<?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%">Kulkarni, Shuklangi A.</style></author><author><style face="normal" font="default" size="100%">Ghormade, Vandana</style></author><author><style face="normal" font="default" size="100%">Kulkarni, Girish</style></author><author><style face="normal" font="default" size="100%">Kapoor, Manisha</style></author><author><style face="normal" font="default" size="100%">Chavan, Santosh B.</style></author><author><style face="normal" font="default" size="100%">Rajendran, Armugam</style></author><author><style face="normal" font="default" size="100%">Patil, Sanjay K.</style></author><author><style face="normal" font="default" size="100%">Shouche, Yogesh</style></author><author><style face="normal" font="default" size="100%">Deshpande, Mukund V.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Comparison of Metarhizium isolates for biocontrol of helicoverpa armigera (Lepidoptera : Noctuidae) in chickpea</style></title><secondary-title><style face="normal" font="default" size="100%">Biocontrol Science and Technology</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">appressorium formation</style></keyword><keyword><style  face="normal" font="default" size="100%">chitin deacetylase</style></keyword><keyword><style  face="normal" font="default" size="100%">chitinase</style></keyword><keyword><style  face="normal" font="default" size="100%">chitosanase</style></keyword><keyword><style  face="normal" font="default" size="100%">Helicoverpa armigera</style></keyword><keyword><style  face="normal" font="default" size="100%">Lipase</style></keyword><keyword><style  face="normal" font="default" size="100%">Metarhizium anisopliae</style></keyword><keyword><style  face="normal" font="default" size="100%">Protease</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%">FEB</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">8</style></number><publisher><style face="normal" font="default" size="100%">TAYLOR &amp; FRANCIS LTD</style></publisher><pub-location><style face="normal" font="default" size="100%">4 PARK SQUARE, MILTON PARK, ABINGDON OX14 4RN, OXON, ENGLAND</style></pub-location><volume><style face="normal" font="default" size="100%">18</style></volume><pages><style face="normal" font="default" size="100%">809-828</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Metarhizium isolates from soil (53) and insect hosts (10) were evaluated for extracellular production of cuticle degrading enzyme (CDE) activities such as chitinase, chitin deacetylase (CDA), chitosanase, protease and lipase. Regression analysis demonstrated the relation of CDE activities with Helicoverpa armigera mortality. On basis of this relation, ten isolates were selected for further evaluation. Subsequently, based on LT(50) of the 10 isolates towards H. armigera, five isolates were selected. Out of these five isolates, three were selected on the basis of higher conidia production (60-75 g/kg rice), faster sedimentation time (ST(50)) (2.3-2.65 h in 0.1% (w/v) Tween 80) and lower LC(50) (1.4- 5.7 x 10(3) conidia/mL) against H. armigera. Finally, three Metarhizium isolates were selected for the molecular fingerprinting using ITS sequencing and RAPD patterning. All three isolates, M34412, M34311 and M81123, showed comparable RAPD patterns with a 935G primer. These were further evaluated for their field performance against H. armigera in a chickpea crop. The percent efficacies with the three Metarhizium isolates were from 65 to 72%, which was comparable to the chemical insecticide, endosulfan (74%).&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">8</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%">0.848</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%">Nahar, Pallavi B.</style></author><author><style face="normal" font="default" size="100%">Kulkarni, Shuklangi A.</style></author><author><style face="normal" font="default" size="100%">Kulye, Mahesh S.</style></author><author><style face="normal" font="default" size="100%">Chavan, Santosh B.</style></author><author><style face="normal" font="default" size="100%">Kulkarni, Girish</style></author><author><style face="normal" font="default" size="100%">Rajendran, Armugham</style></author><author><style face="normal" font="default" size="100%">Yadav, Priya D.</style></author><author><style face="normal" font="default" size="100%">Shouche, Yogesh</style></author><author><style face="normal" font="default" size="100%">Deshpande, Mukund V.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Effect of repeated in vitro sub-culturing on the virulence of metarhizium anisopliae against helicoverpa armigera (Lepidoptera : Noctuidae)</style></title><secondary-title><style face="normal" font="default" size="100%">Biocontrol Science and Technology</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">appressorium formation</style></keyword><keyword><style  face="normal" font="default" size="100%">chitin deacetylase</style></keyword><keyword><style  face="normal" font="default" size="100%">chitinase</style></keyword><keyword><style  face="normal" font="default" size="100%">Helicoverpa armigera</style></keyword><keyword><style  face="normal" font="default" size="100%">in vitro sub-culturing</style></keyword><keyword><style  face="normal" font="default" size="100%">Lipase</style></keyword><keyword><style  face="normal" font="default" size="100%">Metarhizium anisopliae</style></keyword><keyword><style  face="normal" font="default" size="100%">Protease</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%">MAY</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">4</style></number><publisher><style face="normal" font="default" size="100%">TAYLOR &amp; FRANCIS LTD</style></publisher><pub-location><style face="normal" font="default" size="100%">4 PARK SQUARE, MILTON PARK, ABINGDON OX14 4RN, OXON, ENGLAND</style></pub-location><volume><style face="normal" font="default" size="100%">18</style></volume><pages><style face="normal" font="default" size="100%">337-355</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 effect of repeated conidial sub-culturing of Metarhizium anisopliae on its virulence against Helicoverpa armigera (Hbner) was studied. The LT(50) observed against third instar larvae of H. armigera for the first sub-culture was 3.4 days; it increased to 4.5 and 5.6 days for the 20th and the 40th sub-cultures, respectively. The LT50 values after passage of the 40th sub-culture on H. armigera decreased to 4.4 and 3.7 days for the 40th (first in vivo) and the 40th (fifth in vivo) passages, respectively. Similarly, the LC(50) of M. anisopliae towards third instar larvae of H. armigera increased from the first sub-culture (0.17x10(4)) to (3.0x10(4)) for the 40th conidial transfers on potato dextrose agar and again decreased to 0.74x10(4) and 0.23x10(4) in the 40th (first in vivo) and the 40th (fifth in vivo) passage, respectively. Similar trends for LC(50) and LT(50) values were seen when sugarcane woolly aphid, Ceratovacuna lanigera Zehntner was used as a host. Significant variation in appressorium formation and cuticle-degrading enzyme production such as chitinase, chitin deacetylase, chitosanase and protease during subsequent sub-culturing and passage through H. armigera was observed. Though there was no effect on internal transcribed spacer (ITS) sequence pattern, interestingly, in randomly amplified polymorphic DNA (RAPD), significant differences in the band intensities and in the banding pattern for different sub-cultures of M. anisopliae were observed. As stable virulence towards the insect pest is desirable for commercialisation of a mycoinsecticide, such changes in virulence due to repeated in vitro transfer need to be monitored and minimised.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">4</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%">0.848</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%">Trimukhe, K. D.</style></author><author><style face="normal" font="default" size="100%">Mahadik, N. D.</style></author><author><style face="normal" font="default" size="100%">Gokhale, D. V.</style></author><author><style face="normal" font="default" size="100%">Varma, Anjanikumar</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Environment friendly crosslinked chitosan as a matrix for selective adsorption and purification of lipase of aspergillus niger</style></title><secondary-title><style face="normal" font="default" size="100%">International Journal of Biological Macromolecules</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Adsorption</style></keyword><keyword><style  face="normal" font="default" size="100%">Chitosan</style></keyword><keyword><style  face="normal" font="default" size="100%">Lipase</style></keyword><keyword><style  face="normal" font="default" size="100%">Matrix</style></keyword><keyword><style  face="normal" font="default" size="100%">Purification</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%">DEC</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">5</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%">43</style></volume><pages><style face="normal" font="default" size="100%">422-425</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Chitosan and its derivatives have been used as affinity matrices for purification of lipase from Aspergillus niger NCIM 1207. Trimellitic anhydride (TMA)-crosslinked deacetylated chitin adsorbed lipase selectively, yielding approximately 5-fold purification of the crude lipase with 70% yield. Further 9-fold purification occurred on eluting through Sephacryl-100. These results suggest that chitosan derivatives can be used as inexpensive biopolymer matrices for the purification of lipases for industrial applications. (C) 2008 Elsevier B.V. All rights reserved.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">5</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;3.138&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%">Bhushan, Indu</style></author><author><style face="normal" font="default" size="100%">Parshad, Rajinder</style></author><author><style face="normal" font="default" size="100%">Qazi, Gulam Nabi</style></author><author><style face="normal" font="default" size="100%">Ingavle, Ganesh C.</style></author><author><style face="normal" font="default" size="100%">Rajan, C. R.</style></author><author><style face="normal" font="default" size="100%">Ponrathnam, Surendera</style></author><author><style face="normal" font="default" size="100%">Gupta, Vijay Kumar</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Lipase enzyme immobilization on synthetic beaded macroporous copolymers for kinetic resolution of chiral drugs intermediates</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%">1-phenyl ethanol and enantioselectivity</style></keyword><keyword><style  face="normal" font="default" size="100%">chiral resolution</style></keyword><keyword><style  face="normal" font="default" size="100%">enantiomeric excess (ee)</style></keyword><keyword><style  face="normal" font="default" size="100%">ethyl-3-hydroxy-3-phenyl propanoate</style></keyword><keyword><style  face="normal" font="default" size="100%">Immobilization</style></keyword><keyword><style  face="normal" font="default" size="100%">Lipase</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%">APR</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">4</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%">43</style></volume><pages><style face="normal" font="default" size="100%">321-330</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Lipase isolated from Arthrobacter sp. (bacterial strain, MTCC No. 5125) at RRL Jammu, being used for various process development. Arthrobacter sp. lipase (ABL) now has been immobilized on synthetic polymers and reused many a times. In this investigation number of various synthetic macroporous alkylated glycidyl epoxy copolymers with varying hydrophobicity, pore volume and surface area were prepared and used for this study. Among all the polymers prepared and used only two epoxy polymers GMA-EGDM 75-20(I) and GMA-EGDM 75-30(I) with particle size in the range of 150-450 nm, epoxy groups 80 and 70%, tertiary amino groups 20 and 30% was found suitable for immobilization of lipase (ABL). Dibutyl amine (DBA) incorporation created an internal pore radii 20-50 nm and hydrophobic microenvironment in both the polymers for binding the enzyme, which led to improvement in stability and enatioselectivity in racemic resolution process especially by binding to one of the isomers. The optimal ABL binding capacity of polymer GMA-EGDM 75-20(I) was 60 units, 34 mg protein and GMA-EGDM 75-30(l) was 36 units, 21 mg protein/g polymer. The immobilized lipase matrices displayed enhanced pH, thermal, organic solvent and long-term storage stability. Both the immobilized enzyme matrices were tested firstly for the hydrolysis of triglycerides using tributyrin as substrate. After testing, both the matrices were reused for racemic resolution of ethyl-3-hydroxy-3-phenyl propanoate (fluoxetine intermediate, an antidepressant drug) and racemic chiral auxiliary, acetyl-1-phenyl ethanol (intermediate of many chiral drugs) for 15 cycles. These immobilized lipase matrices have shown very high stability on recycling, high-enantioselectivity, high conversion and faster recovery of product compare to free enzyme, therefore these matrices may find use in kinetic resolution process developments. (C) 2007 Elsevier Ltd. All rights reserved.&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%">2.648</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%">Kantak, Jayshree B.</style></author><author><style face="normal" font="default" size="100%">Bagade, Aditi V.</style></author><author><style face="normal" font="default" size="100%">Mahajan, Siddharth A.</style></author><author><style face="normal" font="default" size="100%">Pawar, Shrikant P.</style></author><author><style face="normal" font="default" size="100%">Shouche, Yogesh S.</style></author><author><style face="normal" font="default" size="100%">Prabhune, Asmita</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Isolation, identification and optimization of a new extracellular lipase producing strain of rhizopus sp.</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 steep liquor</style></keyword><keyword><style  face="normal" font="default" size="100%">Fermentation</style></keyword><keyword><style  face="normal" font="default" size="100%">ITS region</style></keyword><keyword><style  face="normal" font="default" size="100%">Lipase</style></keyword><keyword><style  face="normal" font="default" size="100%">Medium optimization</style></keyword><keyword><style  face="normal" font="default" size="100%">Rhizopus</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%">AUG</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%">164</style></volume><pages><style face="normal" font="default" size="100%">969-978</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 lipolytic mesophilic fungus which produces lipase extracellularly was isolated from soil. Based on ITS1-5.8S-ITS4 region sequences of ribosomal RNA, it was concluded that the isolate JK-1 belongs to genus Rhizopus and clades with Rhizopus oryzae. The present paper reports the screening, isolation, identification, and optimization of fermentation conditions for the production of lipase (EC 3.1.1.3). Culture conditions were optimized, and the highest lipase production was observed in basal medium with corn steep liquor as nitrogen source and glucose as carbon source. Maximum lipase production was observed at 72 h, which is about 870 U/ml. Optimization of fermentation conditions resulted in 16-fold enhancement in enzyme production.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">7</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%">2.44</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%">Kantak, Jayshree B.</style></author><author><style face="normal" font="default" size="100%">Prabhune, Asmita</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Characterization of smallest active monomeric lipase from novel rhizopus strain: application in transesterification</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%">Lipase</style></keyword><keyword><style  face="normal" font="default" size="100%">Low molecular weight</style></keyword><keyword><style  face="normal" font="default" size="100%">Purification</style></keyword><keyword><style  face="normal" font="default" size="100%">Rhizopus</style></keyword><keyword><style  face="normal" font="default" size="100%">transesterification</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%">APR</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%">166</style></volume><pages><style face="normal" font="default" size="100%">1769-1780</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 extracellular lipase-producing fungus was isolated from oil-rich soil. This fungus belongs to the genus Rhizopus and clades with Rhizopus oryzae. Lipase was purified to homogeneity from this novel fungal source using ammonium sulphate precipitation followed by Q-Sepharose chromatography. The extracellular lipase was purified 8.6-fold, and enzymatic properties were studied. The molecular mass of the purified enzyme was estimated to be 17 kD by sodium dodecyl sulphate-polyacrylamide gel electrophoresis and 16.25 kD by matrix-assisted laser desorption ionization/time-of-flight analysis. The native molecular mass was estimated to be 17.5 kD by gel filtration, indicating the protein to be monomer. The optimum pH and temperature for the enzyme catalysis were 7.0 A degrees C and 40 A degrees C, respectively. Enzyme was stable in pH range 6.0-7.0 and retains 95-100% activity when incubated at 50 A degrees C for 1 h. The pI of the purified lipase was 4.2. Enzyme was stable in the organic solvents such as ethanol, hexane and methanol for 2 h. Purified enzyme was used for transesterification of oleic acid in the presence of ethanol for production of oleic acid ethyl ester with a conversion efficiency of 66% after 24 h at 30 A degrees C.&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%">Gaikaiwari, Raghavendra P.</style></author><author><style face="normal" font="default" size="100%">Wagh, Shilpa A.</style></author><author><style face="normal" font="default" size="100%">Kulkarni, Bhaskar D.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Efficient lipase purification using reverse micellar extraction</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%">(Hexadicetyltrimethylammoniumbromide)</style></keyword><keyword><style  face="normal" font="default" size="100%">AOT</style></keyword><keyword><style  face="normal" font="default" size="100%">CTAB</style></keyword><keyword><style  face="normal" font="default" size="100%">Lipase</style></keyword><keyword><style  face="normal" font="default" size="100%">RME</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%">MAR</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%">108</style></volume><pages><style face="normal" font="default" size="100%">224-230</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Reverse micellar extraction (RME) of enzyme provides an attractive option for conventional method with the potential to achieve purification and concentration in a single step with high yield. This study presents a methodology for optimization of RME with Pseudomonas lipase as model system. Fold-purification, percent recovery and extraction time were the objective functions while the type and concentration of surfactant, contact time, pH, ionic strength, and the ratio of organic to aqueous phase were the decision variables. Under optimized conditions, the AOT (Aerosol OT (bis 2-ethylhexyl) sodium sulfosuccinate)-isooctane system gave a 15-fold purification, 80% recovery and 2.5-fold concentration of the Pseudomonas lipase with process time of 45 min. (C) 2011 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%">4.75
</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%">Haldar, Saikat</style></author><author><style face="normal" font="default" size="100%">Kale, Balaji S.</style></author><author><style face="normal" font="default" size="100%">Jadhav, Dipesh D.</style></author><author><style face="normal" font="default" size="100%">Thulasiram, Hirekodathakallu V.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Lipase mediated separation of triterpene structural isomers, alpha- and beta-amyrin</style></title><secondary-title><style face="normal" font="default" size="100%">Tetrahedron Letters</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Amyrin</style></keyword><keyword><style  face="normal" font="default" size="100%">Candida rugosa</style></keyword><keyword><style  face="normal" font="default" size="100%">Kinetic separation</style></keyword><keyword><style  face="normal" font="default" size="100%">Lipase</style></keyword><keyword><style  face="normal" font="default" size="100%">Structural isomer</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%">MAY</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">19</style></number><publisher><style face="normal" font="default" size="100%">PERGAMON-ELSEVIER SCIENCE LTD</style></publisher><pub-location><style face="normal" font="default" size="100%">THE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, ENGLAND</style></pub-location><volume><style face="normal" font="default" size="100%">55</style></volume><pages><style face="normal" font="default" size="100%">3122-3125</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Pentacyclic triterpenoids alpha- and beta-amyrin possess a wide range of biological and pharmacological activities. High structural similarity between these two structural isomers makes their chromatographic separation an ineffective and tedious choice. In this study, Candida rugosa lipase catalyzed separation protocol for the isolation of individual isomers has been developed. In the presence of vinyl acetate as the acyl donor, Candida rugosa lipase carried out acetylation of beta-amyrin more efficiently as compared to alpha-amyrin leading to a kinetic separation. The conditions of transesterification reaction were optimized systematically, which was utilized to separate alpha- and beta-amyrin from a mixture obtained from the latex of Plumeria obtusa. (C) 2014 Elsevier Ltd. All rights reserved.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">19</style></issue><custom3><style face="normal" font="default" size="100%">Foreign</style></custom3><custom4><style face="normal" font="default" size="100%">2.68</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%">Sharma, Suraj</style></author><author><style face="normal" font="default" size="100%">Tambe, Sanjeev S.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Soft-sensor development for biochemical systems using genetic programming</style></title><secondary-title><style face="normal" font="default" size="100%">Biochemical Engineering Journal</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Artificial intelligence</style></keyword><keyword><style  face="normal" font="default" size="100%">Batch processing</style></keyword><keyword><style  face="normal" font="default" size="100%">Bioprocess monitoring</style></keyword><keyword><style  face="normal" font="default" size="100%">Lipase</style></keyword><keyword><style  face="normal" font="default" size="100%">Modeling</style></keyword><keyword><style  face="normal" font="default" size="100%">sensors</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%">APR</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%">85</style></volume><pages><style face="normal" font="default" size="100%">89-100</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Soft-sensors are software based process monitoring systems/models. In real-time they estimate those process variables, which are difficult to measure online or whose measurement by analytical procedures is tedious and time-consuming. In this study, the genetic programming (GP), an artificial intelligence based data-driven modeling formalism, has been introduced for the development of soft-sensors for biochemical processes. The novelty of the GP is that given example input-output data, it searches and optimizes both the form (structure) and parameters of an appropriate linear/nonlinear data-fitting model. In this study, GP-based soft-sensors have been developed for two bioprocesses, namely extracellular production of lipase enzyme and bacterial production of poly(3-hydroxybutyrate-co-3-hydroxyvalerate) copolymer. While in case study-I, the soft-sensor predicts the time-dependent lipase activity (U/ml), in case study-II it predicts the amount of accumulated polyhydroxyalkanoates (% dcw). The prediction and generalization performance of the GP-based soft-sensors was compared with the corresponding multi-layer perceptron (MLP) neural network and support vector regression (SVR) based soft-sensors. This comparison indicates that in the first case study the GP-based soft-sensor with the training and test set correlation coefficient (root-mean-squared-error) magnitudes of &amp;gt;0.96 (approximate to 0.962 U/ml) has clearly outperformed the two other soft-sensors. In case study-II involving bacterial copolymer production, the GP and SVR based soft-sensors have performed equally well (correlation coefficient approximate to 0.98) while the MLP based soft-sensor's performance was relatively inferior (correlation coefficient approximate to 0.94). (C) 2014 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%">3.03</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%">Patil, Harshal S.</style></author><author><style face="normal" font="default" size="100%">Jadhav, Dipesh D.</style></author><author><style face="normal" font="default" size="100%">Paul, Ajay</style></author><author><style face="normal" font="default" size="100%">Mulani, Fayaj A.</style></author><author><style face="normal" font="default" size="100%">Karegaonkar, Shrikant J.</style></author><author><style face="normal" font="default" size="100%">Thulasiram, Hirekodathakallu V.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Regioselective and efficient enzymatic synthesis of antimicrobial andrographolide derivatives</style></title><secondary-title><style face="normal" font="default" size="100%">Bioorganic &amp; Medicinal Chemistry Letters</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Acylation</style></keyword><keyword><style  face="normal" font="default" size="100%">Andrographolide</style></keyword><keyword><style  face="normal" font="default" size="100%">Antimicrobial activity</style></keyword><keyword><style  face="normal" font="default" size="100%">biocatalysis</style></keyword><keyword><style  face="normal" font="default" size="100%">Hemolysis</style></keyword><keyword><style  face="normal" font="default" size="100%">Lipase</style></keyword><keyword><style  face="normal" font="default" size="100%">Natural product</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2018</style></year><pub-dates><date><style  face="normal" font="default" size="100%">APR </style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">28</style></volume><pages><style face="normal" font="default" size="100%">1132-1137</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Labdane diterpene andrographolide (1) is a major constituent of Andrographis paniculata and known to exhibit wide spectrum of biological activities. In this study, regioselective monoesters of (1) have been synthesized by using Amano lipase AK (Pseudomonas fluorescens) as a biocatalyst. Amano lipase AK was able to execute highly efficient esterification of hydroxyl group attached to C-14 carbon of (1) in presence of acyl donors. Among the various synthesized derivatives including two novel compounds such as andrographolide-14-propionate (3) and andrographolide-14-caproate (5) displayed antimicrobial activity against Staphylococcus aureus with low minimal inhibitory concentration (MIC) 4 mu g/mL and 16 mu g/mL respectively. Furthermore, they have shown low hemolysis activity at their respective MIC and increase in the permeability of the bacterial cell membrane as delineated by FITC uptake and SEM imaging studies. (C) 2018 Elsevier Ltd. All rights reserved.&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%">2.454</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%">de Souza Brandao, Luma Mirely</style></author><author><style face="normal" font="default" size="100%">Barbosa, Milson dos Santos</style></author><author><style face="normal" font="default" size="100%">de Jesus, Roberta Anjos</style></author><author><style face="normal" font="default" size="100%">Bharad, Pradnya Arunrao</style></author><author><style face="normal" font="default" size="100%">Lima, Alvaro Silva</style></author><author><style face="normal" font="default" size="100%">Faria Soares, Cleide Mara</style></author><author><style face="normal" font="default" size="100%">Navarro Yerga, Rufino Manuel</style></author><author><style face="normal" font="default" size="100%">Bilal, Muhammad</style></author><author><style face="normal" font="default" size="100%">Romanholo Ferreira, Luiz Fernando</style></author><author><style face="normal" font="default" size="100%">Iqbal, Hafiz M. N.</style></author><author><style face="normal" font="default" size="100%">Gopinath, Chinnakonda S.</style></author><author><style face="normal" font="default" size="100%">Figueiredo, Renan Tavares</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Enhanced hydrogen fuel production using synergistic combination of solar radiation and TiO2 photocatalyst coupled with Burkholderia cepacia lipase</style></title><secondary-title><style face="normal" font="default" size="100%">International Journal of Hydrogen Energy</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">hydrogen production</style></keyword><keyword><style  face="normal" font="default" size="100%">Lipase</style></keyword><keyword><style  face="normal" font="default" size="100%">Nano-conjugated enzymes</style></keyword><keyword><style  face="normal" font="default" size="100%">Photocatalyst</style></keyword><keyword><style  face="normal" font="default" size="100%">Solar radiation</style></keyword><keyword><style  face="normal" font="default" size="100%">Titanium dioxide</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2022</style></year><pub-dates><date><style  face="normal" font="default" size="100%">APR </style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">47</style></volume><pages><style face="normal" font="default" size="100%">14483-14492</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;
	Promising and sustainable alternatives for hydrogen production have been investigated. Among these, the use of enzymes may represent an efficient alternative. In this work, an increase in hydrogen production under simulated sunlight by combining TiO2 and TiO2/MgCl2 with Burkholderia cepacia lipase (BCL) was reported. The samples (TiO2, TiO2/MgCl2, and TiO2 /MgCl2/BCL) were characterized by X-ray diffraction (XRD), thermo-gravimetric (TGA), N-2 adsorption-desorption isotherms (BET), scanning electron microscopy (SEM), and UV-Visible absorption spectra. Hydrogen production tests were performed in aqueous methanol solutions under simulated sunlight. The results demonstrated that 130-times greater increase in hydrogen production rate was observed by the addition of BCL than individual TiO2. This better hydrogen production rate can be attributed to the increase in the amount of reduction equivalent of the system due to the oxidation of protein peptides caused by TiO2. In conclusion, the results indicate that hydrogen production efficiency can be significantly improved when integrating TiO2/MgCl2 with BCL. (C) 2022 Hydrogen Energy Publications LLC. Published by Elsevier Ltd. All rights reserved.&lt;/p&gt;
</style></abstract><issue><style face="normal" font="default" size="100%">32</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;
	7.139&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%">Tracy, Preetanshika</style></author><author><style face="normal" font="default" size="100%">Dasgupta, Diptarka</style></author><author><style face="normal" font="default" size="100%">More, Snehal</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Challenges and opportunities for production of C5 sugar fatty acid esters (SFAEs) from renewable resources</style></title><secondary-title><style face="normal" font="default" size="100%">Industrial Crops and Products</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Bioprocess</style></keyword><keyword><style  face="normal" font="default" size="100%">C-5-fatty acid esters</style></keyword><keyword><style  face="normal" font="default" size="100%">Lipase</style></keyword><keyword><style  face="normal" font="default" size="100%">solvent</style></keyword><keyword><style  face="normal" font="default" size="100%">xylitol</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2023</style></year><pub-dates><date><style  face="normal" font="default" size="100%">MAR</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">193</style></volume><pages><style face="normal" font="default" size="100%">116170</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;
	Sugar fatty acid esters represent a billion-dollar market with huge global demand. Although glucose and sucrose-based surfactants have prevailed in the chemical industry for decades, C-5-based esters are relatively unknown and have recently started to gain attention owing to their multifunctional properties. These molecules can be derived from cheap and inexpensive biomass/renewable resources and present promising potential with diverse applications as additives in various nutraceutical, pharmaceutical, and cosmeceutical formulations. However, large-scale production of C-5 sugar esters is limited, with one or two commercial plants operating worldwide. This review highlights the major challenges and prospects of biotechnological production of the C-5 sugar esters, considering the possible advancements over existing technology with various aspects of industrial bioprocessing and product recovery.&lt;/p&gt;
</style></abstract><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;
	5.9&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%">Tracy, Preetanshika</style></author><author><style face="normal" font="default" size="100%">Dasgupta, Diptarka</style></author><author><style face="normal" font="default" size="100%">Ashok, Patel Pratima</style></author><author><style face="normal" font="default" size="100%">More, Snehal</style></author><author><style face="normal" font="default" size="100%">Sarkar, Bipul</style></author><author><style face="normal" font="default" size="100%">Porwal, Jyoti</style></author><author><style face="normal" font="default" size="100%">Tripathi, Deependra</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Enzymatic biodegradation of used engine oil using a novel lipase derived from renewable feedstocks</style></title><secondary-title><style face="normal" font="default" size="100%">World Journal of Microbiology &amp; Biotechnology</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Biodegradation</style></keyword><keyword><style  face="normal" font="default" size="100%">Lipase</style></keyword><keyword><style  face="normal" font="default" size="100%">PC5703</style></keyword><keyword><style  face="normal" font="default" size="100%">Used cooking oil</style></keyword><keyword><style  face="normal" font="default" size="100%">Used engine oil</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2025</style></year><pub-dates><date><style  face="normal" font="default" size="100%">NOV</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">41</style></volume><pages><style face="normal" font="default" size="100%">448</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 introduces an eco-friendly enzymatic approach for biodegrading used engine oil, utilizing a novel lipase from the mesophilic yeast strain Pichia Caribbica. The yeast was cultured in detoxified corncob hydrolysate with used cooking oil as an inducer. OVAT study confirmed that the optimal pH and temperature for lipase production by the strain was 7.0 and 25 degrees Celsius, respectively, with lipase activity of 70 IU/mL. The enzyme effectively degraded similar to 46% of used engine oil over a period of 15 days. Gas Chromatography-Mass Spectrometry (GC-MS) and FT-IR analysis confirmed a significant reduction in hydrocarbon concentrations and the emergence of new functional groups, confirming the enzyme's ability to degrade complex hydrocarbons into less toxic derivatives. These findings highlight the lipase's potential as an effective biocatalyst for eco-friendly bioremediation of oil-contaminated environments, such as soils and aquatic systems, while also emphasizing its role in environmental management through the reuse of waste by-products in enzyme production, thus reducing the environmental impact of improper waste disposal.&lt;/p&gt;
</style></abstract><issue><style face="normal" font="default" size="100%">11</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;
	4.6&lt;/p&gt;
</style></custom4></record></records></xml>