<?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%">Agarwal, Gopal P.</style></author><author><style face="normal" font="default" size="100%">Karan, Raj</style></author><author><style face="normal" font="default" size="100%">Bharti, Sachin</style></author><author><style face="normal" font="default" size="100%">Kumar, Hemant</style></author><author><style face="normal" font="default" size="100%">Jhunjhunwala, Sumit</style></author><author><style face="normal" font="default" size="100%">Sreekrishnan, T. R.</style></author><author><style face="normal" font="default" size="100%">Kharul, Ulhas K.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Effect of foulants on arsenic rejection via polyacrylonitrile ultrafiltration (UF) membrane</style></title><secondary-title><style face="normal" font="default" size="100%">Desalination</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Arsenic rejection</style></keyword><keyword><style  face="normal" font="default" size="100%">Egg white</style></keyword><keyword><style  face="normal" font="default" size="100%">Humic acid</style></keyword><keyword><style  face="normal" font="default" size="100%">Ovalbumin</style></keyword><keyword><style  face="normal" font="default" size="100%">Polyacrylonitrile</style></keyword><keyword><style  face="normal" font="default" size="100%">Ultrafiltration</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%">JAN</style></date></pub-dates></dates><publisher><style face="normal" font="default" size="100%">ELSEVIER SCIENCE BV</style></publisher><pub-location><style face="normal" font="default" size="100%">PO BOX 211, 1000 AE AMSTERDAM, NETHERLANDS</style></pub-location><volume><style face="normal" font="default" size="100%">309</style></volume><pages><style face="normal" font="default" size="100%">243-246</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Arsenic rejection via modified polyacrylonitrile ultrafiltration (UF) membrane was found to be very high, however, the presence of commonly found foulants in arsenic solution affected membrane performance. The effect of commonly found foulants, such as ovalbumin, humic acid and egg white on arsenic rejection were studied. Experiments indicated that the As(V) rejection was affected by the total quantity of proteins and not the variety of proteins present in a solution. As(V) rejection was found to decrease with increasing proteins while fouling was found to increase from 25% for 0.1 mg/ml to 33% for 0.5 mg/ml egg white. The As(V) rejection was found to decrease with increasing concentration of humic acid for PAN membranes. Fouling studies showed that humic acid was a lesser foulant in comparison to egg white. However a combination of the two foulants led to a decrease in the overall fouling. pH was also found to be a very important factor for egg white dissolution and As(V) rejection. (C) 2012 Elsevier B.V. All rights reserved.&lt;/p&gt;</style></abstract><custom3><style face="normal" font="default" size="100%">Foreign</style></custom3><custom4><style face="normal" font="default" size="100%">3.96
</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%">Ullah, Riaz</style></author><author><style face="normal" font="default" size="100%">Khan, Shadab Ali</style></author><author><style face="normal" font="default" size="100%">Aladresi, Aref Ali Mohammed</style></author><author><style face="normal" font="default" size="100%">Alharbi, Sulaiman Ali</style></author><author><style face="normal" font="default" size="100%">Chinnathambi, Arunachalam</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Ovalbumin-mediated synthesis and simultaneous functionalization of graphene with increased protein stability</style></title><secondary-title><style face="normal" font="default" size="100%">Green Chemistry Letters and Reviews</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Atomic force microscopy</style></keyword><keyword><style  face="normal" font="default" size="100%">graphene</style></keyword><keyword><style  face="normal" font="default" size="100%">graphene oxide</style></keyword><keyword><style  face="normal" font="default" size="100%">Ovalbumin</style></keyword><keyword><style  face="normal" font="default" size="100%">SDS-PAGE</style></keyword><keyword><style  face="normal" font="default" size="100%">thermal degradation</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2020</style></year><pub-dates><date><style  face="normal" font="default" size="100%">JAN </style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">13</style></volume><pages><style face="normal" font="default" size="100%">60-67</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;In this article, we have shown an easy, one-step, protein-directed approach for the synthesis of water-soluble and functional graphene using ovalbumin. The obtained ovalbumin functionalized graphene was characterized by UV-visible spectroscopy, X-ray diffraction, Raman spectroscopy, and Fourier transform infrared spectroscopy. Atomic force microscopy was used to check the attachment/functionalization of ovalbumin on grapheme sheets. It was shown that the functionalization of ovalbumin on grapheme sheets makes the protein more thermally stable compare to free ovalbumin, which has been shown by using sodium dodecyl sulfate polyacrylamide gel electrophoresis.&lt;/p&gt;
</style></abstract><issue><style face="normal" font="default" size="100%">1</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%">&lt;p&gt;3.286&lt;/p&gt;
</style></custom4></record></records></xml>