<?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%">Anish, Ramakrishnan</style></author><author><style face="normal" font="default" size="100%">Rao, Mala</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Biochemical characterization of a novel beta-1-3, 1-4 glucan 4-glucanohydrolase from thermomonospora sp having a single active site for lichenan and xylan</style></title><secondary-title><style face="normal" font="default" size="100%">Biochimie</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">1-4 glucan 4-glucanohydrolase</style></keyword><keyword><style  face="normal" font="default" size="100%">beta-1-3</style></keyword><keyword><style  face="normal" font="default" size="100%">bifunctional</style></keyword><keyword><style  face="normal" font="default" size="100%">O-phthaialdehyde</style></keyword><keyword><style  face="normal" font="default" size="100%">single active site</style></keyword><keyword><style  face="normal" font="default" size="100%">Thermomonospora sp.</style></keyword><keyword><style  face="normal" font="default" size="100%">Xylanase</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2007</style></year><pub-dates><date><style  face="normal" font="default" size="100%">DEC</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">12</style></number><publisher><style face="normal" font="default" size="100%">ELSEVIER FRANCE-EDITIONS SCIENTIFIQUES MEDICALES ELSEVIER</style></publisher><pub-location><style face="normal" font="default" size="100%">23 RUE LINOIS, 75724 PARIS, FRANCE</style></pub-location><volume><style face="normal" font="default" size="100%">89</style></volume><pages><style face="normal" font="default" size="100%">1489-1497</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 bifunctional high molecular weight (Mr, 64,500 Da) beta-1-3, 1-4 glucan 4-glucanohydrolase was purified to homogeneity from Thermomonospora sp., exhibiting activity towards lichenan and xylan. A kinetic method was used to analyze the active site that hydrolyzes lichenan and xylan. The experimental data was in agreement with the theoretical values calculated for a single active site. Probing the conformation and microenvironment at active site of the enzyme by fluorescent chemo-affinity label, OPTA resulted in the formation of an isoindole derivative with complete inactivation of the enzyme to hydrolyse both lichenan and xylan confirmed the results of kinetic method. OPTA forms an isoindole derivative by cross-linking the proximal thiol and amino groups. The modification of cysteine and lysine residues by DTNB and TNBS respectively abolished the ability of the enzyme to form an isoindole derivative with OPTA, indicating the participation of cysteine and lysine in the formation of isoindole complex. (C) 2007 Elsevier Masson SAS. All rights reserved.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">12</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;2.474&lt;/p&gt;</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%">Ramakrishnan, Anish</style></author><author><style face="normal" font="default" size="100%">Pandit, Nilesh</style></author><author><style face="normal" font="default" size="100%">Badgujar, Mahesh</style></author><author><style face="normal" font="default" size="100%">Bhaskar, C.</style></author><author><style face="normal" font="default" size="100%">Rao, Mala</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Encapsulation of endoglucanase using a biopolymer Gum arabic for its controlled release</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%">Enzyme catalysis</style></keyword><keyword><style  face="normal" font="default" size="100%">OPTA</style></keyword><keyword><style  face="normal" font="default" size="100%">Thermomonospora sp.</style></keyword><keyword><style  face="normal" font="default" size="100%">Xylanase</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2007</style></year><pub-dates><date><style  face="normal" font="default" size="100%">JAN</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">2</style></number><publisher><style face="normal" font="default" size="100%">AMER CHEMICAL SOC</style></publisher><pub-location><style face="normal" font="default" size="100%">1155 16TH ST, NW, WASHINGTON, DC 20036 USA</style></pub-location><volume><style face="normal" font="default" size="100%">98</style></volume><pages><style face="normal" font="default" size="100%">368-372</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;{Gum Arabic, a biodegradable natural polymer was used as a matrix to encapsulate endoglucanase from Thermomonospora sp. The modified enzyme retained complete biocatalytic activity and exhibited a shift in the optimum temperature [&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">2</style></issue><work-type><style face="normal" font="default" size="100%">Article</style></work-type><custom3><style face="normal" font="default" size="100%">Foreign</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%">Vathipadiekal, Vinod</style></author><author><style face="normal" font="default" size="100%">Verma, Anamika</style></author><author><style face="normal" font="default" size="100%">Rao, Mala</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Glycine-assisted enhancement of 1,4-beta-D-xylan xylanohydrolase activity at alkaline pH with a pH optimum shift</style></title><secondary-title><style face="normal" font="default" size="100%">Biological Chemistry</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Enzyme catalysis</style></keyword><keyword><style  face="normal" font="default" size="100%">OPTA</style></keyword><keyword><style  face="normal" font="default" size="100%">Thermomonospora sp.</style></keyword><keyword><style  face="normal" font="default" size="100%">Xylanase</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2007</style></year><pub-dates><date><style  face="normal" font="default" size="100%">JAN</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">1</style></number><publisher><style face="normal" font="default" size="100%">WALTER DE GRUYTER GMBH</style></publisher><pub-location><style face="normal" font="default" size="100%">GENTHINER STRASSE 13, D-10785 BERLIN, GERMANY</style></pub-location><volume><style face="normal" font="default" size="100%">388</style></volume><pages><style face="normal" font="default" size="100%">61-65</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;This is the first report describing the enhancement of xylanase activity by the neutral amino acid glycine. Xylanase activity is increased seven-fold at alkaline pH in the presence of glycine and its pH optimum is shifted from pH 7 to 8 without using any protein engineering techniques. Analysis of the steady-state kinetics revealed that glycine in the reaction mixture increases the K-m and k(cat) values of the enzyme. Chemoaffinity labeling and studies using glycine esters indicate an involvement of the carboxylate ion of glycine in enhancing xylanase catalytic activity. A novel possible mechanism for the glycine-assisted catalytic action of xylanase is proposed.&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%">Foreign</style></custom3><custom4><style face="normal" font="default" size="100%">4.258</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%">Rao, Mala</style></author><author><style face="normal" font="default" size="100%">Varma, Anjanikumar</style></author><author><style face="normal" font="default" size="100%">Deshmukh, Sumedha S.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Production of single cell protein, essential amino acids, and xylanase by penicillium janthinellum</style></title><secondary-title><style face="normal" font="default" size="100%">Bioresources</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Bagasse hydrolysate</style></keyword><keyword><style  face="normal" font="default" size="100%">Crude protein</style></keyword><keyword><style  face="normal" font="default" size="100%">Microbial biomass production</style></keyword><keyword><style  face="normal" font="default" size="100%">Penicillium janthinellum</style></keyword><keyword><style  face="normal" font="default" size="100%">Xylanase</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%">OCT</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">4</style></number><publisher><style face="normal" font="default" size="100%">NORTH CAROLINA STATE UNIV DEPT WOOD &amp; PAPER SCI</style></publisher><pub-location><style face="normal" font="default" size="100%">CAMPUS BOX 8005, RALEIGH, NC 27695-8005 USA</style></pub-location><volume><style face="normal" font="default" size="100%">5</style></volume><pages><style face="normal" font="default" size="100%">2470-2477</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;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.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">4</style></issue><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;1.418&lt;/p&gt;</style></custom4></record></records></xml>