<?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%">Jagtap, Sharmili</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%">Conformation and microenvironment of the active site of a low molecular weight 1,4-beta-D-glucan glucanohydrolase from an alkalothermophilic thermomonospora sp.: involvement of lysine and cysteine residues</style></title><secondary-title><style face="normal" font="default" size="100%">Biochemical and Biophysical Research Communications</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">1</style></keyword><keyword><style  face="normal" font="default" size="100%">4-beta-D-glucan glucanohydrolase</style></keyword><keyword><style  face="normal" font="default" size="100%">active site microenvironment</style></keyword><keyword><style  face="normal" font="default" size="100%">Cysteine</style></keyword><keyword><style  face="normal" font="default" size="100%">lysine</style></keyword><keyword><style  face="normal" font="default" size="100%">OPTA</style></keyword><keyword><style  face="normal" font="default" size="100%">PHMB</style></keyword><keyword><style  face="normal" font="default" size="100%">Thermomonospora sp.</style></keyword><keyword><style  face="normal" font="default" size="100%">TNBS</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%">AUG</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">2</style></number><publisher><style face="normal" font="default" size="100%">ACADEMIC PRESS INC ELSEVIER SCIENCE</style></publisher><pub-location><style face="normal" font="default" size="100%">525 B ST, STE 1900, SAN DIEGO, CA 92101-4495 USA</style></pub-location><volume><style face="normal" font="default" size="100%">347</style></volume><pages><style face="normal" font="default" size="100%">428-432</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Conformation and microenvironment at the active site of 1,4-beta-D-glucan glucanohydrolase was probed with fluorescent chemo-affinity labeling using o-phthalaldehyde. OPTA has been known to form a fluorescent isoindole derivative by cross-linking the proximal thiol and amino groups of cysteine and lysine. Modification of lysine of the enzyme by TNBS and of cysteine residue by PHMB abolished the ability of the enzyme to form an isoindole derivative with OPTA. Kinetic analysis of the TNBS and PHMB-modified enzyme suggested the presence of essential lysine and cysteine residues, respectively, at the active site of the enzyme. The substrate protection of the enzyme with carboxymethylcellulose (CMC) confirmed the involvement of lysine and cysteine residues in the active site of the enzyme. Multiple sequence alignment of peptides obtained by tryptic digestion of the enzyme showed cysteine is one of the conserved amino acids corroborating the chemical modification studies. (c) 2006 Elsevier Inc. All rights reserved.&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%">&lt;p&gt;Foreign&lt;/p&gt;</style></custom3><custom4><style face="normal" font="default" size="100%">2.371</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%">Divate, Rupesh</style></author><author><style face="normal" font="default" size="100%">Menon, Vishnu</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%">Approach towards biocatalytic valorisation of barley beta-glucan for bioethanol production using 1,3-1,4 beta-glucanase and thermotolerant yeast</style></title><secondary-title><style face="normal" font="default" size="100%">International Biodeterioration &amp; Biodegradation</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">1</style></keyword><keyword><style  face="normal" font="default" size="100%">3-1</style></keyword><keyword><style  face="normal" font="default" size="100%">4 Glucan 4-gluconohydrolyase</style></keyword><keyword><style  face="normal" font="default" size="100%">Barley beta-glucan</style></keyword><keyword><style  face="normal" font="default" size="100%">Ethanol</style></keyword><keyword><style  face="normal" font="default" size="100%">Hydrolysis</style></keyword><keyword><style  face="normal" font="default" size="100%">Synergism</style></keyword><keyword><style  face="normal" font="default" size="100%">Thermotolerant yeast</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%">AUG</style></date></pub-dates></dates><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%">82</style></volume><pages><style face="normal" font="default" size="100%">81-86</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 exploitation of renewable resource containing polymers other than cellulose and hemicellulose are critically important for the feasibility of biofuel production. The potential of 1,3-1,4 glucan 4-gluconohydrolyase mediated saccharification of barley beta-glucan (BG) was investigated for ethanol production using thermotolerant Saccharomyces sp. A maximum hydrolysis of 71% was obtained in 24 h using in-house produced 1,3-1,4 beta-glucanase from an alkalothermophilic Thermomonospora sp. whereas the hydrolysis was 100% with Accellerase (TM) 1000. The synergistic effect of beta-glucosidase and 1,3-1,4 beta-glucanase was demonstrated by the exogenous addition of beta-glucosidase to Thermomonospora 1,3-1,4 beta-glucanase which resulted in complete hydrolysis of BG. The hydrolysates of BG obtained using Accellerase or a cocktail of Thermomonospora 1,3-1,4 beta-glucanase and beta-glucosidase when fermented with free cells of Saccharomyces at 40 degrees C produced an ethanol yield of 0.44 g g(-1) and 0.46 g g(-1) respectively and when fermented with immobilized cells produced a yield of 0.49 g g(-1). The Ca-alginate immobilized yeast cells were reused nine times at 40 degrees C with 100% fermentation efficiency. The economics of barley-to-fuel ethanol program will ameliorate if in addition to barley starch, beta-glucan is also utilized. (c) 2013 Elsevier Ltd. 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%">2.235
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