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functional module</title> <meta name="description" content="Search results for: protein functional module"> <meta name="keywords" content="protein functional module"> <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 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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="protein functional module"> <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> 5698</div> </div> </div> </div> <h1 class="mt-3 mb-3 text-center" style="font-size:1.6rem;">Search results for: protein functional module</h1> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">5698</span> ACOPIN: An ACO Algorithm with TSP Approach for Clustering Proteins in Protein Interaction Networks</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Jamaludin%20Sallim">Jamaludin Sallim</a>, <a href="https://publications.waset.org/abstracts/search?q=Rozlina%20Mohamed"> Rozlina Mohamed</a>, <a href="https://publications.waset.org/abstracts/search?q=Roslina%20Abdul%20Hamid"> Roslina Abdul Hamid</a> </p> <p class="card-text"><strong>Abstract:</strong></p> In this paper, we proposed an Ant Colony Optimization (ACO) algorithm together with Traveling Salesman Problem (TSP) approach to investigate the clustering problem in Protein Interaction Networks (PIN). We named this combination as ACOPIN. The purpose of this work is two-fold. First, to test the efficacy of ACO in clustering PIN and second, to propose the simple generalization of the ACO algorithm that might allow its application in clustering proteins in PIN. We split this paper to three main sections. First, we describe the PIN and clustering proteins in PIN. Second, we discuss the steps involved in each phase of ACO algorithm. Finally, we present some results of the investigation with the clustering patterns. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=ant%20colony%20optimization%20algorithm" title="ant colony optimization algorithm">ant colony optimization algorithm</a>, <a href="https://publications.waset.org/abstracts/search?q=searching%20algorithm" title=" searching algorithm"> searching algorithm</a>, <a href="https://publications.waset.org/abstracts/search?q=protein%20functional%20module" title=" protein functional module"> protein functional module</a>, <a href="https://publications.waset.org/abstracts/search?q=protein%20interaction%20network" title=" protein interaction network "> protein interaction network </a> </p> <a href="https://publications.waset.org/abstracts/22367/acopin-an-aco-algorithm-with-tsp-approach-for-clustering-proteins-in-protein-interaction-networks" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/22367.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">611</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">5697</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">5696</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">370</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">5695</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">5694</span> Effect of Thermal Pretreatment on Functional Properties of Chicken Protein Hydrolysate</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Nutnicha%20Wongpadungkiat">Nutnicha Wongpadungkiat</a>, <a href="https://publications.waset.org/abstracts/search?q=Suwit%20Siriwatanayotin"> Suwit Siriwatanayotin</a>, <a href="https://publications.waset.org/abstracts/search?q=Aluck%20Thipayarat"> Aluck Thipayarat</a>, <a href="https://publications.waset.org/abstracts/search?q=Punchira%20Vongsawasdi"> Punchira Vongsawasdi</a>, <a href="https://publications.waset.org/abstracts/search?q=Chotika%20Viriyarattanasak"> Chotika Viriyarattanasak</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Chicken products are major export product of Thailand. With a dramatically increasing consumption of chicken product in the world, there are abundant wastes from chicken meat processing industry. Recently, much research in the development of value-added products from chicken meat industry has focused on the production of protein hydrolysate, utilized as food ingredients for human diet and animal feed. The present study aimed to determine the effect of thermal pre-treatment on functional properties of chicken protein hydrolysate. Chicken breasts were heated at 40, 60, 80 and 100ºC prior to hydrolysis by Alcalase at 60ºC, pH 8 for 4 hr. The hydrolysate was freeze-dried, and subsequently used for assessment of its functional properties molecular weight by gel electrophoresis (SDS-PAGE). The obtained results show that increasing the pre-treatment temperature increased oil holding capacity and emulsion stability while decreasing antioxidant activity and water holding capacity. The SDS-PAGE analysis showed the evidence of protein aggregation in the hydrolysate treated at the higher pre-treatment temperature. These results suggest the connection between molecular weight of the hydrolysate and its functional properties. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=chicken%20protein%20hydrolysate" title="chicken protein hydrolysate">chicken protein hydrolysate</a>, <a href="https://publications.waset.org/abstracts/search?q=enzymatic%20hydrolysis" title=" enzymatic hydrolysis"> enzymatic hydrolysis</a>, <a href="https://publications.waset.org/abstracts/search?q=thermal%20pretreatment" title=" thermal pretreatment"> thermal pretreatment</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/56093/effect-of-thermal-pretreatment-on-functional-properties-of-chicken-protein-hydrolysate" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/56093.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">270</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">5693</span> Functionality and Application of Rice Bran Protein Hydrolysates in Oil in Water Emulsions: Their Stabilities to Environmental Stresses</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=R.%20Charoen">R. Charoen</a>, <a href="https://publications.waset.org/abstracts/search?q=S.%20Tipkanon"> S. Tipkanon</a>, <a href="https://publications.waset.org/abstracts/search?q=W.%20Savedboworn"> W. Savedboworn</a>, <a href="https://publications.waset.org/abstracts/search?q=N.%20Phonsatta"> N. Phonsatta</a>, <a href="https://publications.waset.org/abstracts/search?q=A.%20Panya"> A. Panya</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Rice bran protein hydrolysates (RBPH) were prepared from defatted rice bran of two different Thai rice cultivars (Plai-Ngahm-Prachinburi; PNP and Khao Dok Mali 105; KDM105) using an enzymatic method. This research aimed to optimize enzyme-assisted protein extraction. In addition, the functional properties of RBPH and their stabilities to environmental stresses including pH (3 to 8), ionic strength (0 mM to 500 mM) and the thermal treatment (30 °C to 90 °C) were investigated. Results showed that enzymatic process for protein extraction of defatted rice bran was as follows: enzyme concentration 0.075 g/ 5 g of protein, extraction temperature 50 °C and extraction time 4 h. The obtained protein hydrolysate powders had a degree of hydrolysis (%) of 21.05% in PNP and 19.92% in KDM105. The solubility of protein hydrolysates at pH 4-6 was ranged from 27.28-38.57% and 27.60-43.00% in PNP and KDM105, respectively. In general, antioxidant activities indicated by total phenolic content, FRAP, ferrous ion-chelating (FIC), and 2,2’-azino-bis-3-ethylbenzthiazoline-6-sulphonic acid (ABTS) of KDM105 had higher than PNP. In terms of functional properties, the emulsifying activity index (EAI) was was 8.78 m²/g protein in KDM105, whereas PNP was 5.05 m²/g protein. The foaming capacity at 5 minutes (%) was 47.33 and 52.98 in PNP and KDM105, respectively. Glutamine, Alanine, Valine, and Leucine are the major amino acid in protein hydrolysates where the total amino acid of KDM105 gave higher than PNP. Furthermore, we investigated environmental stresses on the stability of 5% oil in water emulsion (5% oil, 10 mM citrate buffer) stabilized by RBPH (3.5%). The droplet diameter of emulsion stabilized by KDM105 was smaller (d < 250 nm) than produced by PNP. For environmental stresses, RBPH stabilized emulsions were stable at pH around 3 and 5-6, at high salt (< 400 mM, pH 7) and at temperatures range between 30-50°C. <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=oil%20in%20water%20emulsion" title=" oil in water emulsion"> oil in water emulsion</a>, <a href="https://publications.waset.org/abstracts/search?q=protein%20hydrolysates" title=" protein hydrolysates"> protein hydrolysates</a>, <a href="https://publications.waset.org/abstracts/search?q=rice%20bran%20protein" title=" rice bran protein"> rice bran protein</a> </p> <a href="https://publications.waset.org/abstracts/82295/functionality-and-application-of-rice-bran-protein-hydrolysates-in-oil-in-water-emulsions-their-stabilities-to-environmental-stresses" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/82295.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">5692</span> Nutritional Potential and Functionality of Whey Powder Influenced by Different Processing Temperature and Storage</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Zarmina%20Gillani">Zarmina Gillani</a>, <a href="https://publications.waset.org/abstracts/search?q=Nuzhat%20Huma"> Nuzhat Huma</a>, <a href="https://publications.waset.org/abstracts/search?q=Aysha%20Sameen"> Aysha Sameen</a>, <a href="https://publications.waset.org/abstracts/search?q=Mulazim%20Hussain%20Bukhari"> Mulazim Hussain Bukhari</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Whey is an excellent food ingredient owing to its high nutritive value and its functional properties. However, composition of whey varies depending on composition of milk, processing conditions, processing method, and its whey protein content. The aim of this study was to prepare a whey powder from raw whey and to determine the influence of different processing temperatures (160 and 180 °C) on the physicochemical, functional properties during storage of 180 days and on whey protein denaturation. Results have shown that temperature significantly (P < 0.05) affects the pH, acidity, non-protein nitrogen (NPN), protein total soluble solids, fat and lactose contents. Significantly (p < 0.05) higher foaming capacity (FC), foam stability (FS), whey protein nitrogen index (WPNI), and a lower turbidity and solubility index (SI) were observed in whey powder processed at 160 °C compared to whey powder processed at 180 °C. During storage of 180 days, slow but progressive changes were noticed on the physicochemical and functional properties of whey powder. Reverse phase-HPLC analysis revealed a significant (P < 0.05) effect of temperature on whey protein contents. Denaturation of β-Lactoglobulin is followed by α-lacalbumin, casein glycomacropeptide (CMP/GMP), and bovine serum albumin (BSA). <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=whey%20powder" title="whey powder">whey powder</a>, <a href="https://publications.waset.org/abstracts/search?q=temperature" title=" temperature"> temperature</a>, <a href="https://publications.waset.org/abstracts/search?q=denaturation" title=" denaturation"> denaturation</a>, <a href="https://publications.waset.org/abstracts/search?q=reverse%20phase" title=" reverse phase"> reverse phase</a>, <a href="https://publications.waset.org/abstracts/search?q=HPLC" title=" HPLC"> HPLC</a> </p> <a href="https://publications.waset.org/abstracts/71225/nutritional-potential-and-functionality-of-whey-powder-influenced-by-different-processing-temperature-and-storage" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/71225.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">299</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">5691</span> Bio-Functional Polymeric Protein Based Materials Utilized for Soft Tissue Engineering Application </h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Er-Yuan%20Chuang">Er-Yuan Chuang</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Bio-mimetic matters have biological functionalities. This might be valuable in the development of versatile biomaterials. At biological fields, protein-based materials might be components to form a 3D network of extracellular biomolecules, containing growth factors. Also, the protein-based biomaterial provides biochemical and structural assistance of adjacent cells. In this study, we try to prepare protein based biomaterial, which was harvested from living animal. We analyzed it’s chemical, physical and biological property in vitro. Besides, in vivo bio-interaction of the prepared biomimetic matrix was tested in an animal model. The protein-based biomaterial has degradability and biocompatibility. This development could be used for tissue regenerations and be served as platform technologies. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=protein%20based" title="protein based">protein based</a>, <a href="https://publications.waset.org/abstracts/search?q=in%20vitro%20study" title=" in vitro study"> in vitro study</a>, <a href="https://publications.waset.org/abstracts/search?q=in%20vivo%20study" title=" in vivo study"> in vivo study</a>, <a href="https://publications.waset.org/abstracts/search?q=biomaterials" title=" biomaterials"> biomaterials</a> </p> <a href="https://publications.waset.org/abstracts/105449/bio-functional-polymeric-protein-based-materials-utilized-for-soft-tissue-engineering-application" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/105449.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">189</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">5690</span> Module Valuations and Quasi-Valuations</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Shai%20Sarussi">Shai Sarussi</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Suppose F is a field with valuation v and valuation domain Oᵥ, and R is an Oᵥ-algebra. It is known that there exists a filter quasi-valuation on R; the existence of a quasi-valuation yields several important connections between Oᵥ and R, in particular with respect to their prime spectra. In this paper, the notion of a module valuation is introduced. It is shown that any torsion-free module over Oᵥ has an induced module valuation. Moreover, several results connecting the filter quasi-valuation and module valuations are presented. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=valuations" title="valuations">valuations</a>, <a href="https://publications.waset.org/abstracts/search?q=quasi-valuations" title=" quasi-valuations"> quasi-valuations</a>, <a href="https://publications.waset.org/abstracts/search?q=prime%20spectrum" title=" prime spectrum"> prime spectrum</a>, <a href="https://publications.waset.org/abstracts/search?q=algebras%20over%20valuation%20domains" title=" algebras over valuation domains"> algebras over valuation domains</a> </p> <a href="https://publications.waset.org/abstracts/139887/module-valuations-and-quasi-valuations" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/139887.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">224</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">5689</span> Dissociation of Hydrophobic Interactions in Whey Protein Polymers: Molecular Characterization Using Dilute Solution Viscometry</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Ahmed%20S.%20Eissa">Ahmed S. Eissa</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Whey represents about 85-95% of the milk volume and about 55% of milk nutrients. Whey proteins are of special importance in formulated foods due to their rich nutritional and functional benefits. Whey proteins form large polymers upon heating to a temperature greater than the denaturation temperature. Hydrophobic interactions play an important role in building whey protein polymers. In this study, dissociation of hydrophobic interactions of whey protein polymers was done by adding Sodium Dodecyl Sulphonate (SDS). At low SDS concentrations, protein polymers were dissociated to smaller chains, as revealed by dilution solution viscometry (DSV). Interestingly, at higher SDS concentrations, polymer molecules got larger in size. Intrinsic viscosity was increased to many folds when raising the SDS concentration from 0.5% to 2%. Complex molecular arrangement leads to the formation of larger macromolecules, due to micelle formation. The study opens a venue for manipulating and enhancing whey protein functional properties by manipulating the hydrophobic interactions. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=whey%20proteins" title="whey proteins">whey proteins</a>, <a href="https://publications.waset.org/abstracts/search?q=hydrophobic%20interactions" title=" hydrophobic interactions"> hydrophobic interactions</a>, <a href="https://publications.waset.org/abstracts/search?q=SDS" title=" SDS"> SDS</a> </p> <a href="https://publications.waset.org/abstracts/81422/dissociation-of-hydrophobic-interactions-in-whey-protein-polymers-molecular-characterization-using-dilute-solution-viscometry" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/81422.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">248</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">5688</span> Experimental Study of Semitransparent and Opaque Photovoltaic Modules with and without Air Duct</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Sanjay%20Agrawal">Sanjay Agrawal</a>, <a href="https://publications.waset.org/abstracts/search?q=Trapti%20Varshney"> Trapti Varshney</a>, <a href="https://publications.waset.org/abstracts/search?q=G.%20N.%20Tiwari"> G. N. Tiwari</a> </p> <p class="card-text"><strong>Abstract:</strong></p> In this paper, thermal modeling has been developed for photovoltaic PV modules, namely; Case A: semitransparent PV module without duct, Case B: semitransparent PV module with duct, Case C: opaque PV module without duct, Case D: opaque PV module with duct for Delhi, India climatic condition. MATLAB 7.0 software has been used to solve mathematical models of the proposed system. For validation of proposed system, the experimental study has also been carried out for all above four cases, and then comparative analysis of all different type of PV module has been presented. The hybrid PVT module air collectors presented in this study are self sustaining the system and can be used for the electricity generation in remote areas where access of electricity is not economical due to high transmission and distribution losses. It has been found that overall annual thermal energy and exergy gain of semitransparent PV module is higher by 11.6% and7.32% in summer condition and 16.39% and 18% in winter condition respectively as compared to opaque PV module considering same area (0.61 m2) of PV module. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=semitransparent%20PV%20module" title="semitransparent PV module">semitransparent PV module</a>, <a href="https://publications.waset.org/abstracts/search?q=overall%20exergy" title=" overall exergy"> overall exergy</a>, <a href="https://publications.waset.org/abstracts/search?q=overall%20thermal%20energy" title=" overall thermal energy"> overall thermal energy</a>, <a href="https://publications.waset.org/abstracts/search?q=opaque" title=" opaque "> opaque </a> </p> <a href="https://publications.waset.org/abstracts/67088/experimental-study-of-semitransparent-and-opaque-photovoltaic-modules-with-and-without-air-duct" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/67088.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">437</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">5687</span> An Efficient Algorithm for Global Alignment of Protein-Protein Interaction Networks</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Duc%20Dong%20Do">Duc Dong Do</a>, <a href="https://publications.waset.org/abstracts/search?q=Ngoc%20Ha%20Tran"> Ngoc Ha Tran</a>, <a href="https://publications.waset.org/abstracts/search?q=Thanh%20Hai%20Dang"> Thanh Hai Dang</a>, <a href="https://publications.waset.org/abstracts/search?q=Cao%20Cuong%20Dang"> Cao Cuong Dang</a>, <a href="https://publications.waset.org/abstracts/search?q=Xuan%20Huan%20Hoang"> Xuan Huan Hoang</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Global aligning two protein-protein interaction networks is an essentially important task in bioinformatics/computational biology field of study. It is a challenging and widely studied research topic in recent years. Accurately aligned networks allow us to identify functional modules of proteins and/ororthologous proteins from which unknown functions of a protein can be inferred. We here introduce a novel efficient heuristic global network alignment algorithm called FASTAn, including two phases: the first to construct an initial alignment and the second to improve such alignment by exerting a local optimization repeated procedure. The experimental results demonstrated that FASTAn outperformed the state-of-the-art global network alignment algorithm namely SPINAL in terms of both commonly used objective scores and the run-time. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=FASTAn" title="FASTAn">FASTAn</a>, <a href="https://publications.waset.org/abstracts/search?q=Heuristic%20algorithm" title=" Heuristic algorithm"> Heuristic algorithm</a>, <a href="https://publications.waset.org/abstracts/search?q=biological%20network%20alignment" title=" biological network alignment"> biological network alignment</a>, <a href="https://publications.waset.org/abstracts/search?q=protein-protein%20interaction%20networks" title=" protein-protein interaction networks"> protein-protein interaction networks</a> </p> <a href="https://publications.waset.org/abstracts/17228/an-efficient-algorithm-for-global-alignment-of-protein-protein-interaction-networks" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/17228.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">603</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">5686</span> EverPro as the Missing Piece in the Plant Protein Portfolio to Aid the Transformation to Sustainable Food Systems</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Aylin%20W%20Sahin">Aylin W Sahin</a>, <a href="https://publications.waset.org/abstracts/search?q=Alice%20Jaeger"> Alice Jaeger</a>, <a href="https://publications.waset.org/abstracts/search?q=Laura%20Nyhan"> Laura Nyhan</a>, <a href="https://publications.waset.org/abstracts/search?q=Gregory%20Belt"> Gregory Belt</a>, <a href="https://publications.waset.org/abstracts/search?q=Steffen%20M%C3%BCnch"> Steffen Münch</a>, <a href="https://publications.waset.org/abstracts/search?q=Elke%20K.%20Arendt"> Elke K. Arendt</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Our current food systems cause an increase in malnutrition resulting in more people being overweight or obese in the Western World. Additionally, our natural resources are under enormous pressure and the greenhouse gas emission increases yearly with a significant contribution to climate change. Hence, transforming our food systems is of highest priority. Plant-based food products have a lower environmental impact compared to their animal-based counterpart, representing a more sustainable protein source. However, most plant-based protein ingredients, such as soy and pea, are lacking indispensable amino acids and extremely limited in their functionality and, thus, in their food application potential. They are known to have a low solubility in water and change their properties during processing. The low solubility displays the biggest challenge in the development of milk alternatives leading to inferior protein content and protein quality in dairy alternatives on the market. Moreover, plant-based protein ingredients often possess an off-flavour, which makes them less attractive to consumers. EverPro, a plant-protein isolate originated from Brewer’s Spent Grain, the most abundant by-product in the brewing industry, represents the missing piece in the plant protein portfolio. With a protein content of >85%, it is of high nutritional value, including all indispensable amino acids which allows closing the protein quality gap of plant proteins. Moreover, it possesses high techno-functional properties. It is fully soluble in water (101.7 ± 2.9%), has a high fat absorption capacity (182.4 ± 1.9%), and a foaming capacity which is superior to soy protein or pea protein. This makes EverPro suitable for a vast range of food applications. Furthermore, it does not cause changes in viscosity during heating and cooling of dispersions, such as beverages. Besides its outstanding nutritional and functional characteristics, the production of EverPro has a much lower environmental impact compared to dairy or other plant protein ingredients. Life cycle assessment analysis showed that EverPro has the lowest impact on global warming compared to soy protein isolate, pea protein isolate, whey protein isolate, and egg white powder. It also contributes significantly less to freshwater eutrophication, marine eutrophication and land use compared the protein sources mentioned above. EverPro is the prime example of sustainable ingredients, and the type of plant protein the food industry was waiting for: nutritious, multi-functional, and environmentally friendly. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=plant-based%20protein" title="plant-based protein">plant-based protein</a>, <a href="https://publications.waset.org/abstracts/search?q=upcycled" title=" upcycled"> upcycled</a>, <a href="https://publications.waset.org/abstracts/search?q=brewers%27%20spent%20grain" title=" brewers' spent grain"> brewers' spent grain</a>, <a href="https://publications.waset.org/abstracts/search?q=low%20environmental%20impact" title=" low environmental impact"> low environmental impact</a>, <a href="https://publications.waset.org/abstracts/search?q=highly%20functional%20ingredient" title=" highly functional ingredient"> highly functional ingredient</a> </p> <a href="https://publications.waset.org/abstracts/162371/everpro-as-the-missing-piece-in-the-plant-protein-portfolio-to-aid-the-transformation-to-sustainable-food-systems" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/162371.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">80</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">5685</span> Alternating Current Photovoltaic Module Model </h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Irtaza%20M.%20Syed">Irtaza M. Syed</a>, <a href="https://publications.waset.org/abstracts/search?q=Kaamran%20Raahemifar"> Kaamran Raahemifar</a> </p> <p class="card-text"><strong>Abstract:</strong></p> This paper presents modeling of a Alternating Current (AC) Photovoltaic (PV) module using Matlab/Simulink. The proposed AC-PV module model is simple, realistic, and application oriented. The model is derived on module level as compared to cell level directly from the information provided by the manufacturer data sheet. DC-PV module, MPPT control, BC, VSI and LC filter, all were treated as a single unit. The model accounts for changes in variations of both irradiance and temperature. The AC-PV module proposed model is simulated and the results are compared with the datasheet projected numbers to validate model’s accuracy and effectiveness. Implementation and results demonstrate simplicity and accuracy, as well as reliability of the model. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=PV%20modeling" title="PV modeling">PV modeling</a>, <a href="https://publications.waset.org/abstracts/search?q=AC%20PV%20Module" title=" AC PV Module"> AC PV Module</a>, <a href="https://publications.waset.org/abstracts/search?q=datasheet" title=" datasheet"> datasheet</a>, <a href="https://publications.waset.org/abstracts/search?q=VI%20curves%20irradiance" title=" VI curves irradiance"> VI curves irradiance</a>, <a href="https://publications.waset.org/abstracts/search?q=temperature" title=" temperature"> temperature</a>, <a href="https://publications.waset.org/abstracts/search?q=MPPT" title=" MPPT"> MPPT</a>, <a href="https://publications.waset.org/abstracts/search?q=Matlab%2FSimulink" title=" Matlab/Simulink"> Matlab/Simulink</a> </p> <a href="https://publications.waset.org/abstracts/16003/alternating-current-photovoltaic-module-model" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/16003.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">575</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">5684</span> Integrating Dynamic Brain Connectivity and Transcriptomic Imaging in Major Depressive Disorder</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Qingjin%20Liu">Qingjin Liu</a>, <a href="https://publications.waset.org/abstracts/search?q=Jinpeng%20Niu"> Jinpeng Niu</a>, <a href="https://publications.waset.org/abstracts/search?q=Kangjia%20Chen"> Kangjia Chen</a>, <a href="https://publications.waset.org/abstracts/search?q=Jiao%20Li"> Jiao Li</a>, <a href="https://publications.waset.org/abstracts/search?q=Huafu%20Chen"> Huafu Chen</a>, <a href="https://publications.waset.org/abstracts/search?q=Wei%20Liao"> Wei Liao</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Functional connectomics is essential in cognitive science and neuropsychiatry, offering insights into the brain's complex network structures and dynamic interactions. Although neuroimaging has uncovered functional connectivity issues in Major Depressive Disorder (MDD) patients, the dynamic shifts in connectome topology and their link to gene expression are yet to be fully understood. To explore the differences in dynamic connectome topology between MDD patients and healthy individuals, we conducted an extensive analysis of resting-state functional magnetic resonance imaging (fMRI) data from 434 participants (226 MDD patients and 208 controls). We used multilayer network models to evaluate brain module dynamics and examined the association between whole-brain gene expression and dynamic module variability in MDD using publicly available transcriptomic data. Our findings revealed that compared to healthy individuals, MDD patients showed lower global mean values and higher standard deviations, indicating unstable patterns and increased regional differentiation. Notably, MDD patients exhibited more frequent module switching, primarily within the executive control network (ECN), particularly in the left dorsolateral prefrontal cortex and right fronto-insular regions, whereas the default mode network (DMN), including the superior frontal gyrus, temporal lobe, and right medial prefrontal cortex, displayed lower variability. These brain dynamics predicted the severity of depressive symptoms. Analyzing human brain gene expression data, we found that the spatial distribution of MDD-related gene expression correlated with dynamic module differences. Cell type-specific gene analyses identified oligodendrocytes (OPCs) as major contributors to the transcriptional relationships underlying module variability in MDD. To the best of our knowledge, this is the first comprehensive description of altered brain module dynamics in MDD patients linked to depressive symptom severity and changes in whole-brain gene expression profiles. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=major%20depressive%20disorder" title="major depressive disorder">major depressive disorder</a>, <a href="https://publications.waset.org/abstracts/search?q=module%20dynamics" title=" module dynamics"> module dynamics</a>, <a href="https://publications.waset.org/abstracts/search?q=magnetic%20resonance%20imaging" title=" magnetic resonance imaging"> magnetic resonance imaging</a>, <a href="https://publications.waset.org/abstracts/search?q=transcriptomic" title=" transcriptomic"> transcriptomic</a> </p> <a href="https://publications.waset.org/abstracts/190173/integrating-dynamic-brain-connectivity-and-transcriptomic-imaging-in-major-depressive-disorder" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/190173.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">25</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">5683</span> In vitro Protein Folding and Stability Using Thermostable Exoshells </h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Siddharth%20Deshpande">Siddharth Deshpande</a>, <a href="https://publications.waset.org/abstracts/search?q=Nihar%20Masurkar"> Nihar Masurkar</a>, <a href="https://publications.waset.org/abstracts/search?q=Vallerinteavide%20Mavelli%20Girish"> Vallerinteavide Mavelli Girish</a>, <a href="https://publications.waset.org/abstracts/search?q=Malan%20Desai"> Malan Desai</a>, <a href="https://publications.waset.org/abstracts/search?q=Chester%20Drum"> Chester Drum</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Folding and stabilization of recombinant proteins remain a consistent challenge for industrial and therapeutic applications. Proteins derived from thermophilic bacteria often have superior expression and stability qualities. To develop a generalizable approach to protein folding and stabilization, we tested the hypothesis that wrapping a thermostable exoshell around a protein substrate would aid folding and impart thermostable qualities to the internalized substrate. To test the effect of internalizing a protein within a thermostable exoshell (tES), we tested in vitro folding and stability using green fluorescent protein (GFPuv), horseradish peroxidase (HRP) and renilla luciferase (rLuc). The 8nm interior volume of a thermostable ferritin assembly was engineered to accommodate foreign proteins and either present a positive, neutral or negative interior charge environment. We further engineered the tES complex to reversibly assemble and disassemble with pH titration. Template proteins were expressed as inclusion bodies and an in vitro folding protocol was developed that forced proteins to fold inside a single tES. Functional yield was improved 100-fold, 100-fold and 150-fold with use of tES for GFPuv, HRP and rLuc respectively and was highly dependent on the internal charge environment of the tES. After folding, functional proteins could be released from the tES folding cavity using size exclusion chromatography at pH 5.8. Internalized proteins were tested for improved stability against thermal, organic, urea and guanidine denaturation. Our results demonstrated that thermostable exoshells can efficiently refold and stabilize inactive aggregates into functional proteins. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=thermostable%20shell" title="thermostable shell">thermostable shell</a>, <a href="https://publications.waset.org/abstracts/search?q=in%20vitro%20folding" title=" in vitro folding"> in vitro folding</a>, <a href="https://publications.waset.org/abstracts/search?q=stability" title=" stability"> stability</a>, <a href="https://publications.waset.org/abstracts/search?q=functional%20yield" title=" functional yield"> functional yield</a> </p> <a href="https://publications.waset.org/abstracts/72637/in-vitro-protein-folding-and-stability-using-thermostable-exoshells" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/72637.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">248</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">5682</span> Power and Efficiency of Photovoltaic Module: Effect of Cell Temperature</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=R.%20Nasrin">R. Nasrin</a>, <a href="https://publications.waset.org/abstracts/search?q=M.%20Ferdows"> M. Ferdows</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Among the renewable energy sources, photovoltaic (PV) is a high potential, effective, and sustainable system. Irradiation intensity from 200 W/m2 to 1000 W/m2 has been considered to observe the performance of PV module. Generally, this module converts only about 15% - 20% of incident irradiation into electrical energy and the rest part is converted into heat energy. Finite element method has been used to solve the problem numerically. Simulation has been performed by considering the ambient temperature 30°C. Higher irradiation increase solar cell temperature and electrical power. The electrical efficiency of PV module decreases with the variation of solar radiation. The efficiency of PV module can be increased if cell temperature is reduced. Thus the effect of irradiation is significant to enhance the efficiency of PV module if the solar cell temperature is kept at a certain level. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=PV%20module" title="PV module">PV module</a>, <a href="https://publications.waset.org/abstracts/search?q=solar%20radiation" title=" solar radiation"> solar radiation</a>, <a href="https://publications.waset.org/abstracts/search?q=efficiency" title=" efficiency"> efficiency</a>, <a href="https://publications.waset.org/abstracts/search?q=cell%20temperature" title=" cell temperature"> cell temperature</a> </p> <a href="https://publications.waset.org/abstracts/82035/power-and-efficiency-of-photovoltaic-module-effect-of-cell-temperature" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/82035.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">361</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">5681</span> Aquafaba Derived from Korean Soybean Cultivars: A Novel Vegan Egg Replacer</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Yue%20He">Yue He</a>, <a href="https://publications.waset.org/abstracts/search?q=Youn%20Young%20Shim"> Youn Young Shim</a>, <a href="https://publications.waset.org/abstracts/search?q=Ji%20Hye%20Kim"> Ji Hye Kim</a>, <a href="https://publications.waset.org/abstracts/search?q=Jae%20Youl%20Cho"> Jae Youl Cho</a>, <a href="https://publications.waset.org/abstracts/search?q=Martin%20J.%20T.%20Reaney"> Martin J. T. Reaney</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Recently, pulse cooking water (a.k.a. Aquafaba) has been used as an important and cost-effective alternative to eggs in gluten-free, vegan cooking and baking applications. The aquafaba (AQ) is primarily due to its excellent ability to stabilize foams and emulsions in foods. However, the functional ingredients of this excellent AQ are usually discarded with the compound release. This study developed a high-functional food material, AQ, using functional soybean AQ that has not been studied in Korea. A zero-waste and cost-effective hybrid process were used to produce oil emulsifiers from Korean soybeans. The treatment technique was implemented using a small number of efficient steps. Aquafaba from Backtae had the best emulsion properties (92%) and has the potential to produce more stable food oil emulsions. Therefore, this study is expected to be utilized in the development of the first gluten-free, vegan product for vegetarians and consumers with animal protein allergies, utilizing wastewater from cooked soybeans as a source of plant protein that can replace animal protein. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=aquafaba" title="aquafaba">aquafaba</a>, <a href="https://publications.waset.org/abstracts/search?q=soybean" title=" soybean"> soybean</a>, <a href="https://publications.waset.org/abstracts/search?q=chickpea" title=" chickpea"> chickpea</a>, <a href="https://publications.waset.org/abstracts/search?q=emulsifiers" title=" emulsifiers"> emulsifiers</a>, <a href="https://publications.waset.org/abstracts/search?q=egg%20replacer" title=" egg replacer"> egg replacer</a>, <a href="https://publications.waset.org/abstracts/search?q=egg-free%20products" title=" egg-free products"> egg-free products</a> </p> <a href="https://publications.waset.org/abstracts/142569/aquafaba-derived-from-korean-soybean-cultivars-a-novel-vegan-egg-replacer" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/142569.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">176</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">5680</span> Effect of Cooking Time, Seed-To-Water Ratio and Soaking Time on the Proximate Composition and Functional Properties of Tetracarpidium conophorum (Nigerian Walnut) Seeds</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=J.%20O.%20Idoko">J. O. Idoko</a>, <a href="https://publications.waset.org/abstracts/search?q=C.%20N.%20Michael"> C. N. Michael</a>, <a href="https://publications.waset.org/abstracts/search?q=T.%20O.%20Fasuan"> T. O. Fasuan</a> </p> <p class="card-text"><strong>Abstract:</strong></p> This study investigated the effects of cooking time, seed-to-water ratio and soaking time on proximate and functional properties of African walnut seed using Box-Behnken design and Response Surface Methodology (BBD-RSM) with a view to increase its utilization in the food industry. African walnut seeds were sorted washed, soaked, cooked, dehulled, sliced, dried and milled. Proximate analysis and functional properties of the samples were evaluated using standard procedures. Data obtained were analyzed using descriptive and inferential statistics. Quadratic models were obtained to predict the proximate and functional qualities as a function of cooking time, seed-to-water ratio and soaking time. The results showed that the crude protein ranged between 11.80% and 23.50%, moisture content ranged between 1.00% and 4.66%, ash content ranged between 3.35% and 5.25%, crude fibre ranged from 0.10% to 7.25% and carbohydrate ranged from 1.22% to 29.35%. The functional properties showed that soluble protein ranged from 16.26% to 42.96%, viscosity ranged from 23.43 mPas to 57 mPas, emulsifying capacity ranged from 17.14% to 39.43% and water absorption capacity ranged from 232% to 297%. An increase in the volume of water used during cooking resulted in loss of water soluble protein through leaching, the length of soaking time and the moisture content of the dried product are inversely related, ash content is inversely related to the cooking time and amount of water used, extraction of fat is enhanced by increase in soaking time while increase in cooking and soaking times result into decrease in fibre content. The results obtained indicated that African walnut could be used in several food formulations as protein supplement and binder. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=African%20walnut" title="African walnut">African walnut</a>, <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=proximate%20analysis" title=" proximate analysis"> proximate analysis</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/11005/effect-of-cooking-time-seed-to-water-ratio-and-soaking-time-on-the-proximate-composition-and-functional-properties-of-tetracarpidium-conophorum-nigerian-walnut-seeds" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/11005.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">396</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">5679</span> Text Mining Techniques for Prioritizing Pathogenic Mutations in Protein Families Known to Misfold or Aggregate</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Khaleel%20Saleh%20Al-Rababah">Khaleel Saleh Al-Rababah</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Amyloid fibril forming regions, which are known as protein aggregates, in sequences of some protein families are associated with a number of diseases known as amyloidosis. Mutations play a role in forming fibrils by accelerating the fibril formation process. In this paper we want to extract diseases that caused by those mutations as a result of the impact of the mutations on structural and functional properties of the aggregated protein. We propose a text mining system, to automatically extract mutations, diseases and relations between mutations and diseases. We presented an algorithm based on finite state to cluster mutations found in the same sentence as a sentence could contain different mutation cause different diseases. Also, we presented a co reference algorithm that enables cross-link sentences. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=amyloid" title="amyloid">amyloid</a>, <a href="https://publications.waset.org/abstracts/search?q=amyloidosis" title=" amyloidosis"> amyloidosis</a>, <a href="https://publications.waset.org/abstracts/search?q=co%20reference" title=" co reference"> co reference</a>, <a href="https://publications.waset.org/abstracts/search?q=protein" title=" protein"> protein</a>, <a href="https://publications.waset.org/abstracts/search?q=text%20mining" title=" text mining"> text mining</a> </p> <a href="https://publications.waset.org/abstracts/24232/text-mining-techniques-for-prioritizing-pathogenic-mutations-in-protein-families-known-to-misfold-or-aggregate" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/24232.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">524</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">5678</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">5677</span> Encapsulation and Protection of Bioactive Nutrients Based on Ligand-Binding Property of Milk Proteins</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Hao%20Cheng">Hao Cheng</a>, <a href="https://publications.waset.org/abstracts/search?q=Yingzhou%20Ni"> Yingzhou Ni</a>, <a href="https://publications.waset.org/abstracts/search?q=Amr%20M.%20Bakry"> Amr M. Bakry</a>, <a href="https://publications.waset.org/abstracts/search?q=Li%20Liang"> Li Liang</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Functional foods containing bioactive nutrients offer benefits beyond basic nutrition and hence the possibility of delaying and preventing chronic diseases. However, many bioactive nutrients degrade rapidly under food processing and storage conditions. Encapsulation can be used to overcome these limitations. Food proteins have been widely used as carrier materials for the preparation of nano/micro-particles because of their ability to form gels and emulsions and to interact with polysaccharides. The mechanisms of interaction between bioactive nutrients and proteins must be understood in order to develop protein-based lipid-free delivery systems. Beta-lactoglobulin, a small globular protein in milk whey, exhibits an affinity to a wide range of compounds. Alfa-tocopherol, resveratrol and folic acid were respectively bound to the central cavity, the outer surface near Trp19–Arg124 and the hydrophobic pocket in the groove between the alfa-helix and the beta-barrel of the protein. Beta-lactoglobulin could thus bind the three bioactive nutrients simultaneously to form protein-multi-ligand complexes. Beta-casein, an intrinsically unstructured but major milk protein, could also interact with resveratrol and folic acid to form complexes. These results suggest the potential to develop milk-protein-based complex carrier systems for encapsulation of multiple bioactive nutrients for functional food application and also pharmaceutical and medical uses. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=milk%20protein" title="milk protein">milk protein</a>, <a href="https://publications.waset.org/abstracts/search?q=bioactive%20nutrient" title=" bioactive nutrient"> bioactive nutrient</a>, <a href="https://publications.waset.org/abstracts/search?q=interaction" title=" interaction"> interaction</a>, <a href="https://publications.waset.org/abstracts/search?q=protection" title=" protection"> protection</a> </p> <a href="https://publications.waset.org/abstracts/32528/encapsulation-and-protection-of-bioactive-nutrients-based-on-ligand-binding-property-of-milk-proteins" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/32528.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">412</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">5676</span> Experimental Study of Sahara Climat Effect in Photovoltaic Solar Module</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=A.%20Benatiallah">A. Benatiallah</a>, <a href="https://publications.waset.org/abstracts/search?q=A.%20Hadjadj"> A. Hadjadj</a>, <a href="https://publications.waset.org/abstracts/search?q=D.%20Benatiallah"> D. Benatiallah</a>, <a href="https://publications.waset.org/abstracts/search?q=F.%20Abaidi"> F. Abaidi</a>, <a href="https://publications.waset.org/abstracts/search?q=A.%20Harrouz"> A. Harrouz</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Photovoltaic system is established as a reliable and economical source of electricity in rural and Sahara areas, especially in developing countries where the population is dispersed, has low consumption of energy and the grid power is not extended to these areas due to viability and financial problems. The production of energy by the photovoltaic system is very fluctuates and depend of meteorological conditions. Wind is a very important and often neglected parameter in the behavior of the solar module. The electric performances of a solar module to the silicon are very appreciable to the blows; in the present work we have studies the behavior of multi-crystal solar module according to the density of dust, and the principals electric feature of the solar module. An evaluation permits to affirm that a solar module under the effect of sand will collect a lower flux to the normal conditions. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=photovoltaic" title="photovoltaic">photovoltaic</a>, <a href="https://publications.waset.org/abstracts/search?q=multi-crystal%20module" title=" multi-crystal module"> multi-crystal module</a>, <a href="https://publications.waset.org/abstracts/search?q=experimental" title=" experimental"> experimental</a>, <a href="https://publications.waset.org/abstracts/search?q=effect%20of%20dust" title=" effect of dust"> effect of dust</a>, <a href="https://publications.waset.org/abstracts/search?q=performances" title=" performances"> performances</a> </p> <a href="https://publications.waset.org/abstracts/46063/experimental-study-of-sahara-climat-effect-in-photovoltaic-solar-module" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/46063.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">306</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">5675</span> Chitosan-Whey Protein Isolate Core-Shell Nanoparticles as Delivery Systems</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Zahra%20Yadollahi">Zahra Yadollahi</a>, <a href="https://publications.waset.org/abstracts/search?q=Marjan%20Motiei"> Marjan Motiei</a>, <a href="https://publications.waset.org/abstracts/search?q=Natalia%20Kazantseva"> Natalia Kazantseva</a>, <a href="https://publications.waset.org/abstracts/search?q=Petr%20Saha"> Petr Saha</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Chitosan (CS)-whey protein isolate (WPI) core-shell nanoparticles were synthesized through self-assembly of whey protein isolated polyanions and chitosan polycations in the presence of tripolyphosphate (TPP) as a crosslinker. The formation of this type of nanostructures with narrow particle size distribution is crucial for developing delivery systems since the functional characteristics highly depend on their sizes. To achieve this goal, the nanostructure was optimized by varying the concentrations of WPI, CS, and TPP in the reaction mixture. The chemical characteristics, surface morphology, and particle size of the nanoparticles were evaluated. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=whey%20protein%20isolated" title="whey protein isolated">whey protein isolated</a>, <a href="https://publications.waset.org/abstracts/search?q=chitosan" title=" chitosan"> chitosan</a>, <a href="https://publications.waset.org/abstracts/search?q=nanoparticles" title=" nanoparticles"> nanoparticles</a>, <a href="https://publications.waset.org/abstracts/search?q=delivery%20system" title=" delivery system"> delivery system</a> </p> <a href="https://publications.waset.org/abstracts/157111/chitosan-whey-protein-isolate-core-shell-nanoparticles-as-delivery-systems" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/157111.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">93</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">5674</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">5673</span> De Novo Design of Functional Metalloproteins for Biocatalytic Reactions</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Ketaki%20D.%20Belsare">Ketaki D. Belsare</a>, <a href="https://publications.waset.org/abstracts/search?q=Nicholas%20F.%20Polizzi"> Nicholas F. Polizzi</a>, <a href="https://publications.waset.org/abstracts/search?q=Lior%20Shtayer"> Lior Shtayer</a>, <a href="https://publications.waset.org/abstracts/search?q=William%20F.%20DeGrado"> William F. DeGrado</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Nature utilizes metalloproteins to perform chemical transformations with activities and selectivities that have long been the inspiration for design principles in synthetic and biological systems. The chemical reactivities of metalloproteins are directly linked to local environment effects produced by the protein matrix around the metal cofactor. A complete understanding of how the protein matrix provides these interactions would allow for the design of functional metalloproteins. The de novo computational design of proteins have been successfully used in design of active sites that bind metals like di-iron, zinc, copper containing cofactors; however, precisely designing active sites that can bind small molecule ligands (e.g., substrates) along with metal cofactors is still a challenge in the field. The de novo computational design of a functional metalloprotein that contains a purposefully designed substrate binding site would allow for precise control of chemical function and reactivity. Our research strategy seeks to elucidate the design features necessary to bind the cofactor protoporphyrin IX (hemin) in close proximity to a substrate binding pocket in a four helix bundle. First- and second-shell interactions are computationally designed to control orientation, electronic structure, and reaction pathway of the cofactor and substrate. The design began with a parameterized helical backbone that positioned a single histidine residue (as an axial ligand) to receive a second-shell H-bond from a Threonine on the neighboring helix. The metallo-cofactor, hemin was then manually placed in the binding site. A structural feature, pi-bulge was introduced to give substrate access to the protoporphyrin IX. These de novo metalloproteins are currently being tested for their activity towards hydroxylation and epoxidation. The de novo designed protein shows hydroxylation of aniline to 4-aminophenol. This study will help provide structural information of utmost importance in understanding de novo computational design variables impacting the functional activities of a protein. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=metalloproteins" title="metalloproteins">metalloproteins</a>, <a href="https://publications.waset.org/abstracts/search?q=protein%20design" title=" protein design"> protein design</a>, <a href="https://publications.waset.org/abstracts/search?q=de%20novo%20protein" title=" de novo protein"> de novo protein</a>, <a href="https://publications.waset.org/abstracts/search?q=biocatalysis" title=" biocatalysis"> biocatalysis</a> </p> <a href="https://publications.waset.org/abstracts/110017/de-novo-design-of-functional-metalloproteins-for-biocatalytic-reactions" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/110017.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">151</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">5672</span> Analytical Modeling of Globular Protein-Ferritin in α-Helical Conformation: A White Noise Functional Approach</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Vernie%20C.%20Convicto">Vernie C. Convicto</a>, <a href="https://publications.waset.org/abstracts/search?q=Henry%20P.%20Aringa"> Henry P. Aringa</a>, <a href="https://publications.waset.org/abstracts/search?q=Wilson%20I.%20Barredo"> Wilson I. Barredo</a> </p> <p class="card-text"><strong>Abstract:</strong></p> This study presents a conformational model of the helical structures of globular protein particularly ferritin in the framework of white noise path integral formulation by using Associated Legendre functions, Bessel and convolution of Bessel and trigonometric functions as modulating functions. The model incorporates chirality features of proteins and their helix-turn-helix sequence structural motif. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=globular%20protein" title="globular protein">globular protein</a>, <a href="https://publications.waset.org/abstracts/search?q=modulating%20function" title=" modulating function"> modulating function</a>, <a href="https://publications.waset.org/abstracts/search?q=white%20noise" title=" white noise"> white noise</a>, <a href="https://publications.waset.org/abstracts/search?q=winding%20probability" title=" winding probability"> winding probability</a> </p> <a href="https://publications.waset.org/abstracts/29779/analytical-modeling-of-globular-protein-ferritin-in-a-helical-conformation-a-white-noise-functional-approach" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/29779.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">476</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">5671</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">5670</span> Thrombophilic Risk Factors and Pregnancy Complications</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Hanan%20Azzam1">Hanan Azzam1</a>, <a href="https://publications.waset.org/abstracts/search?q=Nashwa%20Abousamra1"> Nashwa Abousamra1</a>, <a href="https://publications.waset.org/abstracts/search?q=Amany%20Mansour1"> Amany Mansour1</a>, <a href="https://publications.waset.org/abstracts/search?q=Yaser%20Abd%20El-dayem2"> Yaser Abd El-dayem2</a>, <a href="https://publications.waset.org/abstracts/search?q="></a>, <a href="https://publications.waset.org/abstracts/search?q=Solafa%20Elsharawy1">Solafa Elsharawy1</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Background: Inherited thrombophilias are a heterogenous group of conditions which have been implicated in a variety of pregnancy complications. More recently, deficiency of protein Z (PZ) has been liked to pregnancy complications, including preterm delivery. Aim: We designed this study to evaluate the association of inherited thrombophilias including [Protein C (PC), Protein S (PS), Anti thrombin III (ATIII) deficiency and activated protein C (APC) resistance] and protein Z deficiency with a variety of pregnancy complications. Patients and Methods: 60 women with different pregnancy complications, including 20 patients with preeclampsia, 20 patients with intrauterine growth resistance (IUGR), and 20 patients with intrauterine fetal death (IUFD), in addition to 30 healthy pregnant women were recruited for the present study. PC and free PS antigen, ATIII activity, modified functional APC-resistance, and PZ levels were determined. Results: There was no significant association between inherited thrombophilias and complicated pregnancies as regards PC deficiency (p=1.0), AT III and PS deficiency (p=0.312), and APC-resistance (P=0.083). PZ was significantly associated with complicated pregnancies (p=0.012). Patients with protein Z levels below 1.5 µg/ml were considered deficient. Accordingly, we demonstrated protein Z deficiency in 30% of complicated pregnancies (RR 6.0, 95% CI 1.29-27.90;p=0.022), 20% of preeclampsia (RR 3.5, 95% CI 0.57 – 21.28; P = 0.174), 40% of IUGR (RR 9.3 95% CI 1.72-50.61; P = 0.010) and 30% of IUFD (RR 6, 95% CI 1.07 – 33.64; P = 0.042). Conclusions: These findings indicate the absence of association of inherited thrombophilias, including PC, PS, AT III deficiency, and APC resistance with pregnancy complications. However, PZ deficiency is associated with increased risk of pregnancy complications, especially intrauterine growth restriction and intrauterine fetal death. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=protein%20C" title="protein C">protein C</a>, <a href="https://publications.waset.org/abstracts/search?q=protein%20S" title=" protein S"> protein S</a>, <a href="https://publications.waset.org/abstracts/search?q=thrombophelia" title=" thrombophelia"> thrombophelia</a>, <a href="https://publications.waset.org/abstracts/search?q=pregnancy" title=" pregnancy"> pregnancy</a>, <a href="https://publications.waset.org/abstracts/search?q=protein%20Z" title=" protein Z"> protein Z</a> </p> <a href="https://publications.waset.org/abstracts/144318/thrombophilic-risk-factors-and-pregnancy-complications" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/144318.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">234</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">5669</span> Designing Active Sites on Amicyanin Using Histidine S Plus Cobalt, and Measuring Their Functional Activity </h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Han-Bin%20Kim">Han-Bin Kim</a>, <a href="https://publications.waset.org/abstracts/search?q=Sooim%20Shin"> Sooim Shin</a>, <a href="https://publications.waset.org/abstracts/search?q=Moonsung%20Choi"> Moonsung Choi</a> </p> <p class="card-text"><strong>Abstract:</strong></p> There is a growing interest in introducing a desired functional group on enzymes in the field of protein engineering. In here, various redox centers were newly created using histidine tag, which is widely used for protein purification, plus cobalt in one of cupredoxins, amicyanin. The coordination of Cobalt-His tag and reactivity of the Co²⁺ loaded His-tag also were characterized. 3xHis-tag, 6xHis-tag, and 9xHis-tag were introduced on amicyanin by site-directed mutagenesis, and then Co²⁺ was loaded on each His-tagged amicyanin. The spectral changes at 330 nm corresponding to cobalt binding on His-tag site indicated the binding ratio of 3xHis-tag, 6xHis-tag, and 9xHis-tag to cobalt as 1:1, 1:2, 1:3 respectively. Based on kinetic studies of binding cobalt to 3xHis-tag, 6xHis-tag, and 9xHis-tagged amicyanin, the nature of the sites was elucidated. In addition, internal electron transfer properties between Cu¹⁺ site and engineered site of amicyanin were determined. These results provide insight into improvement of metal coordination and alternation of the redox properties of metal as a new catalytic site on proteins. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=amicyanin" title="amicyanin">amicyanin</a>, <a href="https://publications.waset.org/abstracts/search?q=cobalt" title=" cobalt"> cobalt</a>, <a href="https://publications.waset.org/abstracts/search?q=histidine" title=" histidine"> histidine</a>, <a href="https://publications.waset.org/abstracts/search?q=protein%20engineering" title=" protein engineering"> protein engineering</a> </p> <a href="https://publications.waset.org/abstracts/77448/designing-active-sites-on-amicyanin-using-histidine-s-plus-cobalt-and-measuring-their-functional-activity" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/77448.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">162</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=protein%20functional%20module&page=2">2</a></li> <li class="page-item"><a class="page-link" href="https://publications.waset.org/abstracts/search?q=protein%20functional%20module&page=3">3</a></li> <li class="page-item"><a class="page-link" href="https://publications.waset.org/abstracts/search?q=protein%20functional%20module&page=4">4</a></li> <li class="page-item"><a class="page-link" href="https://publications.waset.org/abstracts/search?q=protein%20functional%20module&page=5">5</a></li> <li class="page-item"><a class="page-link" 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