<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Adikane, H. V.</style></author><author><style face="normal" font="default" size="100%">Dange, M. N.</style></author><author><style face="normal" font="default" size="100%">Selvakumari, K.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Optimization of anaerobically digested distillery molasses spent wash decolorization using soil as inoculum in the absence of additional carbon and nitrogen source</style></title><secondary-title><style face="normal" font="default" size="100%">Bioresource Technology</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Decolorization</style></keyword><keyword><style  face="normal" font="default" size="100%">melanoidin</style></keyword><keyword><style  face="normal" font="default" size="100%">molasses spent wash (MSW)</style></keyword><keyword><style  face="normal" font="default" size="100%">Optimization</style></keyword><keyword><style  face="normal" font="default" size="100%">soil</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2006</style></year><pub-dates><date><style  face="normal" font="default" size="100%">NOV</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">16</style></number><publisher><style face="normal" font="default" size="100%">ELSEVIER SCI LTD</style></publisher><pub-location><style face="normal" font="default" size="100%">THE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, OXON, ENGLAND</style></pub-location><volume><style face="normal" font="default" size="100%">97</style></volume><pages><style face="normal" font="default" size="100%">2131-2135</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;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.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">16</style></issue><work-type><style face="normal" font="default" size="100%">Article</style></work-type><custom3><style face="normal" font="default" size="100%">&lt;p&gt;Foreign&lt;/p&gt;</style></custom3><custom4><style face="normal" font="default" size="100%">4.917</style></custom4></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Wang, M.</style></author><author><style face="normal" font="default" size="100%">Adikane, H. V.</style></author><author><style face="normal" font="default" size="100%">Duhamel, J.</style></author><author><style face="normal" font="default" size="100%">Chen, P.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Protection of oligo deoxynucleotides against nuclease degradation through association with self-assembling peptides</style></title><secondary-title><style face="normal" font="default" size="100%">Biomaterials</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">aggregate</style></keyword><keyword><style  face="normal" font="default" size="100%">centrifugation</style></keyword><keyword><style  face="normal" font="default" size="100%">Fluorescence resonance energy transfer (FRET)</style></keyword><keyword><style  face="normal" font="default" size="100%">nuclease resistance</style></keyword><keyword><style  face="normal" font="default" size="100%">oligonucleotide</style></keyword><keyword><style  face="normal" font="default" size="100%">self-assembling peptide</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2008</style></year><pub-dates><date><style  face="normal" font="default" size="100%">MAR</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">8</style></number><publisher><style face="normal" font="default" size="100%">ELSEVIER SCI LTD</style></publisher><pub-location><style face="normal" font="default" size="100%">THE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, OXON, ENGLAND</style></pub-location><volume><style face="normal" font="default" size="100%">29</style></volume><pages><style face="normal" font="default" size="100%">1099-1108</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;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.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">8</style></issue><custom3><style face="normal" font="default" size="100%">Foreign</style></custom3><custom4><style face="normal" font="default" size="100%">7.882</style></custom4></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Adikane, H. V.</style></author><author><style face="normal" font="default" size="100%">Dixit, J. N.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Effect of different operational conditions on the decolorization of molasses spent wash using once developed soil inoculum</style></title><secondary-title><style face="normal" font="default" size="100%">Biodegradation</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Decolorization</style></keyword><keyword><style  face="normal" font="default" size="100%">Membrane flux</style></keyword><keyword><style  face="normal" font="default" size="100%">Molasses spent wash</style></keyword><keyword><style  face="normal" font="default" size="100%">Soil as inoculum</style></keyword><keyword><style  face="normal" font="default" size="100%">stirred vessel</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2009</style></year><pub-dates><date><style  face="normal" font="default" size="100%">NOV</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">6</style></number><publisher><style face="normal" font="default" size="100%">SPRINGER</style></publisher><pub-location><style face="normal" font="default" size="100%">233 SPRING ST, NEW YORK, NY 10013 USA</style></pub-location><volume><style face="normal" font="default" size="100%">20</style></volume><pages><style face="normal" font="default" size="100%">867-874</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;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.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">6</style></issue><custom3><style face="normal" font="default" size="100%">Foreign</style></custom3><custom4><style face="normal" font="default" size="100%">2.012</style></custom4></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Adikane, H. V.</style></author><author><style face="normal" font="default" size="100%">Thakar, D. M.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Studies of penicillin G acylase immobilization using highly porous cellulose-based polymeric membrane</style></title><secondary-title><style face="normal" font="default" size="100%">Applied Biochemistry and Biotechnology</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Brilliant green</style></keyword><keyword><style  face="normal" font="default" size="100%">Immobilization</style></keyword><keyword><style  face="normal" font="default" size="100%">Penicillin G acylase</style></keyword><keyword><style  face="normal" font="default" size="100%">Polymeric membrane</style></keyword><keyword><style  face="normal" font="default" size="100%">Proline</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2010</style></year><pub-dates><date><style  face="normal" font="default" size="100%">FEB</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">4</style></number><publisher><style face="normal" font="default" size="100%">HUMANA PRESS INC</style></publisher><pub-location><style face="normal" font="default" size="100%">999 RIVERVIEW DRIVE SUITE 208, TOTOWA, NJ 07512 USA</style></pub-location><volume><style face="normal" font="default" size="100%">160</style></volume><pages><style face="normal" font="default" size="100%">1130-1145</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;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.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">4</style></issue><custom3><style face="normal" font="default" size="100%">Foreign</style></custom3><custom4><style face="normal" font="default" size="100%">1.879</style></custom4></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Adikane, H. V.</style></author><author><style face="normal" font="default" size="100%">Iyer, G. J.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Chemical modification of ethyl cellulose-based highly porous membrane for the purification of immunoglobulin G</style></title><secondary-title><style face="normal" font="default" size="100%">Applied Biochemistry and Biotechnology</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Affinity bioseparation</style></keyword><keyword><style  face="normal" font="default" size="100%">Ethyl cellulose</style></keyword><keyword><style  face="normal" font="default" size="100%">Glutaraldehyde</style></keyword><keyword><style  face="normal" font="default" size="100%">Immunoglobulin G</style></keyword><keyword><style  face="normal" font="default" size="100%">Polyethylenimine</style></keyword><keyword><style  face="normal" font="default" size="100%">Protein A</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2013</style></year><pub-dates><date><style  face="normal" font="default" size="100%">FEB</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">3</style></number><publisher><style face="normal" font="default" size="100%">HUMANA PRESS INC</style></publisher><pub-location><style face="normal" font="default" size="100%">999 RIVERVIEW DRIVE SUITE 208, TOTOWA, NJ 07512 USA</style></pub-location><volume><style face="normal" font="default" size="100%">169</style></volume><pages><style face="normal" font="default" size="100%">1026-1038</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;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.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">3</style></issue><custom3><style face="normal" font="default" size="100%">Foreign</style></custom3><custom4><style face="normal" font="default" size="100%">1.687
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