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protein</title> <meta name="description" content="Search results for: potential protein"> <meta name="keywords" content="potential protein"> <meta name="viewport" content="width=device-width, initial-scale=1, minimum-scale=1, maximum-scale=1, user-scalable=no"> <meta charset="utf-8"> <link href="https://cdn.waset.org/favicon.ico" type="image/x-icon" rel="shortcut icon"> <link href="https://cdn.waset.org/static/plugins/bootstrap-4.2.1/css/bootstrap.min.css" rel="stylesheet"> <link href="https://cdn.waset.org/static/plugins/fontawesome/css/all.min.css" rel="stylesheet"> <link href="https://cdn.waset.org/static/css/site.css?v=150220211555" rel="stylesheet"> </head> <body> <header> <div class="container"> <nav class="navbar navbar-expand-lg navbar-light"> <a class="navbar-brand" href="https://waset.org"> <img src="https://cdn.waset.org/static/images/wasetc.png" alt="Open Science Research Excellence" title="Open Science Research Excellence" /> </a> <button class="d-block d-lg-none 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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="potential protein"> <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> 13247</div> </div> </div> </div> <h1 class="mt-3 mb-3 text-center" style="font-size:1.6rem;">Search results for: potential protein</h1> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">13247</span> The Effect of Sorafenibe on Soat1 Protein by Using Molecular Docking Method</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Mahdiyeh%20Gholaminezhad">Mahdiyeh Gholaminezhad</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Context: The study focuses on the potential impact of Sorafenib on SOAT1 protein in liver cancer treatment, addressing the need for more effective therapeutic options. Research aim: To explore the effects of Sorafenib on the activity of SOAT1 protein in liver cancer cells. Methodology: Molecular docking was employed to analyze the interaction between Sorafenib and SOAT1 protein. Findings: The study revealed a significant effect of Sorafenib on the stability and activity of SOAT1 protein, suggesting its potential as a treatment for liver cancer. Theoretical importance: This research highlights the molecular mechanism underlying Sorafenib's anti-cancer properties, contributing to the understanding of its therapeutic effects. Data collection: Data on the molecular structure of Sorafenib and SOAT1 protein were obtained from computational simulations and databases. Analysis procedures: Molecular docking simulations were performed to predict the binding interactions between Sorafenib and SOAT1 protein. Question addressed: How does Sorafenib influence the activity of SOAT1 protein and what are the implications for liver cancer treatment? Conclusion: The study demonstrates the potential of Sorafenib as a targeted therapy for liver cancer by affecting the activity of SOAT1 protein. Reviewers' Comments: The study provides valuable insights into the molecular basis of Sorafenib's action on SOAT1 protein, suggesting its therapeutic potential. To enhance the methodology, the authors could consider validating the docking results with experimental data for further validation. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=liver%20cancer" title="liver cancer">liver cancer</a>, <a href="https://publications.waset.org/abstracts/search?q=sorafenib" title=" sorafenib"> sorafenib</a>, <a href="https://publications.waset.org/abstracts/search?q=SOAT1" title=" SOAT1"> SOAT1</a>, <a href="https://publications.waset.org/abstracts/search?q=molecular%20docking" title=" molecular docking"> molecular docking</a> </p> <a href="https://publications.waset.org/abstracts/189263/the-effect-of-sorafenibe-on-soat1-protein-by-using-molecular-docking-method" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/189263.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">26</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">13246</span> Protein and Lipid Extraction from Microalgae with Ultrasound Assisted Osmotic Shock Method</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Nais%20Pinta%20Adetya">Nais Pinta Adetya</a>, <a href="https://publications.waset.org/abstracts/search?q=H.%20Hadiyanto"> H. Hadiyanto</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Microalgae has a potential to be utilized as food and natural colorant. The microalgae components consists of three main parts, these are lipid, protein, and carbohydrate. Crucial step in producing lipid and protein from microalgae is extraction. Microalgae has high water level (70-90%), it causes drying process of biomass needs much more energy and also has potential to distract lipid and protein from microalgae. Extraction of lipid from wet biomass is able to take place efficiently with cell disruption of microalgae by osmotic shock method. In this study, osmotic shock method was going to be integrated with ultrasound to maximalize the extraction yield of lipid and protein from wet biomass Spirulina sp. with osmotic shock method assisted ultrasound. This study consisted of two steps, these were osmotic shock process toward wet biomass and ultrasound extraction assisted. NaCl solution was used as osmotic agent, with the variation of concentrations were 10%, 20%, and 30%. Extraction was conducted in 40°C for 20 minutes with frequency of ultrasound wave was 40kHz. The optimal yield of protein (2.7%) and (lipid 38%) were achieved at 20% osmotic agent concentration. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=extraction" title="extraction">extraction</a>, <a href="https://publications.waset.org/abstracts/search?q=lipid" title=" lipid"> lipid</a>, <a href="https://publications.waset.org/abstracts/search?q=osmotic%20shock" title=" osmotic shock"> osmotic shock</a>, <a href="https://publications.waset.org/abstracts/search?q=protein" title=" protein"> protein</a>, <a href="https://publications.waset.org/abstracts/search?q=ultrasound" title=" ultrasound"> ultrasound</a> </p> <a href="https://publications.waset.org/abstracts/76886/protein-and-lipid-extraction-from-microalgae-with-ultrasound-assisted-osmotic-shock-method" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/76886.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">359</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">13245</span> Lentil Protein Fortification in Cranberry Squash</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Sandhya%20Devi%20A">Sandhya Devi A</a> </p> <p class="card-text"><strong>Abstract:</strong></p> The protein content of the cranberry squash (protein: 0g) may be increased by extracting protein from the lentils (9 g), which is particularly linked to a lower risk of developing heart disease. Using the technique of alkaline extraction from the lentils flour, protein may be extracted. Alkaline extraction of protein from lentil flour was optimized utilizing response surface approach in order to maximize both protein content and yield. Cranberry squash may be taken if a protein fortification syrup is prepared and processed into the squash. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=alkaline%20extraction" title="alkaline extraction">alkaline extraction</a>, <a href="https://publications.waset.org/abstracts/search?q=cranberry%20squash" title=" cranberry squash"> cranberry squash</a>, <a href="https://publications.waset.org/abstracts/search?q=protein%20fortification" title=" protein fortification"> protein fortification</a>, <a href="https://publications.waset.org/abstracts/search?q=response%20surface%20methodology" title=" response surface methodology"> response surface methodology</a> </p> <a href="https://publications.waset.org/abstracts/153178/lentil-protein-fortification-in-cranberry-squash" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/153178.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">111</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">13244</span> Hydration of Protein-RNA Recognition Sites</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Amita%20Barik">Amita Barik</a>, <a href="https://publications.waset.org/abstracts/search?q=Ranjit%20Prasad%20Bahadur"> Ranjit Prasad Bahadur</a> </p> <p class="card-text"><strong>Abstract:</strong></p> We investigate the role of water molecules in 89 protein-RNA complexes taken from the Protein Data Bank. Those with tRNA and single-stranded RNA are less hydrated than with duplex or ribosomal proteins. Protein-RNA interfaces are hydrated less than protein-DNA interfaces, but more than protein-protein interfaces. Majority of the waters at protein-RNA interfaces makes multiple H-bonds; however, a fraction does not make any. Those making Hbonds have preferences for the polar groups of RNA than its partner protein. The spatial distribution of waters makes interfaces with ribosomal proteins and single-stranded RNA relatively ‘dry’ than interfaces with tRNA and duplex RNA. In contrast to protein-DNA interfaces, mainly due to the presence of the 2’OH, the ribose in protein-RNA interfaces is hydrated more than the phosphate or the bases. The minor groove in protein-RNA interfaces is hydrated more than the major groove, while in protein-DNA interfaces it is reverse. The strands make the highest number of water-mediated H-bonds per unit interface area followed by the helices and the non-regular structures. The preserved waters at protein-RNA interfaces make higher number of H-bonds than the other waters. Preserved waters contribute toward the affinity in protein-RNA recognition and should be carefully treated while engineering protein-RNA interfaces. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=h-bonds" title="h-bonds">h-bonds</a>, <a href="https://publications.waset.org/abstracts/search?q=minor-major%20grooves" title=" minor-major grooves"> minor-major grooves</a>, <a href="https://publications.waset.org/abstracts/search?q=preserved%20water" title=" preserved water"> preserved water</a>, <a href="https://publications.waset.org/abstracts/search?q=protein-RNA%20interfaces" title=" protein-RNA interfaces"> protein-RNA interfaces</a> </p> <a href="https://publications.waset.org/abstracts/42932/hydration-of-protein-rna-recognition-sites" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/42932.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">302</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">13243</span> Protein Crystallization Induced by Surface Plasmon Resonance</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Tetsuo%20Okutsu">Tetsuo Okutsu</a> </p> <p class="card-text"><strong>Abstract:</strong></p> We have developed a crystallization plate with the function of promoting protein crystallization. A gold thin film is deposited on the crystallization plate. A protein solution is dropped thereon, and crystallization is promoted when the protein is irradiated with light of a wavelength that protein does not absorb. Protein is densely adsorbed on the gold thin film surface. The light excites the surface plasmon resonance of the gold thin film, the protein is excited by the generated enhanced electric field induced by surface plasmon resonance, and the amino acid residues are radicalized to produce protein dimers. The dimers function as templates for protein crystals, crystallization is promoted. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=lysozyme" title="lysozyme">lysozyme</a>, <a href="https://publications.waset.org/abstracts/search?q=plasmon" title=" plasmon"> plasmon</a>, <a href="https://publications.waset.org/abstracts/search?q=protein" title=" protein"> protein</a>, <a href="https://publications.waset.org/abstracts/search?q=crystallization" title=" crystallization"> crystallization</a>, <a href="https://publications.waset.org/abstracts/search?q=RNaseA" title=" RNaseA"> RNaseA</a> </p> <a href="https://publications.waset.org/abstracts/85433/protein-crystallization-induced-by-surface-plasmon-resonance" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/85433.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">218</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">13242</span> A Novel Protein Elicitor Extracted From Lecanicillium lecanii Induced Resistance Against Whitefly, Bemisia tabaci in Cotton</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Yusuf%20Ali%20Abdulle">Yusuf Ali Abdulle</a>, <a href="https://publications.waset.org/abstracts/search?q=Azhar%20Uddin%20Keerio"> Azhar Uddin Keerio</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Background: Protein elicitors play a key role in signaling or displaying plant defense mechanisms and emerging as vital tools for bio-control of insects. This study was aimed at the characterization of the novel protein elicitor isolated from entomopathogenic fungi Lecanicillium lecanii (V3) strain and its activity against Whitefly, Bemisia tabaci in cotton. The sequence of purified elicitor protein showed 100% similarity with hypothetical protein LEL_00878 [Cordyceps confragosa RCEF 1005], GenBank no (OAA81333.1). This novel protein elicitor has 253 amino acid residues and 762bp with a molecular mass of 29 kDa. The protein recombinant was expressed in Escherichia coli using pET‐28a (+) plasmid. Effects of purified novel protein elicitor on Bemisia tabaci were determined at three concentrations of protein (i.e., 58.32, 41.22, 35.41 μg mL⁻¹) on cotton plants and were exposed to newly molted adult B.tabaci. Bioassay results showed a significant effect of the exogenous application of novel protein elicitor on B. tabaci in cotton. In addition, the gene expression analysis found a significant up-regulation of the major genes associated with salicylic acid (SA) and jasmonic acid (JA) linked plant defense pathways in elicitor protein-treated plants. Our results suggested the potential application of a novel protein elicitor derived from Lecanicillium lecanii as a future bio-intensive controlling approach against the whitefly, Bemisia tabaci. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=resistance" title="resistance">resistance</a>, <a href="https://publications.waset.org/abstracts/search?q=Lecanicillium%20lecanii" title=" Lecanicillium lecanii"> Lecanicillium lecanii</a>, <a href="https://publications.waset.org/abstracts/search?q=secondary%20metabolites" title=" secondary metabolites"> secondary metabolites</a>, <a href="https://publications.waset.org/abstracts/search?q=whitefly" title=" whitefly"> whitefly</a> </p> <a href="https://publications.waset.org/abstracts/151545/a-novel-protein-elicitor-extracted-from-lecanicillium-lecanii-induced-resistance-against-whitefly-bemisia-tabaci-in-cotton" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/151545.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">184</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">13241</span> Bioinformatics and Molecular Biological Characterization of a Hypothetical Protein SAV1226 as a Potential Drug Target for Methicillin/Vancomycin-Staphylococcus aureus Infections</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Nichole%20Haag">Nichole Haag</a>, <a href="https://publications.waset.org/abstracts/search?q=Kimberly%20Velk"> Kimberly Velk</a>, <a href="https://publications.waset.org/abstracts/search?q=Tyler%20McCune"> Tyler McCune</a>, <a href="https://publications.waset.org/abstracts/search?q=Chun%20Wu"> Chun Wu</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Methicillin/multiple-resistant Staphylococcus aureus (MRSA) are infectious bacteria that are resistant to common antibiotics. A previous in silico study in our group has identified a hypothetical protein SAV1226 as one of the potential drug targets. In this study, we reported the bioinformatics characterization, as well as cloning, expression, purification and kinetic assays of hypothetical protein SAV1226 from methicillin/vancomycin-resistant Staphylococcus aureus Mu50 strain. MALDI-TOF/MS analysis revealed a low degree of structural similarity with known proteins. Kinetic assays demonstrated that hypothetical protein SAV1226 is neither a domain of an ATP dependent dihydroxyacetone kinase nor of a phosphotransferase system (PTS) dihydroxyacetone kinase, suggesting that the function of hypothetical protein SAV1226 might be misannotated on public databases such as UniProt and InterProScan 5. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=Methicillin-resistant%20Staphylococcus%20aureus" title="Methicillin-resistant Staphylococcus aureus">Methicillin-resistant Staphylococcus aureus</a>, <a href="https://publications.waset.org/abstracts/search?q=dihydroxyacetone%20kinase" title=" dihydroxyacetone kinase"> dihydroxyacetone kinase</a>, <a href="https://publications.waset.org/abstracts/search?q=essential%20genes" title=" essential genes"> essential genes</a>, <a href="https://publications.waset.org/abstracts/search?q=drug%20target" title=" drug target"> drug target</a>, <a href="https://publications.waset.org/abstracts/search?q=phosphoryl%20group%20donor" title=" phosphoryl group donor"> phosphoryl group donor</a> </p> <a href="https://publications.waset.org/abstracts/21705/bioinformatics-and-molecular-biological-characterization-of-a-hypothetical-protein-sav1226-as-a-potential-drug-target-for-methicillinvancomycin-staphylococcus-aureus-infections" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/21705.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">407</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">13240</span> Antifungal Protein ~35kDa Produced by Bacillus cereus Inhibits the Growth of Some Molds and Yeasts</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Saleh%20H.%20Salmen">Saleh H. Salmen</a>, <a href="https://publications.waset.org/abstracts/search?q=Sulaiman%20Ali%20Alharbi"> Sulaiman Ali Alharbi</a>, <a href="https://publications.waset.org/abstracts/search?q=Hany%20M.%20Yehia"> Hany M. Yehia</a>, <a href="https://publications.waset.org/abstracts/search?q=Mohammad%20A.%20Khiyami"> Mohammad A. Khiyami</a>, <a href="https://publications.waset.org/abstracts/search?q=Milton%20Wainwright"> Milton Wainwright</a>, <a href="https://publications.waset.org/abstracts/search?q=Naiyf%20S.%20Alharbi"> Naiyf S. Alharbi</a>, <a href="https://publications.waset.org/abstracts/search?q=Arunachalam%20Chinnathambi"> Arunachalam Chinnathambi</a> </p> <p class="card-text"><strong>Abstract:</strong></p> An antifungal protein synthesized by Bacillus cereus has been partially purified by the use of ammonium sulfate precipitation and Sephadex-G-200 column chromatography. The protein was produced from Bacillus cereus grown in potato Dextrose Broth Medium (PDB) at 30 ºC for 3 days at 100 rpm. The protein showed antagonistic effect against some fungi and yeasts. Crude extract from medium and semi-purified protein were tested in vitro against both fungi and yeasts using the disc diffusion method in order to detect the inhibitory effect of the protein. Zones of inhibition of the following diameter were found (mm) were Alternaria alternate (28), Rhodotorula glutinis (20), Fusarium sp. (16), Rhizopus sp. (15), Penicillium digitatum (13), Mucor sp. (13) and Aspergillus niger (10). The isolated protein was found to have a molecular weight of ~35kDa by sodium deodecyl sulfate-poly acrylamide gel electrophoresis. The data showed that the protein of Bacillus cereus has antifungal activity, a fact which points to the possibility of using it as a bio-control agent against some fungi, findings which emphasize the potential role of B. cereus as an important bio-control agent. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=bacillus%20cereus" title="bacillus cereus">bacillus cereus</a>, <a href="https://publications.waset.org/abstracts/search?q=~35kDa%20protein" title=" ~35kDa protein"> ~35kDa protein</a>, <a href="https://publications.waset.org/abstracts/search?q=molds" title=" molds"> molds</a>, <a href="https://publications.waset.org/abstracts/search?q=yeasts" title=" yeasts"> yeasts</a> </p> <a href="https://publications.waset.org/abstracts/3422/antifungal-protein-35kda-produced-by-bacillus-cereus-inhibits-the-growth-of-some-molds-and-yeasts" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/3422.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">13239</span> Myeloid Zinc Finger 1/Ets-Like Protein-1/Protein Kinase C Alpha Associated with Poor Prognosis in Patients with Hepatocellular Carcinoma</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Jer-Yuh%20Liu">Jer-Yuh Liu</a>, <a href="https://publications.waset.org/abstracts/search?q=Je-Chiuan%20Ye"> Je-Chiuan Ye</a>, <a href="https://publications.waset.org/abstracts/search?q=Jin-Ming%20Hwang"> Jin-Ming Hwang</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Protein kinase C alpha (PKCα) is a key signaling molecule in human cancer development. As a therapeutic strategy, targeting PKCα is difficult because the molecule is ubiquitously expressed in non-malignant cells. PKCα is regulated by the cooperative interaction of the transcription factors myeloid zinc finger 1 (MZF-1) and Ets-like protein-1 (Elk-1) in human cancer cells. By conducting tissue array analysis, herein, we determined the protein expression of MZF-1/Elk-1/PKCα in various cancers. The data show that the expression of MZF-1/Elk-1 is correlated with that of PKCα in hepatocellular carcinoma (HCC), but not in bladder and lung cancers. In addition, the PKCα down-regulation by shRNA Elk-1 was only observed in the HCC SK-Hep-1 cells. Blocking the interaction between MZF-1 and Elk-1 through the transfection of their binding domain MZF-160–72 decreased PKCα expression. This step ultimately depressed the epithelial-mesenchymal transition potential of the HCC cells. These findings could be used to develop an alternative therapeutic strategy for patients with the PKCα-derived HCC. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=protein%20kinase%20C%20alpha" title="protein kinase C alpha">protein kinase C alpha</a>, <a href="https://publications.waset.org/abstracts/search?q=myeloid%20zinc%20finger%201" title=" myeloid zinc finger 1"> myeloid zinc finger 1</a>, <a href="https://publications.waset.org/abstracts/search?q=ets-like%20protein-1" title=" ets-like protein-1"> ets-like protein-1</a>, <a href="https://publications.waset.org/abstracts/search?q=hepatocellular%20carcinoma" title=" hepatocellular carcinoma"> hepatocellular carcinoma</a> </p> <a href="https://publications.waset.org/abstracts/78123/myeloid-zinc-finger-1ets-like-protein-1protein-kinase-c-alpha-associated-with-poor-prognosis-in-patients-with-hepatocellular-carcinoma" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/78123.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">227</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">13238</span> Protein Remote Homology Detection and Fold Recognition by Combining Profiles with Kernel Methods</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Bin%20Liu">Bin Liu</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Protein remote homology detection and fold recognition are two most important tasks in protein sequence analysis, which is critical for protein structure and function studies. In this study, we combined the profile-based features with various string kernels, and constructed several computational predictors for protein remote homology detection and fold recognition. Experimental results on two widely used benchmark datasets showed that these methods outperformed the competing methods, indicating that these predictors are useful computational tools for protein sequence analysis. By analyzing the discriminative features of the training models, some interesting patterns were discovered, reflecting the characteristics of protein superfamilies and folds, which are important for the researchers who are interested in finding the patterns of protein folds. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=protein%20remote%20homology%20detection" title="protein remote homology detection">protein remote homology detection</a>, <a href="https://publications.waset.org/abstracts/search?q=protein%20fold%20recognition" title=" protein fold recognition"> protein fold recognition</a>, <a href="https://publications.waset.org/abstracts/search?q=profile-based%20features" title=" profile-based features"> profile-based features</a>, <a href="https://publications.waset.org/abstracts/search?q=Support%20Vector%20Machines%20%28SVMs%29" title=" Support Vector Machines (SVMs)"> Support Vector Machines (SVMs)</a> </p> <a href="https://publications.waset.org/abstracts/104054/protein-remote-homology-detection-and-fold-recognition-by-combining-profiles-with-kernel-methods" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/104054.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">161</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">13237</span> Membrane Spanning DNA Origami Nanopores for Protein Translocation</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Genevieve%20Pugh">Genevieve Pugh</a>, <a href="https://publications.waset.org/abstracts/search?q=Johnathan%20Burns"> Johnathan Burns</a>, <a href="https://publications.waset.org/abstracts/search?q=Stefan%20Howorka"> Stefan Howorka</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Single-molecule sensing via protein nanopores has achieved a step-change in portable and label-free DNA sequencing. However, protein pores of both natural or engineered origin are not able to produce the tunable diameters needed for effective protein sensing. Here, we describe a generic strategy to build synthetic DNA nanopores that are wide enough to accommodate folded protein. The pores are composed of interlinked DNA duplexes and carry lipid anchors to achieve the required membrane insertion. Our demonstrator pore has a contiguous cross-sectional channel area of 50 nm2 which is 6-times larger than the largest protein pore. Consequently, transport of folded protein across bilayers is possible. The modular design is amenable for different pore dimensions and can be adapted for protein sensing or to create molecular gates in synthetic biology. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=biosensing" title="biosensing">biosensing</a>, <a href="https://publications.waset.org/abstracts/search?q=DNA%20nanotechnology" title=" DNA nanotechnology"> DNA nanotechnology</a>, <a href="https://publications.waset.org/abstracts/search?q=DNA%20origami" title=" DNA origami"> DNA origami</a>, <a href="https://publications.waset.org/abstracts/search?q=nanopore%20sensing" title=" nanopore sensing"> nanopore sensing</a> </p> <a href="https://publications.waset.org/abstracts/78556/membrane-spanning-dna-origami-nanopores-for-protein-translocation" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/78556.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">324</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">13236</span> Physicochemical and Functional Characteristics of Hemp Protein Isolate</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=El-Sohaimy%20Sobhy%20A.">El-Sohaimy Sobhy A.</a>, <a href="https://publications.waset.org/abstracts/search?q=Androsova%20Natalia"> Androsova Natalia</a>, <a href="https://publications.waset.org/abstracts/search?q=Toshev%20Abuvali%20Djabarovec"> Toshev Abuvali Djabarovec</a> </p> <p class="card-text"><strong>Abstract:</strong></p> The conditions of the isolation of proteins from the hemp seeds were optimized in the current work. Moreover, the physicochemical and functional properties of hemp protein isolate were evaluated for its potential application in food manufacturing. The elastin protein is the most predominant protein in the protein profile with a molecular weight of 58.1 KDa, besides albumin, with a molecular weight of 31.5 KDa. The FTIR spectrum detected the absorption peaks of the amide I in 1750 and 1600 cm⁻¹, which pointed to C=O stretching while N-H was stretching at 1650-1580 cm⁻¹. The peak at 3250 was related to N-H stretching of primary aliphatic amine (3400-3300 cm⁻¹), and the N-H stretching for secondary (II) amine appeared at 3350-3310 cm⁻¹. Hemp protein isolate (HPI) was showed high content of arginine (15.52 g/100 g), phenylalanine+tyrosine (9.63 g/100 g), methionine + cysteine (5.49 g/100 g), leucine + isoleucine (5.21 g/100 g) and valine (4.53 g/100 g). It contains a moderate level of threonine (3.29 g/100 g) and lysine (2.50 g/100 g), with the limiting amino acid being a tryptophan (0.22 g/100 g HPI). HPI showed high water-holding capacity (4.5 ± 2.95 ml/g protein) and oil holding capacity (2.33 ± 1.88 ml/g) values. The foaming capacity of HPI was increased with increasing the pH values to reach the maximum value at pH 11 (67.23±3.20 %). The highest emulsion ability index of HPI was noted at pH 9 (91.3±2.57 m2/g) with low stability (19.15±2.03). <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=Cannabis%20sativa%20ssp." title="Cannabis sativa ssp.">Cannabis sativa ssp.</a>, <a href="https://publications.waset.org/abstracts/search?q=protein%20isolate" title=" protein isolate"> protein isolate</a>, <a href="https://publications.waset.org/abstracts/search?q=isolation%20conditions" title=" isolation conditions"> isolation conditions</a>, <a href="https://publications.waset.org/abstracts/search?q=amino%20acid%20composition" title=" amino acid composition"> amino acid composition</a>, <a href="https://publications.waset.org/abstracts/search?q=chemical%20properties" title=" chemical properties"> chemical properties</a>, <a href="https://publications.waset.org/abstracts/search?q=functional%20properties" title=" functional properties"> functional properties</a> </p> <a href="https://publications.waset.org/abstracts/150400/physicochemical-and-functional-characteristics-of-hemp-protein-isolate" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/150400.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">180</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">13235</span> Development of Protein-based Emulsion Gels For Food Structuring</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Baigts-Allende%20Diana">Baigts-Allende Diana</a>, <a href="https://publications.waset.org/abstracts/search?q=Klojdov%C3%A1%20Iveta"> Klojdová Iveta</a>, <a href="https://publications.waset.org/abstracts/search?q=Kozlu%20Ali"> Kozlu Ali</a>, <a href="https://publications.waset.org/abstracts/search?q=Metri-ojeda%20Jorge"> Metri-ojeda Jorge</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Emulsion gels are constituted by a colloidal system (emulsion) stabilized by a polymeric gel matrix. These systems are more homogeneous and stable than conventional emulsions and can behave as either gel-like or soft-solid. Protein-based emulsion gels (PEG) have been used as carrier systems of bioactive compounds and as food structuring to improve the texture and consistency, mainly in producing low-fat content products. This work studied the effect of protein: polysaccharide ratio 0.75:1.25, 1:1, and 1.25:0.75 (levels -1, 0, and +1) and pH values (2-9) on the stability of protein-based emulsion gels using soy protein isolate and sodium alginate. Protein emulsion capacity was enhaced with increased pH (6,7,8 and 9) compared to acid pH values. The smaller particle size for PEG was at pH 9 (~23µm); however, with increasing protein ratio (level +1), higher particle size was observed (~23µm). The same trend was observed for rheological measurements; the consistency index (K) increased at pH 9 for level -1 (1.17) in comparison to level +1 (0.45). The studied PEG showed good thermal stability at neutral and pH 9 (~98 %) for all biopolymer ratios. Optimal conditions in pH and biopolymer ratios were determined for PEG using soy protein and sodium alginate ingredients with potential use in elaborating stable systems for broad application in the food sector. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=emulsion%20gels" title="emulsion gels">emulsion gels</a>, <a href="https://publications.waset.org/abstracts/search?q=food%20structuring" title=" food structuring"> food structuring</a>, <a href="https://publications.waset.org/abstracts/search?q=biopolymers" title=" biopolymers"> biopolymers</a>, <a href="https://publications.waset.org/abstracts/search?q=food%20systems" title=" food systems"> food systems</a> </p> <a href="https://publications.waset.org/abstracts/175400/development-of-protein-based-emulsion-gels-for-food-structuring" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/175400.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">74</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">13234</span> Potential Use of Cnidoscolus Chayamansa Leaf from Mexico as High-Quality Protein Source</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Diana%20Karina%20Baigts%20Allende">Diana Karina Baigts Allende</a>, <a href="https://publications.waset.org/abstracts/search?q=Mariana%20%20Gonzalez%20Diaz"> Mariana Gonzalez Diaz</a>, <a href="https://publications.waset.org/abstracts/search?q=Luis%20Antonio%20Chel%20Guerrero"> Luis Antonio Chel Guerrero</a>, <a href="https://publications.waset.org/abstracts/search?q=Mukthar%20Sandoval%20Peraza"> Mukthar Sandoval Peraza</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Poverty and food insecurity are still incident problems in the developing countries, where population´s diet is based on cereals which are lack in protein content. Nevertheless, during last years the use of native plants has been studied as an alternative source of protein in order to improve the nutritional intake. Chaya crop also called Spinach tree, is a prehispanic plant native from Central America and South of Mexico (Mayan culture), which has been especially valued due to its high nutritional content particularly protein and some medicinal properties. The aim of this work was to study the effect of protein isolation processing from Chaya leaf harvest in Yucatan, Mexico on its structure quality in order: i) to valorize the Chaya crop and ii) to produce low-cost and high-quality protein. Chaya leaf was extruded, clarified and recovered using: a) acid precipitation by decreasing the pH value until reach the isoelectric point (3.5) and b) thermal coagulation, by heating the protein solution at 80 °C during 30 min. Solubilized protein was re-dissolved in water and spray dried. The presence of Fraction I protein, known as RuBisCO (Rubilose-1,5-biphosfate carboxylase/oxygenase) was confirmed by gel electrophoresis (SDS-PAGE) where molecular weight bands of 55 KDa and 12 KDa were observed. The infrared spectrum showed changes in protein structure due to the isolation method. The use of high temperatures (thermal coagulation) highly decreased protein solubility in comparison to isoelectric precipitated protein, the nutritional properties according to amino acid profile was also disturbed, showing minor amounts of overall essential amino acids from 435.9 to 367.8 mg/g. Chaya protein isolate obtained by acid precipitation showed higher protein quality according to essential amino acid score compared to FAO recommendations, which could represent an important sustainable source of protein for human consumption. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=chaya%20leaf" title="chaya leaf">chaya leaf</a>, <a href="https://publications.waset.org/abstracts/search?q=nutritional%20properties" title=" nutritional properties"> nutritional properties</a>, <a href="https://publications.waset.org/abstracts/search?q=protein%20isolate" title=" protein isolate"> protein isolate</a>, <a href="https://publications.waset.org/abstracts/search?q=protein%20structure" title=" protein structure"> protein structure</a> </p> <a href="https://publications.waset.org/abstracts/56439/potential-use-of-cnidoscolus-chayamansa-leaf-from-mexico-as-high-quality-protein-source" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/56439.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">341</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">13233</span> Functional Properties of Sunflower Protein Concentrates Extracted Using Different Anti-greening Agents - Low-Fat Whipping Cream Preparation</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Tamer%20M.%20El-Messery">Tamer M. El-Messery</a> </p> <p class="card-text"><strong>Abstract:</strong></p> By-products from sunflower oil extraction, such as sunflower cakes, are rich sources of proteins with desirable functional properties for the food industry. However, challenges such as sensory drawbacks and the presence of phenolic compounds have hindered their widespread use. In this study, sunflower protein concentrates were obtained from sunflower cakes using different ant-greening solvents (ascorbic acid (ASC) and N-acetylcysteine (NAC)), and their functional properties were evaluated. The color of extracted proteins ranged from dark green to yellow, where the using of ASC and NAC agents enhanced the color. The protein concentrates exhibited high solubility (>70%) and antioxidant activity, with hydrophobicity influencing emulsifying activity. Emulsions prepared with these proteins showed stability and microencapsulation efficiency. Incorporation of protein concentrates into low-fat whipping cream formulations increased overrun and affected color characteristics. Rheological studies demonstrated pseudoplastic behavior in whipped cream, influenced by shear rates and protein content. Overall, sunflower protein isolates showed promising functional properties, indicating their potential as valuable ingredients in food formulations. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=functional%20properties" title="functional properties">functional properties</a>, <a href="https://publications.waset.org/abstracts/search?q=sunflower%20protein%20concentrates" title=" sunflower protein concentrates"> sunflower protein concentrates</a>, <a href="https://publications.waset.org/abstracts/search?q=antioxidant%20capacity" title=" antioxidant capacity"> antioxidant capacity</a>, <a href="https://publications.waset.org/abstracts/search?q=ant-greening%20agents" title=" ant-greening agents"> ant-greening agents</a>, <a href="https://publications.waset.org/abstracts/search?q=low-fat%20whipping%20cream" title=" low-fat whipping cream"> low-fat whipping cream</a> </p> <a href="https://publications.waset.org/abstracts/185953/functional-properties-of-sunflower-protein-concentrates-extracted-using-different-anti-greening-agents-low-fat-whipping-cream-preparation" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/185953.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">48</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">13232</span> Synthesis and Molecular Docking Studies of Hydrazone Derivatives Potent Inhibitors as a Human Carbonic Anhydrase IX</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Sema%20%C5%9Eeno%C4%9Flu">Sema Şenoğlu</a>, <a href="https://publications.waset.org/abstracts/search?q=Sevgi%20Karaku%C5%9F"> Sevgi Karakuş</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Hydrazone scaffold is important to design new drug groups and is found to possess numerous uses in pharmaceutical chemistry. Besides, hydrazone derivatives are also known for biological activities such as anticancer, antimicrobial, antiviral, and antifungal. Hydrazone derivatives are promising anticancer agents because they inhibit cancer proliferation and induce apoptosis. Human carbonic anhydrase IX has a high potential to be an antiproliferative drug target, and targeting this protein is also important for obtaining potential anticancer inhibitors. The protein construct was retrieved as a PDB file from the RCSB protein database. This binding interaction of proteins and ligands was performed using Discovery Studio Visualizer. In vitro inhibitory activity of hydrazone derivatives was tested against enzyme carbonic anhydrase IX on the PyRx programme. Most of these molecules showed remarkable human carbonic anhydrase IX inhibitory activity compared to the acetazolamide. As a result, these compounds appear to be a potential target in drug design against human carbonic anhydrase IX. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=cancer" title="cancer">cancer</a>, <a href="https://publications.waset.org/abstracts/search?q=carbonic%20anhydrase%20IX%20enzyme" title=" carbonic anhydrase IX enzyme"> carbonic anhydrase IX enzyme</a>, <a href="https://publications.waset.org/abstracts/search?q=docking" title=" docking"> docking</a>, <a href="https://publications.waset.org/abstracts/search?q=hydrazone" title=" hydrazone"> hydrazone</a> </p> <a href="https://publications.waset.org/abstracts/171356/synthesis-and-molecular-docking-studies-of-hydrazone-derivatives-potent-inhibitors-as-a-human-carbonic-anhydrase-ix" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/171356.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">82</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">13231</span> Effects of the Natural Compound on SARS-CoV-2 Spike Protein-Mediated Metabolic Alteration in THP-1 Cells Explored by the ¹H-NMR-Based Metabolomics Approach</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Gyaltsen%20Dakpa">Gyaltsen Dakpa</a>, <a href="https://publications.waset.org/abstracts/search?q=K.%20J.%20Senthil%20Kumar"> K. J. Senthil Kumar</a>, <a href="https://publications.waset.org/abstracts/search?q=Nai-Wen%20Tsao"> Nai-Wen Tsao</a>, <a href="https://publications.waset.org/abstracts/search?q=Sheng-Yang%20Wang"> Sheng-Yang Wang</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Context: Coronavirus disease 2019 (COVID-19) is a severe respiratory illness caused by the SARS-CoV-2 virus. One of the hallmarks of COVID-19 is a change in metabolism, which can lead to increased severity and mortality. The mechanism of SARS-CoV-2-mediated perturbations of metabolic pathways has yet to be fully understood. Research Aim: This study aimed to investigate the metabolic alteration caused by SARS-CoV-2 spike protein in Phorbol 12-myristate 13-acetate (PMA)-induced human monocytes (THP-1) and to examine the regulatory effect of natural compounds like Antcins A on SARS-CoV-2 spike protein-induced metabolic alteration. Methodology: The study used a combination of proton nuclear magnetic resonance (1H-NMR) and MetaboAnalyst 5.0 software. THP-1 cells were treated with SARS-CoV-2 spike protein or control, and the metabolomic profiles of the cells were compared. Antcin A was also added to the cells to assess its regulatory effect on SARS-CoV-2 spike protein-induced metabolic alteration. Findings: The study results showed that treatment with SARS-CoV-2 spike protein significantly altered the metabolomic profiles of THP-1 cells. Eight metabolites, including glycerol-phosphocholine, glycine, canadine, sarcosine, phosphoenolpyruvic acid, glutamine, glutamate, and N, N-dimethylglycine, were significantly different between control and spike-protein treatment groups. Antcin A significantly reversed the changes in these metabolites. In addition, treatment with antacid A significantly inhibited SARS-CoV-2 spike protein-mediated up-regulation of TLR-4 and ACE2 receptors. Theoretical Importance The findings of this study suggest that SARS-CoV-2 spike protein can cause significant metabolic alterations in THP-1 cells. Antcin A, a natural compound, has the potential to reverse these metabolic alterations and may be a potential candidate for developing preventive or therapeutic agents for COVID-19. Data Collection: The data for this study was collected from THP-1 cells that were treated with SARS-CoV-2 spike protein or a control. The metabolomic profiles of the cells were then compared using 1H-NMR and MetaboAnalyst 5.0 software. Analysis Procedures: The metabolomic profiles of the THP-1 cells were analyzed using 1H-NMR and MetaboAnalyst 5.0 software. The software was used to identify and quantify the cells' metabolites and compare the control and spike-protein treatment groups. Questions Addressed: The question addressed by this study was whether SARS-CoV-2 spike protein could cause metabolic alterations in THP-1 cells and whether Antcin A can reverse these alterations. Conclusion: The findings of this study suggest that SARS-CoV-2 spike protein can cause significant metabolic alterations in THP-1 cells. Antcin A, a natural compound, has the potential to reverse these metabolic alterations and may be a potential candidate for developing preventive or therapeutic agents for COVID-19. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=SARS-CoV-2-spike" title="SARS-CoV-2-spike">SARS-CoV-2-spike</a>, <a href="https://publications.waset.org/abstracts/search?q=%C2%B9H-NMR" title=" ¹H-NMR"> ¹H-NMR</a>, <a href="https://publications.waset.org/abstracts/search?q=metabolomics" title=" metabolomics"> metabolomics</a>, <a href="https://publications.waset.org/abstracts/search?q=antcin-A" title=" antcin-A"> antcin-A</a>, <a href="https://publications.waset.org/abstracts/search?q=taiwanofungus%20camphoratus" title=" taiwanofungus camphoratus"> taiwanofungus camphoratus</a> </p> <a href="https://publications.waset.org/abstracts/167444/effects-of-the-natural-compound-on-sars-cov-2-spike-protein-mediated-metabolic-alteration-in-thp-1-cells-explored-by-the-1h-nmr-based-metabolomics-approach" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/167444.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">71</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">13230</span> Design and in Slico Study of the Truncated Spike-M-N SARS-CoV-2 as a Novel Effective Vaccine Candidate</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Aghasadeghi%20MR.">Aghasadeghi MR.</a>, <a href="https://publications.waset.org/abstracts/search?q=Bahramali%20G."> Bahramali G.</a>, <a href="https://publications.waset.org/abstracts/search?q=Sadat%20SM."> Sadat SM.</a>, <a href="https://publications.waset.org/abstracts/search?q=Sadeghi%20SA."> Sadeghi SA.</a>, <a href="https://publications.waset.org/abstracts/search?q=Yousefi%20M."> Yousefi M.</a>, <a href="https://publications.waset.org/abstracts/search?q=Khodaei%20K."> Khodaei K.</a>, <a href="https://publications.waset.org/abstracts/search?q=Ghorbani%20M."> Ghorbani M.</a>, <a href="https://publications.waset.org/abstracts/search?q=Sadat%20Larijani%20M."> Sadat Larijani M.</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Background:The emerging COVID-19 pandemic is a serious concernfor the public health worldwide. Despite the many mutations in the virus genome, it is important to find an effective vaccine against viral mutations. Therefore, in current study, we aimed at immunoinformatic evaluation of the virus proteins immunogenicity to design a preventive vaccine candidate, which could elicit humoral and cellular immune responses as well. Methods:Three antigenic regions are included;Spike, Membrane, and Nucleocapsid amino acid sequences were obtained, and possible fusion proteins were assessed andcompared by immunogenicity, structural features, and population coverage. The best fusion protein was also evaluated for MHC-I and MHC-II T-cell epitopes and the linear and conformational B-cell epitopes. Results: Among the four predicted models, the truncated Spike protein in fusion with M and N proteins is composed of 24 highly immunogenic human MHC class I and 29 MHC class II, along with 14 B-cell linear and 61 discontinues epitopes. Also, the selected protein has high antigenicity and acceptable population coverage of 82.95% in Iran and 92.51% in Europe. Conclusion: The data indicate that the truncated Spike-M-N SARS-CoV-2form which could be potential targets of neutralizing antibodies. The protein also has the ability to stimulate humoral and cellular immunity. The in silico study provided the fusion protein as a potential preventive vaccine candidate for further in vivo evaluation. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=SARS-CoV-2" title="SARS-CoV-2">SARS-CoV-2</a>, <a href="https://publications.waset.org/abstracts/search?q=immunoinformatic" title=" immunoinformatic"> immunoinformatic</a>, <a href="https://publications.waset.org/abstracts/search?q=protein" title=" protein"> protein</a>, <a href="https://publications.waset.org/abstracts/search?q=vaccine" title=" vaccine"> vaccine</a> </p> <a href="https://publications.waset.org/abstracts/143821/design-and-in-slico-study-of-the-truncated-spike-m-n-sars-cov-2-as-a-novel-effective-vaccine-candidate" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/143821.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">223</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">13229</span> Effect of Electromagnetic Fields on Protein Extraction from Shrimp By-Products for Electrospinning Process</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Guido%20Trautmann-S%C3%A1ez">Guido Trautmann-Sáez</a>, <a href="https://publications.waset.org/abstracts/search?q=Mario%20P%C3%A9rez-Won"> Mario Pérez-Won</a>, <a href="https://publications.waset.org/abstracts/search?q=Vilbett%20Briones"> Vilbett Briones</a>, <a href="https://publications.waset.org/abstracts/search?q=Mar%C3%ADa%20Jos%C3%A9%20Bugue%C3%B1o"> María José Bugueño</a>, <a href="https://publications.waset.org/abstracts/search?q=Gipsy%20Tabilo-Munizaga"> Gipsy Tabilo-Munizaga</a>, <a href="https://publications.waset.org/abstracts/search?q=Luis%20Gonz%C3%A1les-Cavieres"> Luis Gonzáles-Cavieres</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Shrimp by-products are a valuable source of protein. However, traditional protein extraction methods have limitations in terms of their efficiency. Protein extraction from shrimp (Pleuroncodes monodon) industrial by-products assisted with ohmic heating (OH), microwave (MW) and pulsed electric field (PEF). It was performed by chemical method (using NaOH and HCl 2M) assisted with OH, MW and PEF in a continuous flow system (5 ml/s). Protein determination, differential scanning calorimetry (DSC) and Fourier-transform infrared (FTIR). Results indicate a 19.25% (PEF) 3.65% (OH) and 28.19% (MW) improvement in protein extraction efficiency. The most efficient method was selected for the electrospinning process and obtaining fiber. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=electrospinning%20process" title="electrospinning process">electrospinning process</a>, <a href="https://publications.waset.org/abstracts/search?q=emerging%20technology" title=" emerging technology"> emerging technology</a>, <a href="https://publications.waset.org/abstracts/search?q=protein%20extraction" title=" protein extraction"> protein extraction</a>, <a href="https://publications.waset.org/abstracts/search?q=shrimp%20by-products" title=" shrimp by-products"> shrimp by-products</a> </p> <a href="https://publications.waset.org/abstracts/171420/effect-of-electromagnetic-fields-on-protein-extraction-from-shrimp-by-products-for-electrospinning-process" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/171420.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">90</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">13228</span> Physicochemical Properties of Soy Protein Isolate (SPI): Starch Conjugates Treated by Sonication</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Gulcin%20Yildiz">Gulcin Yildiz</a>, <a href="https://publications.waset.org/abstracts/search?q=Hao%20Feng"> Hao Feng</a> </p> <p class="card-text"><strong>Abstract:</strong></p> In recent years there is growing interested in using soy protein because of several advantages compared to other protein sources, such as high nutritional value, steady supply, and low cost. Soy protein isolate (SPI) is the most refined soy protein product. It contains 90% protein in a moisture-free form and has some desirable functionalities. Creating a protein-polysaccharide conjugate to be the emulsifying agent rather than the protein alone can markedly enhance its stability. This study was undertaken to examine the effects of ultrasound treatments on the physicochemical properties of SPI-starch conjugates. The soy protein isolate (SPI, Pro-Fam® 955) samples were obtained from the Archer Daniels Midland Company. Protein concentrations were analyzed by the Bardford method using BSA as the standard. The volume-weighted mean diameters D [4,3] of protein–polysaccharide conjugates were measured by dynamic light scattering (DLS). Surface hydrophobicity of the conjugates was measured by using 1-anilino-8-naphthalenesulfonate (ANS) (Sigma-Aldrich, St. Louis, MO, USA). Increasing the pH from 2 to 12 resulted in increased protein solubility. The highest solubility was 69.2% for the sample treated with ultrasonication at pH 12, while the lowest (9.13%) was observed in the Control. For the other pH conditions, the protein solubility values ranged from 40.53 to 49.65%. The ultrasound treatment significantly decreased the particle sizes of the SPI-modified starch conjugates. While the D [4,3] for the Control was 731.6 nm, it was 293.7 nm for the samples treated by sonication at pH 12. The surface hydrophobicity (H0) of SPI-starch at all pH conditions were significantly higher than those in the Control. Ultrasonication was proven to be effective in improving the solubility and emulsifying properties of soy protein isolate-starch conjugates. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=particle%20size" title="particle size">particle size</a>, <a href="https://publications.waset.org/abstracts/search?q=solubility" title=" solubility"> solubility</a>, <a href="https://publications.waset.org/abstracts/search?q=soy%20protein%20isolate" title=" soy protein isolate"> soy protein isolate</a>, <a href="https://publications.waset.org/abstracts/search?q=ultrasonication" title=" ultrasonication"> ultrasonication</a> </p> <a href="https://publications.waset.org/abstracts/64023/physicochemical-properties-of-soy-protein-isolate-spi-starch-conjugates-treated-by-sonication" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/64023.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">422</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">13227</span> Effect of Removing Hub Domain on Human CaMKII Isoforms Sensitivity to Calcium/Calmodulin</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Ravid%20Inbar">Ravid Inbar</a> </p> <p class="card-text"><strong>Abstract:</strong></p> CaMKII (calcium-calmodulin dependent protein kinase II) makes up 2% of the protein in our brain and has a critical role in memory formation and long-term potentiation of neurons. Despite this, research has yet to uncover the role of one of the domains on the activation of this kinase. The following proposes to express the protein without the hub domain in E. coli, leaving only the kinase and regulatory segment of the protein. Next, a series of kinase assays will be conducted to elucidate the role the hub domain plays on CaMKII sensitivity to calcium/calmodulin activation. The hub domain may be important for activation; however, it may also be a variety of domains working together to influence protein activation and not the hub alone. Characterization of a protein is critical to the future understanding of the protein's function, as well as for producing pharmacological targets in cases of patients with diseases. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=CaMKII" title="CaMKII">CaMKII</a>, <a href="https://publications.waset.org/abstracts/search?q=hub%20domain" title=" hub domain"> hub domain</a>, <a href="https://publications.waset.org/abstracts/search?q=kinase%20assays" title=" kinase assays"> kinase assays</a>, <a href="https://publications.waset.org/abstracts/search?q=kinase%20%2B%20reg%20seg" title=" kinase + reg seg"> kinase + reg seg</a> </p> <a href="https://publications.waset.org/abstracts/157748/effect-of-removing-hub-domain-on-human-camkii-isoforms-sensitivity-to-calciumcalmodulin" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/157748.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">90</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">13226</span> Fortification of Concentrated Milk Protein Beverages with Soy Proteins: Impact of Divalent Cations and Heating Treatment on the Physical Stability</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Yichao%20Liang">Yichao Liang</a>, <a href="https://publications.waset.org/abstracts/search?q=Biye%20Chen"> Biye Chen</a>, <a href="https://publications.waset.org/abstracts/search?q=Xiang%20Li"> Xiang Li</a>, <a href="https://publications.waset.org/abstracts/search?q=Steven%20R.%20Dimler"> Steven R. Dimler</a> </p> <p class="card-text"><strong>Abstract:</strong></p> This study investigated the effects of adding calcium and magnesium chloride on heat and storage stability of milk protein concentrate-soy protein isolate (8:2 respectively) mixtures containing 10% w/w total protein subjected to the in-container sterilization (115 °C x 15 min). The particle size does not change when emulsions are heated at pH between 6.7 and 7.3 irrespective of the mixed protein ratio. Increasing concentration of divalent cation salts resulted in an increase in protein particle size, dry sediment formation and sediment height and a decrease in pH, heat stability and hydration in milk protein concentrate-soy protein isolate mixtures solutions on sterilization at 115°C. Fortification of divalent cation salts in milk protein concentrate-soy protein isolate mixture solutions resulted in an accelerated protein sedimentation and two unique sediment regions during accelerated storage stability testing. Moreover, the heat stability decreased upon sterilization at 115°C, with addition of MgCl₂ causing a greater increase in sedimentation velocity and compressibility than CaCl₂. Increasing pH value of protein milk concentrate-soy protein isolate mixtures solutions from 6.7 to 7.2 resulted in an increase in viscosity following the heat treatment. The study demonstrated that the type and concentration of divalent cation salts used strongly impact heat and storage stability of milk protein concentrate-soy protein isolate mixture nutritional beverages. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=divalent%20cation%20salts" title="divalent cation salts">divalent cation salts</a>, <a href="https://publications.waset.org/abstracts/search?q=heat%20stability" title=" heat stability"> heat stability</a>, <a href="https://publications.waset.org/abstracts/search?q=milk%20protein%20concentrate" title=" milk protein concentrate"> milk protein concentrate</a>, <a href="https://publications.waset.org/abstracts/search?q=soy%20protein%20isolate" title=" soy protein isolate"> soy protein isolate</a>, <a href="https://publications.waset.org/abstracts/search?q=storage%20stability" title=" storage stability"> storage stability</a> </p> <a href="https://publications.waset.org/abstracts/94469/fortification-of-concentrated-milk-protein-beverages-with-soy-proteins-impact-of-divalent-cations-and-heating-treatment-on-the-physical-stability" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/94469.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">331</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">13225</span> The Relation Between Protein-Protein and Polysaccharide-Protein Interaction on Aroma Release from Brined Cheese Model</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Mehrnaz%20Aminifar">Mehrnaz Aminifar</a> </p> <p class="card-text"><strong>Abstract:</strong></p> The relation between textural parameters and casein network on release of aromatic compounds was investigated over 90-days of ripening. Low DE maltodextrin and WPI were used to modify the textural properties of low fat brined cheese. Hardness, brittleness and compaction of casein network were affected by addition of maltodextrin and WPI. Textural properties and aroma release from cheese texture were affected by interaction of WPI protein-cheese protein and maltodexterin-cheese protein. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=aroma%20release" title="aroma release">aroma release</a>, <a href="https://publications.waset.org/abstracts/search?q=brined%20cheese" title=" brined cheese"> brined cheese</a>, <a href="https://publications.waset.org/abstracts/search?q=maltodexterin" title=" maltodexterin"> maltodexterin</a>, <a href="https://publications.waset.org/abstracts/search?q=WPI" title=" WPI"> WPI</a> </p> <a href="https://publications.waset.org/abstracts/6193/the-relation-between-protein-protein-and-polysaccharide-protein-interaction-on-aroma-release-from-brined-cheese-model" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/6193.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">355</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">13224</span> Nutritional Characteristics, Mineral contents, Amino acid Composition and Phytochemical Analysis of Eryngium alpinium Leaf Protein Concentrates</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Owonikoko%20A.%20D.">Owonikoko A. D.</a>, <a href="https://publications.waset.org/abstracts/search?q=Odoje%20O.%20F."> Odoje O. F.</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Fresh sample of Eryngium alpinum was purchased and processed for leaf protein concentrates with a view to evaluating its nutritional potential, mineral composition, amino acid characteristics and phytochemical constituents. Using standard analytical methods. The proximate composition of the leaf protein concentrates revealed moisture content;(5.35±0.21)g/100g, ash;(11.37±0.43)g/100g, crude protein;(48.17±0.46)g/100g, crude fat;(15.38±0.07)g/100g, crude fibre (3.05±0.46)g/100g, and Nitrogen free extractive; (16.68±0.30) g/100g. The mineral content was: Na;(51.88±0.23) mg/100g, K;(65.40±0.32)mg/100g, Ca; (86.89±0.46)mg/100g, Mg;(49.27±0.42) mg/100g, Zn;(0.62±0.03)mg/100g, Fe (6.65±0.43)mg/100g, Mn;(0.96±0.54)mg/100g, Cd;(0.28±0.04)mg/100g, P; (8.55±0.97)mg/100g, while selenium, lead and mercury were not detected in the sample indicating that the sample is free of causing risk of metal poisoning. The results of phytochemical constituents showed phytate; (18.34±0.36)mg/100g, flavonoid (0.25±0.41)mg/100g. The sample contain both essential and non-essential amino acid, with the highest value of Glutamic acid (12.26) and the lowest value of Tryptophan 1.05. the content of the leaf protein content shows that the sample is fit for dietary consumption and could as well be processed to be used as food additives. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=mineral%20composition" title="mineral composition">mineral composition</a>, <a href="https://publications.waset.org/abstracts/search?q=phytochemical%20analysis" title=" phytochemical analysis"> phytochemical analysis</a>, <a href="https://publications.waset.org/abstracts/search?q=leaf%20protein%20concentrates" title=" leaf protein concentrates"> leaf protein concentrates</a>, <a href="https://publications.waset.org/abstracts/search?q=eryngium%20alpinum" title=" eryngium alpinum"> eryngium alpinum</a> </p> <a href="https://publications.waset.org/abstracts/166086/nutritional-characteristics-mineral-contents-amino-acid-composition-and-phytochemical-analysis-of-eryngium-alpinium-leaf-protein-concentrates" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/166086.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">109</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">13223</span> Amino Acid Profile, Protein Digestibility, Antioxidant and Functional Properties of Protein Concentrate of Local Varieties (Kwandala, Yardass, Jeep, and Jamila) of Rice Brands from Nigeria</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=C.%20E.%20Chinma">C. E. Chinma</a>, <a href="https://publications.waset.org/abstracts/search?q=S.%20O.%20Azeez"> S. O. Azeez</a>, <a href="https://publications.waset.org/abstracts/search?q=J.%20C.%20Anuonye"> J. C. Anuonye</a>, <a href="https://publications.waset.org/abstracts/search?q=O.%20B.%20Ocheme"> O. B. Ocheme</a>, <a href="https://publications.waset.org/abstracts/search?q=C.%20M.%20Yakubu"> C. M. Yakubu</a>, <a href="https://publications.waset.org/abstracts/search?q=S.%20James"> S. James</a>, <a href="https://publications.waset.org/abstracts/search?q=E.%20U.%20Ohuoba"> E. U. Ohuoba</a>, <a href="https://publications.waset.org/abstracts/search?q=I.%20A.%20Baba"> I. A. Baba </a> </p> <p class="card-text"><strong>Abstract:</strong></p> There is growing interest in the use of rice bran protein in food formulation due to its hypoallergenic protein, high nutritional value and health promoting potentials. For the first time, the amino acid profile, protein digestibility, antioxidant, and functional properties of protein concentrate from some local varieties of rice bran from Nigeria were studied for possible food applications. Protein concentrates were prepared from rice bran and analysed using standard methods. Results showed that protein content of Kwandala, Yardass, Jeep, and Jamila were 69.24%, 69.97%, 68.73%, and 71.62%, respectively while total essential amino acid were 52.71, 53.03, 51.86, and 55.75g/100g protein, respectively. In vitro protein digestibility of protein concentrate from Kwandala, Yardass, Jeep and Jamila were 90.70%, 91.39%, 90.57% and 91.63% respectively. DPPH radical inhibition of protein from Kwandala, Yardass, Jeep, and Jamila were 48.15%, 48.90%, 47.56%, and 53.29%, respectively while ferric reducing ability power were 0.52, 0.55, 0.47 and 0.67mmol TE per gram, respectively. Protein concentrate from Jamila had higher onset (92.57oC) and denaturation temperature (102.13oC), and enthalpy (0.72J/g) than Jeep (91.46oC, 101.76oC, and 0.68J/g, respectively), Kwandala (90.32oC, 100.54oC and 0.57J/g, respectively), and Yardass (88.94oC, 99.45oC, and 0.51J/g, respectively). In vitro digestibility of protein from Kwandala, Yardas, Jeep, and Jamila were 90.70%, 91.39%, 90.57% and 91.63% respectively. Oil absorption capacity of Kwandala, Yardass, Jeep, and Jamila were 3.61, 3.73, 3.40, and 4.23g oil/g sample respectively, while water absorption capacity were 4.19, 4.32, 3.55 and 4.48g water/g sample, respectively. Protein concentrates had low bulk density (0.37-0.43g/ml). Protein concentrate from Jamila rice bran had the highest foam capacity (37.25%), followed by Yardass (34.20%), Kwandala (30.14%) and Jeep (28.90%). Protein concentrates showed low emulsifying and gelling capacities. In conclusion, protein concentrate prepared from these local rice bran varieties could serve as functional ingredients in food formulations and for enriching low protein foods. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=rice%20bran%20protein" title="rice bran protein">rice bran protein</a>, <a href="https://publications.waset.org/abstracts/search?q=amino%20acid%20profile" title=" amino acid profile"> amino acid profile</a>, <a href="https://publications.waset.org/abstracts/search?q=protein%20digestibility" title=" protein digestibility"> protein digestibility</a>, <a href="https://publications.waset.org/abstracts/search?q=antioxidant%20and%20functional%20properties" title=" antioxidant and functional properties"> antioxidant and functional properties</a> </p> <a href="https://publications.waset.org/abstracts/17730/amino-acid-profile-protein-digestibility-antioxidant-and-functional-properties-of-protein-concentrate-of-local-varieties-kwandala-yardass-jeep-and-jamila-of-rice-brands-from-nigeria" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/17730.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">372</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">13222</span> Analysis of Formyl Peptide Receptor 1 Protein Value as an Indicator of Neutrophil Chemotaxis Dysfunction in Aggressive Periodontitis</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Prajna%20Metta">Prajna Metta</a>, <a href="https://publications.waset.org/abstracts/search?q=Yanti%20Rusyanti"> Yanti Rusyanti</a>, <a href="https://publications.waset.org/abstracts/search?q=Nunung%20Rusminah"> Nunung Rusminah</a>, <a href="https://publications.waset.org/abstracts/search?q=Bremmy%20Laksono"> Bremmy Laksono</a> </p> <p class="card-text"><strong>Abstract:</strong></p> The decrease of neutrophil chemotaxis function may cause increased susceptibility to aggressive periodontitis (AP). Neutrophil chemotaxis is affected by formyl peptide receptor 1 (FPR1), which when activated will respond to bacterial chemotactic peptide formyl methionyl leusyl phenylalanine (FMLP). FPR1 protein value is decreased in response to a wide number of inflammatory stimuli in AP patients. This study was aimed to assess the alteration of FPR1 protein value in AP patients and if FPR1 protein value could be used as an indicator of neutrophil chemotaxis dysfunction in AP. This is a case control study with 20 AP patients and 20 control subjects. Three milliliters of peripheral blood were drawn and analyzed for FPR1 protein value with ELISA. The data were statistically analyzed with Mann-Whitney test (p>0,05<u>)</u>. Results showed that the mean value of FPR1 protein value in AP group is 0,353 pg/mL (0,11 to 1,18 pg/mL) and the mean value of FPR1 protein value in control group is 0,296 pg/mL (0,05 to 0,88 pg/mL). P value 0,787 > 0,05 suggested that there is no significant difference of FPR1 protein value in both groups. The present study suggests that FPR1 protein value has no significance alteration in AP patients and could not be used as an indicator of neutrophil chemotaxis dysfunction. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=aggressive%20periodontitis" title="aggressive periodontitis">aggressive periodontitis</a>, <a href="https://publications.waset.org/abstracts/search?q=chemotaxis%20dysfunction" title=" chemotaxis dysfunction"> chemotaxis dysfunction</a>, <a href="https://publications.waset.org/abstracts/search?q=FPR1%20protein%20value" title=" FPR1 protein value"> FPR1 protein value</a>, <a href="https://publications.waset.org/abstracts/search?q=neutrophil" title=" neutrophil"> neutrophil</a> </p> <a href="https://publications.waset.org/abstracts/58541/analysis-of-formyl-peptide-receptor-1-protein-value-as-an-indicator-of-neutrophil-chemotaxis-dysfunction-in-aggressive-periodontitis" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/58541.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">218</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">13221</span> Physicochemical Properties of Pea Protein Isolate (PPI)-Starch and Soy Protein Isolate (SPI)-Starch Nanocomplexes Treated by Ultrasound at Different pH Values</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Gulcin%20Yildiz">Gulcin Yildiz</a>, <a href="https://publications.waset.org/abstracts/search?q=Hao%20%20Feng"> Hao Feng</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Soybean proteins are the most widely used and researched proteins in the food industry. Due to soy allergies among consumers, however, alternative legume proteins having similar functional properties have been studied in recent years. These alternative proteins are also expected to have a price advantage over soy proteins. One such protein that has shown good potential for food applications is pea protein. Besides the favorable functional properties of pea protein, it also contains fewer anti-nutritional substances than soy protein. However, a comparison of the physicochemical properties of pea protein isolate (PPI)-starch nanocomplexes and soy protein isolate (SPI)-starch nanocomplexes treated by ultrasound has not been well documented. This study was undertaken to investigate the effects of ultrasound treatment on the physicochemical properties of PPI-starch and SPI-starch nanocomplexes. Pea protein isolate (85% pea protein) provided by Roquette (Geneva, IL, USA) and soy protein isolate (SPI, Pro-Fam® 955) obtained from the Archer Daniels Midland Company were adjusted to different pH levels (2-12) and treated with 5 minutes of ultrasonication (100% amplitude) to form complexes with starch. The soluble protein content was determined by the Bradford method using BSA as the standard. The turbidity of the samples was measured using a spectrophotometer (Lambda 1050 UV/VIS/NIR Spectrometer, PerkinElmer, Waltham, MA, USA). The volume-weighted mean diameters (D4, 3) of the soluble proteins were determined by dynamic light scattering (DLS). The emulsifying properties of the proteins were evaluated by the emulsion stability index (ESI) and emulsion activity index (EAI). Both the soy and pea protein isolates showed a U-shaped solubility curve as a function of pH, with a high solubility above the isoelectric point and a low one below it. Increasing the pH from 2 to 12 resulted in increased solubility for both the SPI and PPI-starch complexes. The pea nanocomplexes showed greater solubility than the soy ones. The SPI-starch nanocomplexes showed better emulsifying properties determined by the emulsion stability index (ESI) and emulsion activity index (EAI) due to SPI’s high solubility and high protein content. The PPI had similar or better emulsifying properties at certain pH values than the SPI. The ultrasound treatment significantly decreased the particle sizes of both kinds of nanocomplex. For all pH levels with both proteins, the droplet sizes were found to be lower than 300 nm. The present study clearly demonstrated that applying ultrasonication under different pH conditions significantly improved the solubility and emulsify¬ing properties of the SPI and PPI. The PPI exhibited better solubility and emulsifying properties than the SPI at certain pH levels <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=emulsifying%20properties" title="emulsifying properties">emulsifying properties</a>, <a href="https://publications.waset.org/abstracts/search?q=pea%20protein%20isolate" title=" pea protein isolate"> pea protein isolate</a>, <a href="https://publications.waset.org/abstracts/search?q=soy%20protein%20isolate" title=" soy protein isolate"> soy protein isolate</a>, <a href="https://publications.waset.org/abstracts/search?q=ultrasonication" title=" ultrasonication"> ultrasonication</a> </p> <a href="https://publications.waset.org/abstracts/53195/physicochemical-properties-of-pea-protein-isolate-ppi-starch-and-soy-protein-isolate-spi-starch-nanocomplexes-treated-by-ultrasound-at-different-ph-values" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/53195.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">319</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">13220</span> Selection of Pichia kudriavzevii Strain for the Production of Single-Cell Protein from Cassava Processing Waste</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Phakamas%20Rachamontree">Phakamas Rachamontree</a>, <a href="https://publications.waset.org/abstracts/search?q=Theerawut%20Phusantisampan"> Theerawut Phusantisampan</a>, <a href="https://publications.waset.org/abstracts/search?q=Natthakorn%20Woravutthikul"> Natthakorn Woravutthikul</a>, <a href="https://publications.waset.org/abstracts/search?q=Peerapong%20Pornwongthong"> Peerapong Pornwongthong</a>, <a href="https://publications.waset.org/abstracts/search?q=Malinee%20Sriariyanun"> Malinee Sriariyanun</a> </p> <p class="card-text"><strong>Abstract:</strong></p> A total of 115 yeast strains isolated from local cassava processing wastes were measured for crude protein content. Among these strains, the strain MSY-2 possessed the highest protein concentration (>3.5 mg protein/mL). By using molecular identification tools, it was identified to be a strain of Pichia kudriavzevii based on similarity of D1/D2 domain of 26S rDNA region. In this study, to optimize the protein production by MSY-2 strain, Response Surface Methodology (RSM) was applied. The tested parameters were the carbon content, nitrogen content, and incubation time. Here, the value of regression coefficient (R2) = 0.7194 could be explained by the model, which is high to support the significance of the model. Under the optimal condition, the protein content was produced up to 3.77 g per L of the culture and MSY-2 strain contain 66.8 g protein per 100 g of cell dry weight. These results revealed the plausibility of applying the novel strain of yeast in single-cell protein production. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=single%20cell%20protein" title="single cell protein">single cell protein</a>, <a href="https://publications.waset.org/abstracts/search?q=response%20surface%20methodology" title=" response surface methodology"> response surface methodology</a>, <a href="https://publications.waset.org/abstracts/search?q=yeast" title=" yeast"> yeast</a>, <a href="https://publications.waset.org/abstracts/search?q=cassava%20processing%20waste" title=" cassava processing waste"> cassava processing waste</a> </p> <a href="https://publications.waset.org/abstracts/27179/selection-of-pichia-kudriavzevii-strain-for-the-production-of-single-cell-protein-from-cassava-processing-waste" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/27179.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">403</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">13219</span> Effect of Different Irrigation Intervals on Protein and Gel Production of Aloe Vera (Aloe Barbadensis M.) in Iran</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Seyed%20Mohammad%20Hosein%20Al%20Omrani%20Nejad">Seyed Mohammad Hosein Al Omrani Nejad</a>, <a href="https://publications.waset.org/abstracts/search?q=Ali%20Rezvani%20Aghdam"> Ali Rezvani Aghdam</a> </p> <p class="card-text"><strong>Abstract:</strong></p> This study was done in order to evaluation different irrigation intervals on amount of protein, and gel production in Aloe vera, a traditional medicinal plant. Plants was plnted in Greenhouse and irrigated according to Accumulative Pan Evaporation(APE). The treatments were included 20, 40, 60, 80, 100, 120, 140, 160, 180, and 200 mm APE which has been showed W1,W2, W3, W4, W5, W6, W7, W8,W9 and W10 respectively.The amount of protein and gel production was measured seperately. Results showed that highest protein and fresh weight of gel obtained plants which irrigated W6 and W7 respectively. According to these results can recomend which if plant irrigatedwhen APE reached 120 and 140 mm by Class A Evaporation Pan method gel production and protein would besuitable in north of khozestan province in limited irrigation conditions. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=irrigation" title="irrigation">irrigation</a>, <a href="https://publications.waset.org/abstracts/search?q=protein" title=" protein"> protein</a>, <a href="https://publications.waset.org/abstracts/search?q=gel" title=" gel"> gel</a>, <a href="https://publications.waset.org/abstracts/search?q=aloe%20vera" title=" aloe vera"> aloe vera</a>, <a href="https://publications.waset.org/abstracts/search?q=Iran" title=" Iran"> Iran</a> </p> <a href="https://publications.waset.org/abstracts/30907/effect-of-different-irrigation-intervals-on-protein-and-gel-production-of-aloe-vera-aloe-barbadensis-m-in-iran" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/30907.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">389</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">13218</span> In vitro and invivo Antioxidant Studies of Grewia crenata Leaves Extract in Albino Rats</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=A.%20N.Ukwuani">A. N.Ukwuani</a>, <a href="https://publications.waset.org/abstracts/search?q=A.%20K.%20Abdulfatah"> A. K. Abdulfatah</a> </p> <p class="card-text"><strong>Abstract:</strong></p> G. crenata is used locally for the treatment of fractured bones, wound healing and inflammatory conditions. In vitro and in vivo antioxidant activity of hydromethanolic extracts of the leaves of G. crenata were assessed. The phytochemical analysis shows the presence of phenols, flavonoids, saponins, cardiac glycosides and tannins. An in vitro quantitative analysis of phenols, flavonoids and tannins respectively were (164±1.20, 199±0.88 and 88.67±0.88 mg/100g FW). In vivo studies of hydromethanolic extract demonstrated a dose dependent increase in hepatic superoxide dismutase (1.14±0.14, 2.13±0.11, 2.55±0.11 U/mg Protein) with improvement in hepatic glutathione (6.98±0.42, 8.91±0.37, 11.07±0.46 µM/mg Protein) and Catalase (4.47±0.05, 6.24±0.02, 7.17±0.04 U/mg Protein) and Total protein (6.18±0.08, 6.69±0.18, 7.27±0.16 mg/ml) respectively at 100-300mg/kg body weight Grewia crenata leaves when compared to the control and standard drug. It can be concluded from the present findings of that G. crenata leaves possess antioxidant potential. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=Grewia%20crenata" title="Grewia crenata">Grewia crenata</a>, <a href="https://publications.waset.org/abstracts/search?q=antioxidant" title=" antioxidant"> antioxidant</a>, <a href="https://publications.waset.org/abstracts/search?q=hydromethanolic%20extract" title=" hydromethanolic extract"> hydromethanolic extract</a>, <a href="https://publications.waset.org/abstracts/search?q=in%20vivo" title=" in vivo"> in vivo</a>, <a href="https://publications.waset.org/abstracts/search?q=in%20vitro" title=" in vitro"> in vitro</a> </p> <a href="https://publications.waset.org/abstracts/15568/in-vitro-and-invivo-antioxidant-studies-of-grewia-crenata-leaves-extract-in-albino-rats" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/15568.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">553</span> </span> </div> </div> <ul class="pagination"> <li class="page-item disabled"><span class="page-link">&lsaquo;</span></li> <li class="page-item active"><span class="page-link">1</span></li> <li class="page-item"><a class="page-link" href="https://publications.waset.org/abstracts/search?q=potential%20protein&page=2">2</a></li> <li class="page-item"><a class="page-link" href="https://publications.waset.org/abstracts/search?q=potential%20protein&page=3">3</a></li> <li class="page-item"><a class="page-link" href="https://publications.waset.org/abstracts/search?q=potential%20protein&page=4">4</a></li> <li class="page-item"><a class="page-link" href="https://publications.waset.org/abstracts/search?q=potential%20protein&page=5">5</a></li> <li class="page-item"><a class="page-link" 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