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Search results for: Ermias Melake Tesfay

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</div> </nav> </div> </header> <main> <div class="container mt-4"> <div class="row"> <div class="col-md-9 mx-auto"> <form method="get" action="https://publications.waset.org/abstracts/search"> <div id="custom-search-input"> <div class="input-group"> <i class="fas fa-search"></i> <input type="text" class="search-query" name="q" placeholder="Author, Title, Abstract, Keywords" value="Ermias Melake Tesfay"> <input type="submit" class="btn_search" value="Search"> </div> </div> </form> </div> </div> <div class="row mt-3"> <div class="col-sm-3"> <div class="card"> <div class="card-body"><strong>Commenced</strong> in January 2007</div> </div> </div> <div class="col-sm-3"> <div class="card"> <div class="card-body"><strong>Frequency:</strong> Monthly</div> </div> </div> <div class="col-sm-3"> <div class="card"> <div class="card-body"><strong>Edition:</strong> International</div> </div> </div> <div class="col-sm-3"> <div class="card"> <div class="card-body"><strong>Paper Count:</strong> 4</div> </div> </div> </div> <h1 class="mt-3 mb-3 text-center" style="font-size:1.6rem;">Search results for: Ermias Melake Tesfay</h1> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">4</span> Cloning and Characterization of UDP-Glucose Pyrophosphorylases from Lactobacillus kefiranofaciens and Rhodococcus wratislaviensis</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Mesfin%20Angaw%20Tesfay">Mesfin Angaw Tesfay</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Uridine-5’-diphosphate (UDP)-glucose is one of the most versatile building blocks within the metabolism of prokaryotes and eukaryotes, serving as an activated sugar donor during the glycosylation of natural products. It is formed by the enzyme UDP-glucose pyrophosphorylase (UGPase) using uridine-5′-triphosphate (UTP) and α-d-glucose 1-phosphate as a substrate. Herein, two UGPase genes from Lactobacillus kefiranofaciens ZW3 (LkUGPase) and Rhodococcus wratislaviensis IFP 2016 (RwUGPase) were identified through genome mining approaches. The LkUGPase and RwUGPase have 299 and 306 amino acids, respectively. Both UGPase has the conserved UTP binding site (G-X-G-T-R-X-L-P) and the glucose -1-phosphate binding site (V-E-K-P). The LkUGPase and RwUGPase were cloned in E. coli, and SDS-PAGE analysis showed the expression of both enzymes forming about 36 KDa of protein band after induction. LkUGPase and RwUGPase have an activity of 1549.95 and 671.53 U/mg, respectively. Currently, their kinetic properties are under investigation. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=UGPase" title="UGPase">UGPase</a>, <a href="https://publications.waset.org/abstracts/search?q=LkUGPase" title=" LkUGPase"> LkUGPase</a>, <a href="https://publications.waset.org/abstracts/search?q=RwUGPase" title=" RwUGPase"> RwUGPase</a>, <a href="https://publications.waset.org/abstracts/search?q=UDP-glucose" title=" UDP-glucose"> UDP-glucose</a>, <a href="https://publications.waset.org/abstracts/search?q=glycosylation" title=" glycosylation"> glycosylation</a> </p> <a href="https://publications.waset.org/abstracts/192250/cloning-and-characterization-of-udp-glucose-pyrophosphorylases-from-lactobacillus-kefiranofaciens-and-rhodococcus-wratislaviensis" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/192250.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">24</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">3</span> Cloning and Characterization of Uridine-5’-Diphosphate -Glucose Pyrophosphorylases from Lactobacillus Kefiranofaciens and Rhodococcus Wratislaviensis</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Mesfin%20Angaw%20Tesfay">Mesfin Angaw Tesfay</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Uridine-5’-diphosphate (UDP)-glucose is one of the most versatile building blocks within the metabolism of prokaryotes and eukaryotes serving as an activated sugar donor during the glycosylation of natural products. It is formed by the enzyme UDP-glucose pyrophosphorylase (UGPase) using uridine-5′-triphosphate (UTP) and α-d-glucose 1-phosphate as a substrate. Herein two UGPase genes from Lactobacillus kefiranofaciens ZW3 (LkUGPase) and Rhodococcus wratislaviensis IFP 2016 (RwUGPase) were identified through genome mining approaches. The LkUGPase and RwUGPase have 299 and 306 amino acids, respectively. Both UGPase has the conserved UTP binding site (G-X-G-T-R-X-L-P) and the glucose -1-phosphate binding site (V-E-K-P). The LkUGPase and RwUGPase were cloned in E. coli and SDS-PAGE analysis showed the expression of both enzymes forming about 36 KDa of protein band after induction. LkUGPase and RwUGPase have an activity of 1549.95 and 671.53 U/mg respectively. Currently, their kinetic properties are under investigation. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=UGPase" title="UGPase">UGPase</a>, <a href="https://publications.waset.org/abstracts/search?q=LkUGPase" title=" LkUGPase"> LkUGPase</a>, <a href="https://publications.waset.org/abstracts/search?q=RwUGPase" title=" RwUGPase"> RwUGPase</a>, <a href="https://publications.waset.org/abstracts/search?q=UDP-glucose" title=" UDP-glucose"> UDP-glucose</a>, <a href="https://publications.waset.org/abstracts/search?q=Glycosylation" title=" Glycosylation"> Glycosylation</a> </p> <a href="https://publications.waset.org/abstracts/192286/cloning-and-characterization-of-uridine-5-diphosphate-glucose-pyrophosphorylases-from-lactobacillus-kefiranofaciens-and-rhodococcus-wratislaviensis" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/192286.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">20</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">2</span> Heat and Mass Transfer in MHD Flow of Nanofluids through a Porous Media Due to a Permeable Stretching Sheet with Viscous Dissipation and Chemical Reaction Effects</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Yohannes%20Yirga">Yohannes Yirga</a>, <a href="https://publications.waset.org/abstracts/search?q=Daniel%20Tesfay"> Daniel Tesfay</a> </p> <p class="card-text"><strong>Abstract:</strong></p> The convective heat and mass transfer in nanofluid flow through a porous media due to a permeable stretching sheet with magnetic field, viscous dissipation, and chemical reaction and Soret effects are numerically investigated. Two types of nanofluids, namely Cu-water and Ag-water were studied. The governing boundary layer equations are formulated and reduced to a set of ordinary differential equations using similarity transformations and then solved numerically using the Keller box method. Numerical results are obtained for the skin friction coefficient, Nusselt number and Sherwood number as well as for the velocity, temperature and concentration profiles for selected values of the governing parameters. Excellent validation of the present numerical results has been achieved with the earlier linearly stretching sheet problems in the literature. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=heat%20and%20mass%20transfer" title="heat and mass transfer">heat and mass transfer</a>, <a href="https://publications.waset.org/abstracts/search?q=magnetohydrodynamics" title=" magnetohydrodynamics"> magnetohydrodynamics</a>, <a href="https://publications.waset.org/abstracts/search?q=nanofluid" title=" nanofluid"> nanofluid</a>, <a href="https://publications.waset.org/abstracts/search?q=fluid%20dynamics" title=" fluid dynamics"> fluid dynamics</a> </p> <a href="https://publications.waset.org/abstracts/4910/heat-and-mass-transfer-in-mhd-flow-of-nanofluids-through-a-porous-media-due-to-a-permeable-stretching-sheet-with-viscous-dissipation-and-chemical-reaction-effects" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/4910.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">291</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">1</span> Biosynthesis of L-Xylose from Xylitol Using a Dual Enzyme Cascade in Escherichia coli</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Mesfin%20Angaw%20Tesfay">Mesfin Angaw Tesfay</a> </p> <p class="card-text"><strong>Abstract:</strong></p> L-xylose is an important intermediate in the pharmaceutical industry, playing a key role in the production of various antiviral and anticancer drugs. Despite its significance, L-xylose is a rare and costly sugar with limited availability in nature. In recent years, enzymatic production methods have garnered considerable attention due to their benefits over conventional chemical synthesis. In this research, a dual enzyme cascade system was developed to synthesize L-xylose from an inexpensive substrate, xylitol. The study involved cloning and co-expressing two key genes: the L-fucose isomerase (L-fucI) gene from Escherichia coli K-12 and the xylitol-4-dehydrogenase (xdh) gene from Pantoea ananatis ATCC 43072 in Escherichia coli. The resulting recombinant cells, engineered with the PET28a-xdh/L-fucI vector, were able to effectively convert xylitol to L-xylose. The system showed optimal performance at 40°C and a pH of 10.0. Moreover, Zn²⁺ (7.5 mM) enhanced the catalytic activity by 1.34 times. This approach yielded 52.2 g/L of L-xylose from an initial 80 g/L xylitol concentration, with a 65% conversion efficiency and a productivity rate of 1.86. The study highlights a practical method for producing L-xylose from xylitol through a co-expression system carrying the L-fucI and xdh genes. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=l-fucose%20isomerase" title="l-fucose isomerase">l-fucose isomerase</a>, <a href="https://publications.waset.org/abstracts/search?q=xylitol-4-dehydrogenase" title=" xylitol-4-dehydrogenase"> xylitol-4-dehydrogenase</a>, <a href="https://publications.waset.org/abstracts/search?q=l-xylose" title=" l-xylose"> l-xylose</a>, <a href="https://publications.waset.org/abstracts/search?q=xylitol" title=" xylitol"> xylitol</a>, <a href="https://publications.waset.org/abstracts/search?q=co-expression" title=" co-expression"> co-expression</a> </p> <a href="https://publications.waset.org/abstracts/192338/biosynthesis-of-l-xylose-from-xylitol-using-a-dual-enzyme-cascade-in-escherichia-coli" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/192338.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">25</span> </span> </div> </div> </div> </main> <footer> <div id="infolinks" class="pt-3 pb-2"> <div class="container"> <div style="background-color:#f5f5f5;" class="p-3"> <div class="row"> <div class="col-md-2"> <ul class="list-unstyled"> About <li><a href="https://waset.org/page/support">About Us</a></li> <li><a href="https://waset.org/page/support#legal-information">Legal</a></li> <li><a target="_blank" rel="nofollow" href="https://publications.waset.org/static/files/WASET-16th-foundational-anniversary.pdf">WASET celebrates its 16th foundational anniversary</a></li> </ul> </div> <div class="col-md-2"> <ul class="list-unstyled"> Account <li><a href="https://waset.org/profile">My Account</a></li> </ul> </div> <div class="col-md-2"> <ul class="list-unstyled"> Explore <li><a href="https://waset.org/disciplines">Disciplines</a></li> <li><a href="https://waset.org/conferences">Conferences</a></li> <li><a href="https://waset.org/conference-programs">Conference Program</a></li> <li><a href="https://waset.org/committees">Committees</a></li> <li><a href="https://publications.waset.org">Publications</a></li> </ul> </div> <div class="col-md-2"> <ul class="list-unstyled"> Research <li><a href="https://publications.waset.org/abstracts">Abstracts</a></li> <li><a href="https://publications.waset.org">Periodicals</a></li> <li><a href="https://publications.waset.org/archive">Archive</a></li> </ul> </div> <div class="col-md-2"> <ul class="list-unstyled"> Open Science <li><a target="_blank" rel="nofollow" href="https://publications.waset.org/static/files/Open-Science-Philosophy.pdf">Open Science Philosophy</a></li> <li><a target="_blank" rel="nofollow" href="https://publications.waset.org/static/files/Open-Science-Award.pdf">Open Science Award</a></li> <li><a target="_blank" rel="nofollow" href="https://publications.waset.org/static/files/Open-Society-Open-Science-and-Open-Innovation.pdf">Open Innovation</a></li> <li><a target="_blank" rel="nofollow" href="https://publications.waset.org/static/files/Postdoctoral-Fellowship-Award.pdf">Postdoctoral Fellowship Award</a></li> <li><a target="_blank" rel="nofollow" href="https://publications.waset.org/static/files/Scholarly-Research-Review.pdf">Scholarly Research Review</a></li> </ul> </div> <div class="col-md-2"> <ul class="list-unstyled"> Support <li><a href="https://waset.org/page/support">Support</a></li> <li><a href="https://waset.org/profile/messages/create">Contact Us</a></li> <li><a href="https://waset.org/profile/messages/create">Report Abuse</a></li> </ul> </div> </div> </div> </div> </div> <div class="container text-center"> <hr style="margin-top:0;margin-bottom:.3rem;"> <a href="https://creativecommons.org/licenses/by/4.0/" target="_blank" class="text-muted small">Creative Commons Attribution 4.0 International License</a> <div id="copy" class="mt-2">&copy; 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