cellulose-based membrane was carried out to make it suitable for bioseparation. The different reagents were used for the modification of membrane to couple protein A (PA) to study the purification of immunoglobulin G (IgG) from blood. The chemical modification was carried out using relatively simple and mild reaction conditions. The attenuated total reflectance Fourier transform infrared analysis of chemically modified membrane showed new peak at 1,596.06 and 1,716.49 cm(-1). The scanning electron microscopy of PA-coupled membrane, which was used for IgG purification showed open pores and 950 +/- 21.5 LMH (L m(-2) h(-1)) operational flux at 0.5-bar out pressure. The flux of unmodified membrane was 1,746 +/- 18.5 LMH at 0.5-bar out pressure. The equilibrium adsorption concentration (318.5 +/- 5.9 mu g cm(-2)) was obtained at 3 h. The adsorption character of PA-coupled membrane was consistent with the Langmuir adsorption model and the non-specific binding was 67.08 +/- 1.3 mu g cm(-2). The sodium dodecyl sulfate polyacrylamide gel electrophoresis analysis showed similar purification pattern for purified IgG from human serum and commercial preparation of IgG. All the results have suggested a high potential of PA-coupled ethyl cellulose-based membrane for large-scale purification of IgG.</p>10aAffinity bioseparation10aEthyl cellulose10aGlutaraldehyde10aImmunoglobulin G10aPolyethylenimine10aProtein A1 aAdikane, H., V.1 aIyer, G., J.  uhttps://library.ncl.res.in/content/chemical-modification-ethyl-cellulose-based-highly-porous-membrane-purification-0