<?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%">Laxman, Ryali Seeta</style></author><author><style face="normal" font="default" size="100%">Sonawane, A. P.</style></author><author><style face="normal" font="default" size="100%">More, Shivaji V.</style></author><author><style face="normal" font="default" size="100%">Rao, B. S.</style></author><author><style face="normal" font="default" size="100%">Rele, M. V.</style></author><author><style face="normal" font="default" size="100%">Jogdand, Vitthal V.</style></author><author><style face="normal" font="default" size="100%">Deshpande, V. V.</style></author><author><style face="normal" font="default" size="100%">Rao, M. B.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Optimization and scale up of production of alkaline protease from Conidiobolus coronatus</style></title><secondary-title><style face="normal" font="default" size="100%">Process Biochemistry</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Alkaline Protease</style></keyword><keyword><style  face="normal" font="default" size="100%">Conidiobolus</style></keyword><keyword><style  face="normal" font="default" size="100%">Fermentation</style></keyword><keyword><style  face="normal" font="default" size="100%">Optimization</style></keyword><keyword><style  face="normal" font="default" size="100%">scale up</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2005</style></year><pub-dates><date><style  face="normal" font="default" size="100%">SEP</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">9</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%">40</style></volume><pages><style face="normal" font="default" size="100%">3152-3158</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Alkaline protease secreted by Conidiobolus coronatus has been evaluated extensively in tanneries and finds application in pre-tanning operations in leather manufacture. It is important to produce the enzyme in inexpensive and optimized media on large scale for the process to be commercially viable. The present paper describes optimization of fermentation conditions in shake flasks and scale up of production to 100 L in fermentors. The production is complete in 2-3 days comparable to bacterial fermentations. The organism utilized several carbon sources such as starch, sucrose, lactose, glucose and fructose for production. Soyabean meal at an optimum concentration of 2-3% was found to be best inducer. Diammonium hydrogen phosphate, casamino acids and Hi-media peptone gave activities comparable to yeast extract. Preservation and stabilization studies showed that glycerol conferred considerable stabilization at room temperature while ammonium sulphate precipitated enzyme at 0.9 saturation was best with stability up to 2 years even at room temperature. (c) 2005 Elsevier Ltd. All rights reserved.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">9</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%">2.529</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%">Poopal, Ashwini C.</style></author><author><style face="normal" font="default" size="100%">Laxman, Ryali Seeta</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Hexavalent chromate reduction by immobilized streptomyces griseus</style></title><secondary-title><style face="normal" font="default" size="100%">Biotechnology Letters</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Chromate reduction</style></keyword><keyword><style  face="normal" font="default" size="100%">Immobilized cells</style></keyword><keyword><style  face="normal" font="default" size="100%">polyvinyl alcohol</style></keyword><keyword><style  face="normal" font="default" size="100%">Streptomyces griseus</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%">JUN</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%">VAN GODEWIJCKSTRAAT 30, 3311 GZ DORDRECHT, NETHERLANDS</style></pub-location><volume><style face="normal" font="default" size="100%">30</style></volume><pages><style face="normal" font="default" size="100%">1005-1010</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Hexavalent chromium, which is a mutagen and carcinogen, was efficiently reduced by Streptomyces griseus. This activity was associated with the cell. Cr6+ reduction by free as well as immobilized cells was studied: cells in PVA- alginate had the highest ( 100%) Cr6+ removal efficiency in 24 h with reduction rates similar to free cells. Immobilized cells completely reduced 25 mg Cr6+ l(-1) in 24 h. PVA- alginate immobilized cells could be reused four times to completely reduce 25 mg Cr6+ l(-1) in 24 h each time. Chromate in a simulated effluent containing Cu2+, Mg2+, Mn2+ and Zn2+ was completely reduced by PVA- alginate immobilized cells within 9 h.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">6</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;1.639&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%">Poopal, Ashwini C.</style></author><author><style face="normal" font="default" size="100%">Laxman, Ryali Seeta</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Chromate reduction by PVA-alginate immobilized streptomyces griseus in a bioreactor</style></title><secondary-title><style face="normal" font="default" size="100%">Biotechnology Letters</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Bioremediation</style></keyword><keyword><style  face="normal" font="default" size="100%">Chromate reduction</style></keyword><keyword><style  face="normal" font="default" size="100%">Immobilized cells</style></keyword><keyword><style  face="normal" font="default" size="100%">Polyvinyl alcohol-alginate</style></keyword><keyword><style  face="normal" font="default" size="100%">Streptomyces griseus</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%">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%">SPRINGER</style></publisher><pub-location><style face="normal" font="default" size="100%">VAN GODEWIJCKSTRAAT 30, 3311 GZ DORDRECHT, NETHERLANDS</style></pub-location><volume><style face="normal" font="default" size="100%">31</style></volume><pages><style face="normal" font="default" size="100%">71-76</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 reduction of toxic Cr(6+) to the less toxic Cr(3+) is potentially a useful bioremediation process. Among the matrices tested for whole cell immobilization of an efficient chromate-reducing Streptomyces griseus strain, PVA-alginate was the most effective and was used for reduction of Cr(VI) in a bioreactor. Cr(6+) reduction efficiency decreased as Cr(6+) was increased from 2 to 12 mg l(-1) but increased with an increase in biomass concentration. However, increasing the flow rate from 2 to 8 ml h(-1) did not significantly affect Cr(6+) reduction. The reduction was faster in simulated effluent than in synthetic medium and complete removal of 8 mg Cr(6+) l(-1) from effluent and synthetic medium occurred in 2 and 12 h, respectively. Our results indicate that immobilized S. griseus cells could be applied for the large-scale bioremediation of chromate-containing effluents and wastewaters.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">1</style></issue><custom3><style face="normal" font="default" size="100%">Foreign</style></custom3><custom4><style face="normal" font="default" size="100%">1.768</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%">Singh, Rajkumar</style></author><author><style face="normal" font="default" size="100%">Varma, Anjanikumar</style></author><author><style face="normal" font="default" size="100%">Laxman, Ryali Seeta</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%">Hydrolysis of cellulose derived from steam exploded bagasse by penicillium cellulases: comparison with commercial cellulase</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%">Accellerase (TM) 1000</style></keyword><keyword><style  face="normal" font="default" size="100%">Enzymatic hydrolysis</style></keyword><keyword><style  face="normal" font="default" size="100%">High beta-glucosidase</style></keyword><keyword><style  face="normal" font="default" size="100%">Penicillium cellulase</style></keyword><keyword><style  face="normal" font="default" size="100%">Sugarcane bagasse</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%">DEC</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">24</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%">100</style></volume><pages><style face="normal" font="default" size="100%">6679-6681</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 complete cellulase from Penicillium pinophilum was evaluated for the hydrolysis of a-cellulose derived from steam exploded sugarcane bagasse and other cellulosic substrates. alpha-Cellulose at 1% substrate concentration was completely hydrolyzed by Penicillium cellulase within 3 h wherein at 10% the hydrolysis was 100% within 24 h with an enzyme loading of 10 FPU/g. The hydrolysate yielded glucose as major end product as analyzed by HPLC. Under similar conditions, hydrolysis of Sigmacell (microcrystalline cellulose), CP-123 (pulverized cellulose powder) and ball milled Solka Floc were 42%, 56% and 52%, respectively. Further the hydrolysis performance of Penicillium sp. cellulase is compared with Trichoderma reesei cellulase (Accellerase (TM) 1000) from Genencore. The kinetics of hydrolysis with respect to enzyme and substrate concentration will be presented. (C) 2009 Elsevier Ltd. All rights reserved.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">24</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;4.365&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%">Poopal, Ashwini C.</style></author><author><style face="normal" font="default" size="100%">Laxman, Ryali Seeta</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Studies on biological reduction of chromate by Streptomyces griseus</style></title><secondary-title><style face="normal" font="default" size="100%">Journal of Hazardous Materials</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Bioreduction</style></keyword><keyword><style  face="normal" font="default" size="100%">Chromate reductase</style></keyword><keyword><style  face="normal" font="default" size="100%">Hexavalent chromium</style></keyword><keyword><style  face="normal" font="default" size="100%">Streptomyces griseus</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%">SEP</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">1-3</style></number><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%">169</style></volume><pages><style face="normal" font="default" size="100%">539-545</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Chromium is a toxic heavy metal used in various industries and leads to environmental pollution due to improper handling. The most toxic form of chromium Cr(VI) can be converted to less toxic Cr(III) by reduction. Among the actinomycetes tested for chromate reduction, thirteen strains reduced Cr(VI) to Cr(III), of which one strain of Streptomyces griseus (NCIM 2020) was most efficient showing complete reduction within 24h. The organism was able to use a number of carbon sources as electron donors. Sulphate, nitrate, chloride and carbonate had no effect on chromate reduction during growth while cations such as Cd, Ni, Co and Cu were inhibitory to varying degrees. Chromate reduction was associated with the bacterial cells and sonication was the best method of cell breakage to release the enzyme. The enzyme was constitutive and did not require presence of chromate during growth for expression of activity. Chromate reduction with cell free extract (CFE) was observed without added NADH. However, addition of NAD(P)H resulted in 2-3-fold increase in activity. Chromate reductase showed optimum activity at 28 degrees C and pH 7 (C) 2009 Elsevier B.V. All rights reserved.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">1-3</style></issue><custom3><style face="normal" font="default" size="100%">Foreign</style></custom3><custom4><style face="normal" font="default" size="100%">3.723</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%">Shankar, Shiv</style></author><author><style face="normal" font="default" size="100%">Laxman, Ryali Seeta</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Immobilization of conidiobolus coronatus alkaline protease on waste fungal biomass</style></title><secondary-title><style face="normal" font="default" size="100%">Environmental Engineering and Management Journal</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Alkaline Protease</style></keyword><keyword><style  face="normal" font="default" size="100%">Conidiobolus coronatus</style></keyword><keyword><style  face="normal" font="default" size="100%">fungal biomass</style></keyword><keyword><style  face="normal" font="default" size="100%">Immobilization</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2011</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%">11</style></number><publisher><style face="normal" font="default" size="100%">GH ASACHI TECHNICAL UNIV IASI</style></publisher><pub-location><style face="normal" font="default" size="100%">71 MANGERON BLVD, IASI, 700050, ROMANIA</style></pub-location><volume><style face="normal" font="default" size="100%">10</style></volume><pages><style face="normal" font="default" size="100%">1727-1732</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Alkaline protease from Conidiobolus coronatus which is optimally active at pH 10 and 40 degrees C finds application in leather and detergent industries as well as for recovery of silver from waste photographic films. The protease was immobilized in Ca-alginate, polyacrylamide gel and alkali treated waste fungal biomass (ATWFB). ATWFB was found to be most suitable among the matrices tested. Glutaraldehyde marginally increased the binding to ATWFB. Binding of protease to ATWFB seems to be through adsorption as confirmed by FTIR spectra. Though temperature optima of free and immobilized proteases were identical, optimum pH of the immobilized enzyme shifted to 11 from 10. Temperature stability of the protease increased after immobilization. Immobilized protease could be reused 3 times with marginal loss in activity.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">11</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%">1.004</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%">Shankar, Shiv</style></author><author><style face="normal" font="default" size="100%">Rao, Mala</style></author><author><style face="normal" font="default" size="100%">Laxman, Ryali Seeta</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Purification and characterization of an alkaline protease by a new strain of Beauveria sp</style></title><secondary-title><style face="normal" font="default" size="100%">Process Biochemistry</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Alkaline Protease</style></keyword><keyword><style  face="normal" font="default" size="100%">Animal cell culture</style></keyword><keyword><style  face="normal" font="default" size="100%">Beauveria sp</style></keyword><keyword><style  face="normal" font="default" size="100%">Sequence homology</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2011</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%">2</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%">46</style></volume><pages><style face="normal" font="default" size="100%">579-585</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 fungal culture isolated from animal dung was identified as a new strain of Beauveria sp MTCC 5184 based on 18S rDNA and ITS nucleotide sequence homology. The fungal isolate secretes alkaline protease active at pH 9 and 50 degrees C. The alkaline protease from Beauveria sp (BAP) was purified to homogeneity with 10.2-folds increase in specific activity and 38.6% recovery. The molecular mass and isoelectric point of the protease were found to be 29 kDa and 9.3, respectively. The N-terminal sequence of the BAP showed only partial homology with subtilisin like proteases from other fungi. The enzyme was stable up to 40 degrees C and pH 3-11. The protease was inhibited by Cd(2+), Hg(2+) and Mn(2+). The activity was totally lost in the presence of 1 mM PMSF suggesting it to be a serine protease. The protease showed maximum activity with casein followed by haemoglobin and BSA. The purified protease is able to separate the endothelial cells and can be used in animal cell culture. (C) 2010 Elsevier Ltd. All rights reserved.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">2</style></issue><custom3><style face="normal" font="default" size="100%">Foreign</style></custom3><custom4><style face="normal" font="default" size="100%">3.43</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%">Sahare, Padmavati</style></author><author><style face="normal" font="default" size="100%">Singh, Rajkumar</style></author><author><style face="normal" font="default" size="100%">Laxman, Ryali Seeta</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%">Effect of alkali pretreatment on the structural properties and enzymatic hydrolysis of corn cob</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%">Corn cob</style></keyword><keyword><style  face="normal" font="default" size="100%">Crystallinity index</style></keyword><keyword><style  face="normal" font="default" size="100%">Enzymatic hydrolysis</style></keyword><keyword><style  face="normal" font="default" size="100%">Penicillium pinophilum</style></keyword><keyword><style  face="normal" font="default" size="100%">Specific surface area</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2012</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%">7</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%">168</style></volume><pages><style face="normal" font="default" size="100%">1806-1819</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;An effective alkali pretreatment which affects the structural properties of cellulose (corn cob) has been studied. The pretreatment of corn cob was carried out with different combinations of alkali at varying temperatures. The most effective pretreatment of corn cob was achieved with 1 % alkali at 50 A degrees C in 4 h. The crystallinity index (CrI) and specific surface area (SSA) of untreated corn cob was 39 % and 0.52 m(2)/g wherein after alkali pretreatment CrI decreased to 15 % and SSA increased to 3.32 m(2)/g. The fungal organism was identified as Penicillium pinophilum on the basis of ITS sequence. At 5 % substrate concentration using a complete cellulase from Penicillium pinophilum the hydrolysis of untreated corn cob with 5, 10 and 20 FPU/g enzyme loadings were 11 %, 13 % and 16 %, whereas after alkali treatment the hydrolysis increased to 78 %, 90 % and 100 %, respectively. Further hydrolytic potential of commercial cellulases viz. Accellerase (TM) 1,000, Palkofeel-30 and Palkocel-40 were investigated under similar conditions.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">7</style></issue><custom3><style face="normal" font="default" size="100%">Foreign</style></custom3><custom4><style face="normal" font="default" size="100%">1.893
</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%">Pol, Dipali</style></author><author><style face="normal" font="default" size="100%">Laxman, Ryali Seeta</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%">Purification and biochemical characterization of endoglucanase from Penicillium pinophilum MS 20</style></title><secondary-title><style face="normal" font="default" size="100%">Indian Journal of Biochemistry &amp; Biophysics</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Biochemical properties</style></keyword><keyword><style  face="normal" font="default" size="100%">Carboxymethyl cellulose</style></keyword><keyword><style  face="normal" font="default" size="100%">Endoglucanase</style></keyword><keyword><style  face="normal" font="default" size="100%">Penicillium pinophilum MS 20</style></keyword><keyword><style  face="normal" font="default" size="100%">Purification</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2012</style></year><pub-dates><date><style  face="normal" font="default" size="100%">JUN</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">3</style></number><publisher><style face="normal" font="default" size="100%">NATL INST SCIENCE COMMUNICATION-NISCAIR</style></publisher><pub-location><style face="normal" font="default" size="100%">DR K S KRISHNAN MARG, PUSA CAMPUS, NEW DELHI 110 012, INDIA</style></pub-location><volume><style face="normal" font="default" size="100%">49</style></volume><pages><style face="normal" font="default" size="100%">189-194</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Cellulases find increasing prominence in sustainable production of fuel and feedstock from lignocellulosic biomass. The purification and biochemical characterization of individual components of cellulase complex is important to understand the mechanism of their action for the solubilization of crystalline cellulose. In this study, an extra-cellular endoglucanase isolated from culture filtrate of Penicillium pinophilum MS 20 was purified to homogeneity by ammonium sulphate precipitation, ion-exchange chromatography and gel filtration. The purified endoglucanase (specific activity 69 U/mg) was a monomeric protein with molecular mass of 42 kDa, as determined by SDS-PAGE. The endoglucanase was active over a broad range of pH (4-7) with maximum activity at pH 5 and showed optimum temperature of 50 degrees C. It retained 100% activity at 50 degrees C for 6 h and half- lives of 4 h and 3 h at 60 degrees C and 70 degrees C, respectively. The kinetic constants for the endoglucanase determined with carboxymethyl cellulose as substrate were V-max of 72.5 U/mg and apparent K-m of 4.8 mg/ml. The enzyme also showed moderate activity towards H3PO4 swollen cellulose and p-nitrophenyl beta-D-glucoside, but no activity towards filter paper, Avicel and oat spelt xylan. The activity was positively modulated by 47, 32 and 25% in the presence of Co2+, Zn2+ and Mg2+, respectively to the reaction mixture. The wide pH stability (4-7) and temperature stability up to 50 degrees C of endoglucanase makes the enzyme suitable for use in cellulose saccharification at moderate temperature and pH.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">3</style></issue><custom3><style face="normal" font="default" size="100%">Indian</style></custom3><custom4><style face="normal" font="default" size="100%">1.026
</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%">More, Shivaji V.</style></author><author><style face="normal" font="default" size="100%">Khandelwal, Harish B.</style></author><author><style face="normal" font="default" size="100%">Joseph, M. A.</style></author><author><style face="normal" font="default" size="100%">Laxman, Ryali Seeta</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Enzymatic degumming of silk with microbial proteases</style></title><secondary-title><style face="normal" font="default" size="100%">Journal of Natural Fibers</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Alkaline Protease</style></keyword><keyword><style  face="normal" font="default" size="100%">bivoltine</style></keyword><keyword><style  face="normal" font="default" size="100%">degumming</style></keyword><keyword><style  face="normal" font="default" size="100%">microbial</style></keyword><keyword><style  face="normal" font="default" size="100%">Silk</style></keyword><keyword><style  face="normal" font="default" size="100%">weight loss</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><number><style face="normal" font="default" size="100%">2</style></number><publisher><style face="normal" font="default" size="100%">TAYLOR &amp; FRANCIS INC</style></publisher><pub-location><style face="normal" font="default" size="100%">325 CHESTNUT ST, SUITE 800, PHILADELPHIA, PA 19106 USA</style></pub-location><volume><style face="normal" font="default" size="100%">10</style></volume><pages><style face="normal" font="default" size="100%">98-111</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Degumming of Chinese bivoltine silk with alkaline proteases from various microbial sources was investigated and compared with commercial enzymes. Among the proteases tested, two fungal and two actinomycete proteases were promising, which showed weight loss similar to conventional method (19.58% to 21.78%). Conidiobolus brefeldianus and BOA-2 proteases were best enzymes, which showed weight loss similar to conventional method with low enzyme concentrations and in shorter time. No significant differences were found in tensile strength or elongation at break by enzymatic degumming indicating that there was no damage to the fiber. Scanning electron micrographs showed the sericin deposits were removed and the fibers were separated.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">2</style></issue><custom3><style face="normal" font="default" size="100%">Foreign</style></custom3><custom4><style face="normal" font="default" size="100%">0.512
</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%">Dalal, Sayli A.</style></author><author><style face="normal" font="default" size="100%">More, Snehal V.</style></author><author><style face="normal" font="default" size="100%">Shankar, Shiv</style></author><author><style face="normal" font="default" size="100%">Laxman, Ryali Seeta</style></author><author><style face="normal" font="default" size="100%">Gaikwad, Sushama M.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Subtilase from Beauveria sp.: conformational and functional investigation of unusual stability</style></title><secondary-title><style face="normal" font="default" size="100%">European Biophysics Journal With Biophysics Letters</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Beauveria</style></keyword><keyword><style  face="normal" font="default" size="100%">Chemical denaturation</style></keyword><keyword><style  face="normal" font="default" size="100%">Conformational transitions</style></keyword><keyword><style  face="normal" font="default" size="100%">Serine protease</style></keyword><keyword><style  face="normal" font="default" size="100%">Subtilase</style></keyword><keyword><style  face="normal" font="default" size="100%">Thermal denaturation</style></keyword><keyword><style  face="normal" font="default" size="100%">Thermodynamic stability</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2014</style></year><pub-dates><date><style  face="normal" font="default" size="100%">SEP</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">8-9</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%">43</style></volume><pages><style face="normal" font="default" size="100%">393-403</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Retention of total activity of the subtilisin-like serine protease from Beauveria sp. MTCC 5184 (Bprot) in the vicinity of (1) 3 M GdnHCl for 12 h, (2) 50 % methanol and dimethyl sulfoxide each for 24 h, and (3) proteolytic enzymes (trypsin, chymotrypsin, and proteinase K) for 48 h led to expect the enzyme to be a kinetically stable protein. Also, the structure of the protein was stable at pH 2.0. Biophysical characterization and conformational transitions were monitored using steady-state and time-resolved fluorescence, FTIR, and CD spectroscopy. Single tryptophan in the protein exists as two conformers, in hydrophobic and polar environment. The secondary structure of Bprot was stable in 3 M GdnHCl as seen in far-UV CD spectra. The active fraction of Bprot obtained from size-exclusion chromatography in the presence of GdnHCl (1.0-3.0 M) eluted at reduced retention time. The peak area of inactive or denatured protein with the same retention time as that of native protein increased with increasing concentration of denaturant (1.0-4.0 M GdnHCl). However, the kinetics of GdnHCl-induced unfolding as studied from intrinsic fluorescence revealed k (unf) of native protein to be 5.407 x 10(-5) s(-1) and a half-life of 3.56 h. The enzyme is thermodynamically stable in spite of being resistant to the denaturant, which could be due to the effect of GdnHCl imparting rigidity to the active fraction and simultaneously unfolding the partially unfolded protein that exists in equilibrium with the folded active protein. Thermal and pH denaturation of Bprot exhibited interesting structural transitions.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">8-9</style></issue><custom3><style face="normal" font="default" size="100%">Foreign</style></custom3><custom4><style face="normal" font="default" size="100%">0.09</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%">Nisal, Anuya</style></author><author><style face="normal" font="default" size="100%">Trivedy, Kanika</style></author><author><style face="normal" font="default" size="100%">Mohammad, Hasan</style></author><author><style face="normal" font="default" size="100%">Panneri, Suyana</style></author><author><style face="normal" font="default" size="100%">Sen Gupta, Sayam</style></author><author><style face="normal" font="default" size="100%">Lele, Ashish K.</style></author><author><style face="normal" font="default" size="100%">Manchala, Ramesh</style></author><author><style face="normal" font="default" size="100%">Kumar, Nirmal S.</style></author><author><style face="normal" font="default" size="100%">Gadgil, Mugdha</style></author><author><style face="normal" font="default" size="100%">Khandelwal, Harish B.</style></author><author><style face="normal" font="default" size="100%">More, Snehal</style></author><author><style face="normal" font="default" size="100%">Laxman, Ryali Seeta</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Uptake of Azo dyes into silk glands for production of colored silk cocoons using a green feeding approach</style></title><secondary-title><style face="normal" font="default" size="100%">ACS Sustainable Chemistry &amp; Engineering</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Azo dyes</style></keyword><keyword><style  face="normal" font="default" size="100%">Biochemical pathways</style></keyword><keyword><style  face="normal" font="default" size="100%">Color silk</style></keyword><keyword><style  face="normal" font="default" size="100%">Dye uptake</style></keyword><keyword><style  face="normal" font="default" size="100%">`' Green `' silk</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2014</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%">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%">2</style></volume><pages><style face="normal" font="default" size="100%">312-317</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Dyeing of textile fabrics is considered to be one of the most polluting industries today, and there is a need to develop green processes that can reduce this pollution. A promising technology that can potentially cleanup the dyeing of silk fibers that are widely used for textile applications would involve the generation of intrinsically colored silk cocoons. This can be achieved by feeding of Bombyx mori silkworm larvae with a modified feed of mulberry leaves containing a sprayed dye solution. This process significantly reduces the need for treating toxic dye effluents that are generated in traditional dyeing processes. In this report, we have evaluated a set of seven different azo dyes that are used in the textile industry for dyeing to produce intrinsically dyed silk. The dyes used in the study had similar chemical structures with systematically varying partition coefficients. The results suggest that while some dyes produced intrinsically colored silk other did not. Careful evaluation of the physical properties of these related azo dyes suggest that the balance of hydrophobic and hydrophilic character is necessary for diffusion of the dye from the alimentary canal of the silkworm larva into the hemolymph and later into the silk glands. The partition coefficient of the dye also determines the preferential association of the dye with either sericin or fibroin protein in the silkworm gland and finally into the cocoon. These insights are extremely important in development of novel dye molecules that can be successfully fed to Bombyx mori silkworm larvae for producing intrinsically colored silk of various colors and shades.&lt;/p&gt;</style></abstract><custom3><style face="normal" font="default" size="100%">Foreign</style></custom3><custom4><style face="normal" font="default" size="100%">4.73</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%">Shankar, Shiv</style></author><author><style face="normal" font="default" size="100%">Laxman, Ryali Seeta</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Biophysicochemical characterization of an alkaline protease from beauveria sp. MTCC 5184 with multiple applications</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%">Active site</style></keyword><keyword><style  face="normal" font="default" size="100%">Alkaline Protease</style></keyword><keyword><style  face="normal" font="default" size="100%">Beauveria sp</style></keyword><keyword><style  face="normal" font="default" size="100%">Organic solvent</style></keyword><keyword><style  face="normal" font="default" size="100%">Substrate kinetics</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2015</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%">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%">175</style></volume><pages><style face="normal" font="default" size="100%">589-602</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 study illustrates the biophysicochemical properties of an alkaline protease, BAP (Beauveria sp. alkaline protease) from Beauveria sp. MTCC 5184. This protease exhibited maximum activity at 50 degrees C, pH 9.0, and stability in a broad pH range, in the presence of organic solvents, denaturants, as well as detergents. Wash performance studies revealed that BAP was able to remove blood clots/stains from blood-soaked cloth. Peptide mass fingerprinting results demonstrated partial homology of BAP with subtilisin-like proteinase. BAP showed catalytic activity against natural as well as synthetic substrates. Active site characterization of BAP confirmed the involvement of serine, tryptophan, and aspartic acid in catalytic activity. Detailed kinetic and thermodynamic studies of BAP demonstrated that the activation energy (Ea) for casein hydrolysis was 82.55 kJ/M, the specificity constant (Kcat/K-m), and the values of Delta G (change in Gibbs free energy) decreased with increase in temperature, whereas Delta H (change in enthalapy) and Delta S (change in entropy) were constant. The results of the present study indicate that BAP has potential for applications as detergent additive, in peptide synthesis, and in basic research.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">1</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%">1.606</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%">Khandelwal, Harish B.</style></author><author><style face="normal" font="default" size="100%">More, Snehal V.</style></author><author><style face="normal" font="default" size="100%">Kalal, K. M.</style></author><author><style face="normal" font="default" size="100%">Laxman, Ryali Seeta</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Eco-friendly enzymatic dehairing of skins and hides by C-brefeldianus protease</style></title><secondary-title><style face="normal" font="default" size="100%">Clean Technologies and Environmental Policy</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Alkaline Protease</style></keyword><keyword><style  face="normal" font="default" size="100%">Conidiobolus brefeldianus</style></keyword><keyword><style  face="normal" font="default" size="100%">Cow hides</style></keyword><keyword><style  face="normal" font="default" size="100%">Dehaired pelts</style></keyword><keyword><style  face="normal" font="default" size="100%">Enzymatic dehairing</style></keyword><keyword><style  face="normal" font="default" size="100%">Sheep skins</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2015</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%">2</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%">17</style></volume><pages><style face="normal" font="default" size="100%">393-405</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Alkaline protease from Conidiobolus brefeldianus was efficient in unhairing various types of skins and hides. The crude protease preparation was active toward keratin-azure, elastin-orcin, azocasein, and azocoll, but did not show true collagenase activity. In addition, the crude enzyme exhibited other enzyme activities such as chondroitinase, laminarase, and chitinase. Complete hair removal of skin/hide by the protease achieved in 16-18 h. The dehaired pelt showed smooth and white appearance due to hair removal along with epidermal layer. In addition, the grain was clean and without damage in enzymatically dehaired pelts. The microscopic observation of the cross-section of dehaired goat skin and cow hide showed absence of epidermis, hair shaft with empty follicles. Enzymatic dehairing resulted in complete and uniform fiber opening in the dermis and corium region. Physical properties viz. tensile strength, elongation, and tear strength of dyed crust of enzymatically and conventionally dehaired pelts were comparable. Results were also validated on large scale with goat skins and cow hides.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">2</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%">1.934</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%">Shankar, Shiv</style></author><author><style face="normal" font="default" size="100%">Prasad, R. G. S. V.</style></author><author><style face="normal" font="default" size="100%">Selvakannan, P. R.</style></author><author><style face="normal" font="default" size="100%">Jaiswal, Lily</style></author><author><style face="normal" font="default" size="100%">Laxman, Ryali Seeta</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Green synthesis of silver nanoribbons from waste X-ray films using alkaline protease</style></title><secondary-title><style face="normal" font="default" size="100%">Materials Express</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Alkaline Protease</style></keyword><keyword><style  face="normal" font="default" size="100%">Characterization</style></keyword><keyword><style  face="normal" font="default" size="100%">Cytotoxicity</style></keyword><keyword><style  face="normal" font="default" size="100%">Silver Nanoribbons</style></keyword><keyword><style  face="normal" font="default" size="100%">Waste X-ray Film</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2015</style></year><pub-dates><date><style  face="normal" font="default" size="100%">APR</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 SCIENTIFIC PUBLISHERS</style></publisher><pub-location><style face="normal" font="default" size="100%">26650 THE OLD RD, STE 208, VALENCIA, CA 91381-0751 USA</style></pub-location><volume><style face="normal" font="default" size="100%">5</style></volume><pages><style face="normal" font="default" size="100%">165-170</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 work illustrates a facile approach to synthesize silver nanoribbons from waste X-ray films using alkaline protease from Beauveria sp. MTCC 5184 (BAP). The green synthesized nanoribbons have been characterized by UV-Vis spectroscopy, TEM, and FTIR. The UV-visible spectra gave maximum absorbance at 400 nm. TEM micrograph showed well-dispersed silver nanoribbons with an average length of 200-400 nm. FTIR result demonstrated the respective bands of the silver nanoribbons and proteins. XRD data revealed crystalline nature of silver nanoribbons dominated with (111) facets. In vitro antibacterial activity in terms of minimum inhibitory concentrations (MIC) and minimum bactericidal concentration (MBC) showed 8/16 mu g/mL (MIC/MBC) against Staphylococcus aureus ATCC 29213 and 4/8 mu g/mL (MIC/MBC) against Escherichia coli ATCC 25922. The green synthesized silver nanoribbons showed excellent biocompatibility up to 40 mu g/mL concentrations on mouse fibroblast cell line (L929).&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">2</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%">1.606</style></custom4></record></records></xml>