<?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%">Harshe, Yogesh M.</style></author><author><style face="normal" font="default" size="100%">Utikar, R. P.</style></author><author><style face="normal" font="default" size="100%">Ranade, V. V.</style></author><author><style face="normal" font="default" size="100%">Pahwa, D.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Modeling of rotary desiccant wheels</style></title><secondary-title><style face="normal" font="default" size="100%">Chemical Engineering &amp; Technology</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">1</style></keyword><keyword><style  face="normal" font="default" size="100%">4-benzodioxan-2-carboxylate</style></keyword><keyword><style  face="normal" font="default" size="100%">4-benzodioxan-2-carboxylic acid</style></keyword><keyword><style  face="normal" font="default" size="100%">doxazosin</style></keyword><keyword><style  face="normal" font="default" size="100%">enantio selectivity</style></keyword><keyword><style  face="normal" font="default" size="100%">enantiomeric ratio</style></keyword><keyword><style  face="normal" font="default" size="100%">ethyl 1</style></keyword><keyword><style  face="normal" font="default" size="100%">ethyl acetate</style></keyword><keyword><style  face="normal" font="default" size="100%">Lipases</style></keyword><keyword><style  face="normal" font="default" size="100%">transesterfication</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%">DEC</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">12</style></number><publisher><style face="normal" font="default" size="100%">WILEY-V C H VERLAG GMBH</style></publisher><pub-location><style face="normal" font="default" size="100%">PO BOX 10 11 61, D-69451 WEINHEIM, GERMANY</style></pub-location><volume><style face="normal" font="default" size="100%">28</style></volume><pages><style face="normal" font="default" size="100%">1473-1479</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Rotary desiccant wheels are widely used in dehumidification and energy recovery applications. In this work, we have developed a 2D, steady state model of a rotary desiccant wheel. Mass and energy balance equations for the air streams and the desiccant wheels were developed. The hydraulic diameter and surface area for heat and mass transfer were calculated based on knowledge of the flute geometry. Appropriate correlations for the Sherwood number and Nusselt number were used to estimate heat and mass transfer coefficients. The model is capable of predicting steady state behavior of desiccant wheels having at the most three sections (process, purge, and regeneration). The mathematical model was validated using a real desiccant wheel, and the calculation results are in reasonable agreement with the experimental data. Based on this model, the temperature and humidity profiles in the wheel during both the dehumidification and the regeneration processes are analyzed. The simulated results were used to gain an insight into the operation of desiccant wheels. The model and the presented results will be useful for optimizing dehumidification and energy recovery applications.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">12</style></issue><work-type><style face="normal" font="default" size="100%">Article</style></work-type><notes><style face="normal" font="default" size="100%">Joint 5th International Symposium on Catalysis in Multiphase Reactors/4th International Symposium on Multifunctional Reactors, Portoroz-Portorose, SLOVENIA, JUN 15-18, 2005</style></notes><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%">2.385</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%">Kasture, Sangita M.</style></author><author><style face="normal" font="default" size="100%">Varma, R</style></author><author><style face="normal" font="default" size="100%">Kalkote, Uttam R.</style></author><author><style face="normal" font="default" size="100%">Nene, S</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%">Novel enzymatic route for kinetic resolution of (+/-)1,4-benzodioxan-2-carboxylic acid</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%">1</style></keyword><keyword><style  face="normal" font="default" size="100%">4-benzodioxan-2-carboxylate</style></keyword><keyword><style  face="normal" font="default" size="100%">4-benzodioxan-2-carboxylic acid</style></keyword><keyword><style  face="normal" font="default" size="100%">doxazosin</style></keyword><keyword><style  face="normal" font="default" size="100%">enantio selectivity</style></keyword><keyword><style  face="normal" font="default" size="100%">enantiomeric ratio</style></keyword><keyword><style  face="normal" font="default" size="100%">ethyl 1</style></keyword><keyword><style  face="normal" font="default" size="100%">ethyl acetate</style></keyword><keyword><style  face="normal" font="default" size="100%">Lipases</style></keyword><keyword><style  face="normal" font="default" size="100%">transesterfication</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%">DEC</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">1</style></number><publisher><style face="normal" font="default" size="100%">ELSEVIER SCIENCE SA</style></publisher><pub-location><style face="normal" font="default" size="100%">PO BOX 564, 1001 LAUSANNE, SWITZERLAND</style></pub-location><volume><style face="normal" font="default" size="100%">27</style></volume><pages><style face="normal" font="default" size="100%">66-71</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">Ethyl 1,4-benzodioxan-2-carboxylate is used as an intermediate compound for the production of drug doxazosin mesylate. The title compound was kinetically resolved to get S-enantiomer of ethyl 1,4-benzodioxan 2-carboxylate in a simple lipase catalyzed transesterificafion reaction. Ethyl acetate was used as reaction medium as well as acyl donor. The influence of the enzyme source and time of reaction on the enantio selectivity of product were studied. Lipase from Candida antartica-B (Novozyme A/S) catalyzed transesterification reaction with good enantio selectivity towards S-enantiomer. The high enantiomeric ratio, E= 160, provided S-2 an acceptable chemical yield (50%) and enaritiomeric excess (&gt;95%). (c) 2005 Elsevier B.V. All rights reserved.</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%">2.463</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%">Varma, Rita</style></author><author><style face="normal" font="default" size="100%">Kasture, Sangita M.</style></author><author><style face="normal" font="default" size="100%">Nene, Sanjay</style></author><author><style face="normal" font="default" size="100%">Kalkote, Uttam R.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Lipases catalyzed enantioselective hydrolysis of (R,S)-methyl 1,4-benzodioxan-2-carboxylate intermediate for (S)-doxazosin mesylate</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%">1</style></keyword><keyword><style  face="normal" font="default" size="100%">4-benzodioxan-2-carboxylate</style></keyword><keyword><style  face="normal" font="default" size="100%">4-benzodioxan-2-carboxylic acid</style></keyword><keyword><style  face="normal" font="default" size="100%">doxazosin</style></keyword><keyword><style  face="normal" font="default" size="100%">Enantioselectivity</style></keyword><keyword><style  face="normal" font="default" size="100%">Lipases</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%">SPRINGER</style></publisher><pub-location><style face="normal" font="default" size="100%">233 SPRING STREET, NEW YORK, NY 10013 USA</style></pub-location><volume><style face="normal" font="default" size="100%">24</style></volume><pages><style face="normal" font="default" size="100%">577-579</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;(S)-1,4-benzodioxan-2-carboxylic acid-1 is used as starting compound for the production of the more effective (S) enantiomer of the drug doxazosin mesylate. The catalytic ability of some commercial lipases for preparations of (S) enantiomer of 1 from (+/-) methyl 1,4-benzodioxin-2-carboxylate-2 is reported. Lipases from bacterial sources were more successful in resolving the ester than those from the yeast lipases. About 85% enantiomerically pure ester was achieved by lipase from alcaligenes sp.&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%">1.214</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%">Sarate, P. J.</style></author><author><style face="normal" font="default" size="100%">Tamhane, V. A.</style></author><author><style face="normal" font="default" size="100%">Kotkar, H. M.</style></author><author><style face="normal" font="default" size="100%">Ratnakaran, N.</style></author><author><style face="normal" font="default" size="100%">Susan, N.</style></author><author><style face="normal" font="default" size="100%">Gupta, Vidya S.</style></author><author><style face="normal" font="default" size="100%">Giri, Ashok P.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Developmental and digestive flexibilities in the midgut of a polyphagous pest, the cotton bollworm, helicoverpa armigera</style></title><secondary-title><style face="normal" font="default" size="100%">Journal of Insect Science</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">amylases</style></keyword><keyword><style  face="normal" font="default" size="100%">larval performance</style></keyword><keyword><style  face="normal" font="default" size="100%">Lipases</style></keyword><keyword><style  face="normal" font="default" size="100%">Proteases</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><number><style face="normal" font="default" size="100%">3-4</style></number><publisher><style face="normal" font="default" size="100%">UNIV ARIZONA</style></publisher><pub-location><style face="normal" font="default" size="100%">LIBRARY C327, TUCSON, AZ 85721 USA</style></pub-location><volume><style face="normal" font="default" size="100%">12</style></volume><pages><style face="normal" font="default" size="100%">42</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Developmental patterns and survival of the cotton bollworm, Helicoverpa armigera Hubner (Lepidoptera: Noctuidae), a polyphagous insect pest, have been studied with reference to the effect of diet on major gut digestive enzymes (amylases, proteases, and lipases). Significant correlations between nutritional quality of the diet and larval and pupal mass were observed when H. armigera larvae were fed on various host plants viz. legumes (chickpea and pigeonpea), vegetables (tomato and okra), flowers (rose and marigold), and cereals (sorghum and maize). Larvae fed on diets rich in proteins and/or carbohydrates (pigeonpea, chickpea, maize, and sorghum) showed higher larval mass and developed more rapidly than larvae fed on diets with low protein and carbohydrate content (rose, marigold, okra, and tomato). Low calorific value diets like rose and marigold resulted in higher mortality (25-35%) of H. armigera. Even with highly varying development efficiency and larval/pupal survival rates, H. armigera populations feeding on different diets completed their life cycles. Digestive enzymes of H. armigera displayed variable expression levels and were found to be regulated on the basis of macromolecular composition of the diet. Post-ingestive adaptations operating at the gut level, in the form of controlled release of digestive enzymes, might be a key factor contributing to the physiological plasticity in H. armigera.&lt;/p&gt;</style></abstract><custom3><style face="normal" font="default" size="100%">&lt;p&gt;Foreign&lt;/p&gt;</style></custom3><custom4><style face="normal" font="default" size="100%">&lt;p&gt;2.39&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%">Rupani, Banin</style></author><author><style face="normal" font="default" size="100%">Kodam, Kisan M.</style></author><author><style face="normal" font="default" size="100%">Gadre, Ramchandra V.</style></author><author><style face="normal" font="default" size="100%">Najafpour, Ghasem D.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Lipase-mediated hydrolysis of flax seed oil for selective enrichment of alpha-linolenic acid</style></title><secondary-title><style face="normal" font="default" size="100%">European Journal of Lipid Science and Technology</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">a-Linolenic acid</style></keyword><keyword><style  face="normal" font="default" size="100%">Flax seed oil</style></keyword><keyword><style  face="normal" font="default" size="100%">Lipases</style></keyword><keyword><style  face="normal" font="default" size="100%">PUFA</style></keyword><keyword><style  face="normal" font="default" size="100%">Urea complexation</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%">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%">WILEY-BLACKWELL</style></publisher><pub-location><style face="normal" font="default" size="100%">111 RIVER ST, HOBOKEN 07030-5774, NJ USA</style></pub-location><volume><style face="normal" font="default" size="100%">114</style></volume><pages><style face="normal" font="default" size="100%">1246-1253</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Polyunsaturated fatty acids (PUFA) are important ingredients of human diet because of their prominent role in the function of human brain, eye and kidney. alpha-Linolenic acid (ALA), a C18, n-3 PUFA is a precursor of long chain PUFA in humans. Commercial lipases of Candida rugosa, Pseudomonas cepacea, Pseudomonas fluorescens, and Rhizomucor miehei were used for hydrolysis of flax seed oil. Reversed phase high performance liquid chromatography followed by gas chromatography showed that the purified oil contained 12 triacylglycerols (TAGs) with differences in fatty acid compositions. Flax seed oil TAGs contained alpha-linolenic acid (50%) as a major fatty acid while palmitic, oleic, linoleic made up rest of the portion. Among the four commercial lipases C. rugosa has preference for ALA, and that ALA was enriched in free fatty acids. C. rugosa lipase mediated hydrolysis of the TAGs resulted in a fatty acid mixture that was enriched in alpha-linolenic to about 72% yield that could be further enriched to 80% yield by selective removal of saturated fatty acids by urea complexation. Such purified ALA can be used for preparation of ALA-enriched glycerides. Practical applications: This methodology allows purifying ALA from fatty acid mixture obtained from flax seed oil by urea complexation.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">11</style></issue><custom3><style face="normal" font="default" size="100%">Foreign</style></custom3><custom4><style face="normal" font="default" size="100%">2.266
</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%">Mahajan, Pankaj S.</style></author><author><style face="normal" font="default" size="100%">Gonnade, Rajesh G.</style></author><author><style face="normal" font="default" size="100%">Mhaske, Santosh B.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Protecting-group-free diastereoselective total synthesis of (+/-)-6-epi-cleistenolide and chemoenzymatic synthesis of (-)-6-epi-cleistenolide</style></title><secondary-title><style face="normal" font="default" size="100%">European Journal of Organic Chemistry</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Asymmetric synthesis</style></keyword><keyword><style  face="normal" font="default" size="100%">diastereoselectivity</style></keyword><keyword><style  face="normal" font="default" size="100%">Enzyme catalysis</style></keyword><keyword><style  face="normal" font="default" size="100%">Lipases</style></keyword><keyword><style  face="normal" font="default" size="100%">Oxygen heterocycles</style></keyword><keyword><style  face="normal" font="default" size="100%">Total synthesis</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%">DEC</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">36</style></number><publisher><style face="normal" font="default" size="100%">WILEY-V C H VERLAG GMBH</style></publisher><pub-location><style face="normal" font="default" size="100%">BOSCHSTRASSE 12, D-69469 WEINHEIM, GERMANY</style></pub-location><pages><style face="normal" font="default" size="100%">8049-8054</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 short, efficient, practical, and protecting-group-free diastereoselective total synthesis of (+/-)-6-epi-cleistenolide (1) has been achieved in five steps in 60% overall yield. The use of a chemoenzymatic approach also gave (-)-6-epi-cleistenolide (1) (&amp;gt;99.9% ee). The Achmatowicz reaction, chemoselective oxidation of a hemiacetal, diastereoselective 1,3-anti reduction of alpha-hydroxy ketone, and enzymatic resolution of a 1,3-diol are the key features of this linear total synthesis. The synthetic strategy demonstrated in this paper could be extended for an asymmetric total synthesis of (-)-cleistenolide (1) and related biologically active natural products.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">36</style></issue><custom3><style face="normal" font="default" size="100%">Foreign</style></custom3><custom4><style face="normal" font="default" size="100%">3.13</style></custom4></record></records></xml>