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Oxidase (DAO) enzyme</title> <meta name="description" content="Search results for: D-amino Acid Oxidase (DAO) enzyme"> <meta name="keywords" content="D-amino Acid Oxidase (DAO) enzyme"> <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" /> 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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="D-amino Acid Oxidase (DAO) enzyme"> <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> 4111</div> </div> </div> </div> <h1 class="mt-3 mb-3 text-center" style="font-size:1.6rem;">Search results for: D-amino Acid Oxidase (DAO) enzyme</h1> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">4111</span> Optimization of Radiation Therapy with a Nanotechnology Based Enzymatic Therapy</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=R.%20D.%20Esposito">R. D. Esposito</a>, <a href="https://publications.waset.org/abstracts/search?q=V.%20M.%20Barber%C3%A1"> V. M. Barberá</a>, <a href="https://publications.waset.org/abstracts/search?q=P.%20Garc%C3%ADa%20Morales"> P. García Morales</a>, <a href="https://publications.waset.org/abstracts/search?q=P.%20Dorado%20Rodr%C3%ADguez"> P. Dorado Rodríguez</a>, <a href="https://publications.waset.org/abstracts/search?q=J.%20Sanz"> J. Sanz</a>, <a href="https://publications.waset.org/abstracts/search?q=M.%20Fuentes"> M. Fuentes</a>, <a href="https://publications.waset.org/abstracts/search?q=D.%20Planes%20Meseguer"> D. Planes Meseguer</a>, <a href="https://publications.waset.org/abstracts/search?q=M.%20Saceda"> M. Saceda</a>, <a href="https://publications.waset.org/abstracts/search?q=L.%20Fern%C3%A1ndez%20Fornos"> L. Fernández Fornos</a>, <a href="https://publications.waset.org/abstracts/search?q=M.%20P.%20Ventero"> M. P. Ventero</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Results obtained by our group on glioblastoma multiforme (GBM) primary cultures , show a dramatic potentiation of radiation effects when 2 units/ml of D-amino acid oxidase (DAO) enzyme are added, free or immobilized in magnetic nanoparticles, to irradiated samples just after the irradiation. Cell cultures were exposed to radiation doses of 7Gy and 15Gy of 6 MV photons from a clinical linear accelerator. At both doses, we observed a clear enhancing effect of radiation-induced damages due to the addition of DAO. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=D-amino%20Acid%20Oxidase%20%28DAO%29%20enzyme" title="D-amino Acid Oxidase (DAO) enzyme">D-amino Acid Oxidase (DAO) enzyme</a>, <a href="https://publications.waset.org/abstracts/search?q=magnetic%20particles" title=" magnetic particles"> magnetic particles</a>, <a href="https://publications.waset.org/abstracts/search?q=nanotechnology" title=" nanotechnology"> nanotechnology</a>, <a href="https://publications.waset.org/abstracts/search?q=radiation%20therapy%20enhancement" title=" radiation therapy enhancement"> radiation therapy enhancement</a> </p> <a href="https://publications.waset.org/abstracts/29814/optimization-of-radiation-therapy-with-a-nanotechnology-based-enzymatic-therapy" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/29814.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">523</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">4110</span> Comparative Electrochemical Studies of Enzyme-Based and Enzyme-less Graphene Oxide-Based Nanocomposite as Glucose Biosensor</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Chetna%20Tyagi.%20G.%20B.%20V.%20S.%20Lakshmi">Chetna Tyagi. G. B. V. S. Lakshmi</a>, <a href="https://publications.waset.org/abstracts/search?q=Ambuj%20Tripathi"> Ambuj Tripathi</a>, <a href="https://publications.waset.org/abstracts/search?q=D.%20K.%20Avasthi"> D. K. Avasthi</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Graphene oxide provides a good host matrix for preparing nanocomposites due to the different functional groups attached to its edges and planes. Being biocompatible, it is used in therapeutic applications. As enzyme-based biosensor requires complicated enzyme purification procedure, high fabrication cost and special storage conditions, we need enzyme-less biosensors for use even in a harsh environment like high temperature, varying pH, etc. In this work, we have prepared both enzyme-based and enzyme-less graphene oxide-based biosensors for glucose detection using glucose-oxidase as enzyme and gold nanoparticles, respectively. These samples were characterized using X-ray diffraction, UV-visible spectroscopy, scanning electron microscopy, and transmission electron microscopy to confirm the successful synthesis of the working electrodes. Electrochemical measurements were performed for both the working electrodes using a 3-electrode electrochemical cell. Cyclic voltammetry curves showed the homogeneous transfer of electron on the electrodes in the scan range between -0.2V to 0.6V. The sensing measurements were performed using differential pulse voltammetry for the glucose concentration varying from 0.01 mM to 20 mM, and sensing was improved towards glucose in the presence of gold nanoparticles. Gold nanoparticles in graphene oxide nanocomposite played an important role in sensing glucose in the absence of enzyme, glucose oxidase, as evident from these measurements. The selectivity was tested by measuring the current response of the working electrode towards glucose in the presence of the other common interfering agents like cholesterol, ascorbic acid, citric acid, and urea. The enzyme-less working electrode also showed storage stability for up to 15 weeks, making it a suitable glucose biosensor. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=electrochemical" title="electrochemical">electrochemical</a>, <a href="https://publications.waset.org/abstracts/search?q=enzyme-less" title=" enzyme-less"> enzyme-less</a>, <a href="https://publications.waset.org/abstracts/search?q=glucose" title=" glucose"> glucose</a>, <a href="https://publications.waset.org/abstracts/search?q=gold%20nanoparticles" title=" gold nanoparticles"> gold nanoparticles</a>, <a href="https://publications.waset.org/abstracts/search?q=graphene%20oxide" title=" graphene oxide"> graphene oxide</a>, <a href="https://publications.waset.org/abstracts/search?q=nanocomposite" title=" nanocomposite"> nanocomposite</a> </p> <a href="https://publications.waset.org/abstracts/123186/comparative-electrochemical-studies-of-enzyme-based-and-enzyme-less-graphene-oxide-based-nanocomposite-as-glucose-biosensor" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/123186.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">141</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">4109</span> Investigations of Metals and Metal-Antibrowning Agent Effects on Polyphenol Oxidase Activity from Red Poppy Leaf </h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Gulnur%20Arabaci">Gulnur Arabaci</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Heavy metals are one of the major groups of contaminants in the environment and many of them are toxic even at very low concentration in plants and animals. However, some metals play important roles in the biological function of many enzymes in living organisms. Metals such as zinc, iron, and cooper are important for survival and activity of enzymes in plants, however heavy metals can inhibit enzyme which is responsible for defense system of plants. Polyphenol oxidase (PPO) is a copper-containing metalloenzyme which is responsible for enzymatic browning reaction of plants. Enzymatic browning is a major problem for the handling of vegetables and fruits in food industry. It can be increased and effected with many different futures such as metals in the nature and ground. In the present work, PPO was isolated and characterized from green leaves of red poppy plant (Papaver rhoeas). Then, the effect of some known antibrowning agents which can form complexes with metals and metals were investigated on the red poppy PPO activity. The results showed that glutathione was the most potent inhibitory effect on PPO activity. Cu(II) and Fe(II) metals increased the enzyme activities however, Sn(II) had the maximum inhibitory effect and Zn(II) and Pb(II) had no significant effect on the enzyme activity. In order to reduce the effect of heavy metals, the effects of metal-antibrowning agent complexes on the PPO activity were determined. EDTA and metal complexes had no significant effect on the enzyme. L-ascorbic acid and metal complexes decreased but L-ascorbic acid-Cu(II)-complex had no effect. Glutathione–metal complexes had the best inhibitory effect on Red poppy leaf PPO activity. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=inhibition" title="inhibition">inhibition</a>, <a href="https://publications.waset.org/abstracts/search?q=metal" title=" metal"> metal</a>, <a href="https://publications.waset.org/abstracts/search?q=red%20poppy" title=" red poppy"> red poppy</a>, <a href="https://publications.waset.org/abstracts/search?q=poly%20phenol%20oxidase%20%28PPO%29" title=" poly phenol oxidase (PPO)"> poly phenol oxidase (PPO)</a> </p> <a href="https://publications.waset.org/abstracts/16692/investigations-of-metals-and-metal-antibrowning-agent-effects-on-polyphenol-oxidase-activity-from-red-poppy-leaf" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/16692.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">328</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">4108</span> Effect of Vinclozolin on Some Biochemical Parameters of Galleria mellonella (Lepidoptera: Pyralidae)</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Rahile%20Ozturk">Rahile Ozturk</a>, <a href="https://publications.waset.org/abstracts/search?q=Esra%20Maltas"> Esra Maltas</a> </p> <p class="card-text"><strong>Abstract:</strong></p> This study aimed to determine the effect of vinclozolin on some biochemical characteristics of Galleria mellonella (Lepidoptera: Pyralidae) which is an economically harmful species damaging the honeycomb in beekeeping. For experimental groups, the eggs obtained from stock were dropped into the mixed feed of vinclozolin at different doses (20, 40 and 60 ppm) and had the larvae fed with this feed. As result of the addition of vinclozolin at concentrations of 20, 40 and 60 ppm, glycogen contents of G. mellonella were determined and a significant reduction in the amount of glycogen was observed with increasing concentration of vinclozolin. In this study, activity of catalase enzyme, particularly effective in defense mechanism, activity of xanthine oxidase involved in nucleotide metabolism and activity of glucose oxidase in the metabolism of carbohydrates were measured. When compared with the results from control groups, the enzyme activities of the larvaes fed with the feed including 20, 40 and 60 ppm of vinclozolin were observed to vary or remain constant. Accordingly, glucose oxidase and catalase activities increased with the increase in amount of vinclozolin in the feed and the activity of xanthine oxidase remained stable. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=Catalase" title="Catalase">Catalase</a>, <a href="https://publications.waset.org/abstracts/search?q=Galleria%20mellonella" title=" Galleria mellonella"> Galleria mellonella</a>, <a href="https://publications.waset.org/abstracts/search?q=glucose%20oxidase" title=" glucose oxidase"> glucose oxidase</a>, <a href="https://publications.waset.org/abstracts/search?q=vinclozolin" title=" vinclozolin"> vinclozolin</a>, <a href="https://publications.waset.org/abstracts/search?q=xanthine%20oxidase." title=" xanthine oxidase."> xanthine oxidase.</a> </p> <a href="https://publications.waset.org/abstracts/43860/effect-of-vinclozolin-on-some-biochemical-parameters-of-galleria-mellonella-lepidoptera-pyralidae" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/43860.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">297</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">4107</span> Effect of Acetic Acid Fermentation on Bioactive Components and Anti-Xanthine Oxidase Activities in Vinegar Brewed from Monascus-Fermented Soybeans</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Kyung-Soon%20Choi">Kyung-Soon Choi</a>, <a href="https://publications.waset.org/abstracts/search?q=Ji-Young%20Hwang"> Ji-Young Hwang</a>, <a href="https://publications.waset.org/abstracts/search?q=Young-Hee%20Pyo"> Young-Hee Pyo</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Vinegars have been used as an alternative remedy for treating gout, but the scientific basis remains to be elucidated. In this study, acetic acid fermentation was applied for the first time to Monascus-fermented soybeans to examine its effect on the bioactive components together with the xanthine oxidase inhibitory (XOI) activity of the soy vinegar. The content of total phenols (0.47~0.97 mg gallic acid equivalents/mL) and flavonoids (0.18~0.39 mg quercetin equivallents/mL) were spectrophotometrically determined, and the content of organic acid (10.22~59.76 mg/mL) and isoflavones (6.79~7.46 mg/mL) were determined using HPLC-UV. The analytical method for ubiquinones (0.079~0.276 μg/mL) employed saponification before solvent extraction and quantification using LC-MS. Soy vinegar also showed significant XOI (95.3%) after 20 days of acetic acid fermentation at 30 °C. The results suggest that soy vinegar has potential as a novel medicinal food. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=acetic%20acid%20fermentation" title="acetic acid fermentation">acetic acid fermentation</a>, <a href="https://publications.waset.org/abstracts/search?q=bioactive%20component" title=" bioactive component"> bioactive component</a>, <a href="https://publications.waset.org/abstracts/search?q=soy%20vinegar" title=" soy vinegar"> soy vinegar</a>, <a href="https://publications.waset.org/abstracts/search?q=xanthine%20oxidase%20inhibitory%20activity" title=" xanthine oxidase inhibitory activity"> xanthine oxidase inhibitory activity</a> </p> <a href="https://publications.waset.org/abstracts/66060/effect-of-acetic-acid-fermentation-on-bioactive-components-and-anti-xanthine-oxidase-activities-in-vinegar-brewed-from-monascus-fermented-soybeans" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/66060.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">383</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">4106</span> Role of Fish Hepatic Aldehyde Oxidase in Oxidative In Vitro Metabolism of Phenanthridine Heterocyclic Aromatic Compound</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Khaled%20S.%20Al%20Salhen">Khaled S. Al Salhen</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Aldehyde oxidase is molybdo-flavoenzyme involved in the oxidation of hundreds of endogenous and exogenous and N-heterocyclic compounds and environmental pollutants. Uncharged N-heterocyclic aromatic compounds such phenanthridine are commonly distributed pollutants in soil, air, sediments, surface water and groundwater, and in animal and plant tissues. Phenanthridine as uncharged N-heterocyclic aromatic compound was incubated with partially purified aldehyde oxidase from rainbow trout fish liver. Reversed-phase HLPC method was used to separate the oxidation products from phenanthridine and the metabolite was identified. The 6(5H)-phenanthridinone was identified the major metabolite by partially purified aldehyde oxidase from fish liver. Kinetic constant for the oxidation reactions were determined spectrophotometrically and showed that this substrate has a good affinity (Km = 78 ± 7.6 µM) for hepatic aldehyde oxidase, coupled with a relatively high oxidation rate (0.77± 0.03 nmol/min/mg protein). In addition, the kinetic parameters of hepatic fish aldehyde oxidase towards the phenanthridine substrate indicate that in vitro biotransformation by hepatic fish aldehyde oxidase will be a significant pathway. This study confirms that partially purified aldehyde oxidase from fish liver is indeed the enzyme responsible for the in vitro production 6(5H)-phenanthridinone metabolite as it is a major metabolite by mammalian aldehyde oxidase. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=aldehyde%20oxidase" title="aldehyde oxidase">aldehyde oxidase</a>, <a href="https://publications.waset.org/abstracts/search?q=fish" title=" fish"> fish</a>, <a href="https://publications.waset.org/abstracts/search?q=phenanthridine" title=" phenanthridine"> phenanthridine</a>, <a href="https://publications.waset.org/abstracts/search?q=specificity" title=" specificity"> specificity</a> </p> <a href="https://publications.waset.org/abstracts/3951/role-of-fish-hepatic-aldehyde-oxidase-in-oxidative-in-vitro-metabolism-of-phenanthridine-heterocyclic-aromatic-compound" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/3951.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">364</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">4105</span> Bienzymatic Nanocomposites Biosensors Complexed with Gold Nanoparticles, Polyaniline, Recombinant MN Peroxidase from Corn, and Glucose Oxidase to Measure Glucose</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Anahita%20Izadyar">Anahita Izadyar</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Using a recombinant enzyme derived from corn and a simple modification, we are fabricating a facile, fast, and cost-beneficial novel biosensor to measure glucose. We are applying Plant Produced Mn Peroxidase (PPMP), glucose oxidase (GOx), polyaniline (PANI) as conductive polymer and gold nanoparticles (AuNPs) on Au electrode using electrochemical response to detect glucose. We applied the entrapment method of enzyme composition, which is generally used to immobilize conductive polymer and facilitate electron transfer from the enzyme oxidation-reduction center to the sample solution. In this work, the oxidation of glucose on the modified gold electrode was quantified with Linear Sweep Voltammetry(LSV). We expect that the modified biosensor has the potential for monitoring various biofluids. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=plant-produced%20manganese%20peroxidase" title="plant-produced manganese peroxidase">plant-produced manganese peroxidase</a>, <a href="https://publications.waset.org/abstracts/search?q=enzyme-based%20biosensors" title=" enzyme-based biosensors"> enzyme-based biosensors</a>, <a href="https://publications.waset.org/abstracts/search?q=glucose" title=" glucose"> glucose</a>, <a href="https://publications.waset.org/abstracts/search?q=modified%20gold%20nanoparticles%20electrode" title=" modified gold nanoparticles electrode"> modified gold nanoparticles electrode</a>, <a href="https://publications.waset.org/abstracts/search?q=polyaniline" title=" polyaniline"> polyaniline</a> </p> <a href="https://publications.waset.org/abstracts/141685/bienzymatic-nanocomposites-biosensors-complexed-with-gold-nanoparticles-polyaniline-recombinant-mn-peroxidase-from-corn-and-glucose-oxidase-to-measure-glucose" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/141685.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">200</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">4104</span> Amperometric Biosensor for Glucose Determination Based on a Recombinant Mn Peroxidase from Corn Cross-linked to a Gold Electrode</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Anahita%20Izadyar">Anahita Izadyar</a>, <a href="https://publications.waset.org/abstracts/search?q=My%20Ni%20Van"> My Ni Van</a>, <a href="https://publications.waset.org/abstracts/search?q=Kayleigh%20Amber%20Rodriguez"> Kayleigh Amber Rodriguez</a>, <a href="https://publications.waset.org/abstracts/search?q=Ilwoo%20Seok"> Ilwoo Seok</a>, <a href="https://publications.waset.org/abstracts/search?q=Elizabeth%20E.%20Hood"> Elizabeth E. Hood</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Using a recombinant enzyme derived from corn and a simple modification, we fabricated a facile, fast, and cost-beneficial biosensor to measure glucose. The Nafion/ Plant Produced Mn Peroxidase (PPMP)– glucose oxidase (GOx)- Bovine serum albumin (BSA) /Au electrode showed an excellent amperometric response to detect glucose. This biosensor is capable of responding to a wide range of glucose—20.0 µM−15.0 mM and has a lower detection limit (LOD) of 2.90µM. The reproducibility response using six electrodes is also very substantial and indicates the high capability of this biosensor to detect a wide range of 3.10±0.19µM to 13.2±1.8 mM glucose concentration. Selectivity of this electrode was investigated in an optimized experimental solution contains 10% diet green tea with citrus containing ascorbic acid (AA), and citric acid (CA) in a wide concentration of glucose at 0.02 to 14.0mM with an LOD of 3.10µM. Reproducibility was also investigated using 4 electrodes in this sample and shows notable results in the wide concentration range of 3.35±0.45µM to of 13.0 ± 0.81 mM. We also used other voltammetry methods to evaluate this biosensor. We applied linear sweep voltammetry (LSV) and this technique shows a wide range of 0.10−15.0 mM to detect glucose with a lower detection limit of 19.5µM. The performance and strength of this enzyme biosensor were the simplicity, wide linear ranges, sensitivities, selectivity, and low limits of detection. We expect that the modified biosensor has the potential for monitoring various biofluids. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=plant-produced%20manganese%20peroxidase" title="plant-produced manganese peroxidase">plant-produced manganese peroxidase</a>, <a href="https://publications.waset.org/abstracts/search?q=enzyme-based%20biosensors" title=" enzyme-based biosensors"> enzyme-based biosensors</a>, <a href="https://publications.waset.org/abstracts/search?q=glucose" title=" glucose"> glucose</a>, <a href="https://publications.waset.org/abstracts/search?q=modified%20gold%20electrode" title=" modified gold electrode"> modified gold electrode</a>, <a href="https://publications.waset.org/abstracts/search?q=glucose%20oxidase" title=" glucose oxidase"> glucose oxidase</a> </p> <a href="https://publications.waset.org/abstracts/133907/amperometric-biosensor-for-glucose-determination-based-on-a-recombinant-mn-peroxidase-from-corn-cross-linked-to-a-gold-electrode" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/133907.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">139</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">4103</span> High Pressure Processing of Jackfruit Bulbs: Effect on Color, Nutrient Profile and Enzyme Inactivation</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Jyoti%20Kumari">Jyoti Kumari</a>, <a href="https://publications.waset.org/abstracts/search?q=Pavuluri%20Srinivasa%20Rao"> Pavuluri Srinivasa Rao</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Jackfruit (ArtocarpusheterophyllusL.) is an underutilized yet highly nutritious fruit with unique flavour, known for its therapeutic and culinary properties. Fresh jackfruit bulb has a very short shelf life due to high moisture and sugar content leading to microbial and enzymatic browning, hindering its consumer acceptability and marketability. An attempt has been made for the preservation of the ripe jackfruit bulbs, by the application of high pressure (HP) over a range of 200-500 MPa at ambient temperature for dwell times ranging from 5 to 20 min. The physicochemical properties of jackfruit bulbs such as the pH, TSS, and titrable acidity were not affected by the pressurization process. The ripening index of the fruit bulb also decreased following HP treatment. While the ascorbic acid and antioxidant activity of jackfruit bulb were well retained by high pressure processing (HPP), the total phenols and carotenoids showed a slight increase. The HPP significantly affected the colour and textural properties of jackfruit bulb. High pressure processing was highly effective in reducing the browning index of jackfruit bulbs in comparison to untreated bulbs. The firmness of the bulbs improved upon the pressure treatment with longer dwelling time. The polyphenol oxidase has been identified as the most prominent oxidative enzyme in the jackfruit bulb. The enzymatic activity of polyphenol oxidase and peroxidase were significantly reduced by up to 40% following treatment at 400 MPa/15 min. HPP of jackfruit bulbs at ambient temperatures is shown to be highly beneficial in improving the shelf stability, retaining its nutrient profile, color, and appearance while ensuring the maximum inactivation of the spoilage enzymes. <p class="card-text"><strong>Keywords:</strong> <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=ascorbic%20acid" title=" ascorbic acid"> ascorbic acid</a>, <a href="https://publications.waset.org/abstracts/search?q=carotenoids" title=" carotenoids"> carotenoids</a>, <a href="https://publications.waset.org/abstracts/search?q=color" title=" color"> color</a>, <a href="https://publications.waset.org/abstracts/search?q=HPP-high%20pressure%20processing" title=" HPP-high pressure processing"> HPP-high pressure processing</a>, <a href="https://publications.waset.org/abstracts/search?q=jackfruit%20bulbs" title=" jackfruit bulbs"> jackfruit bulbs</a>, <a href="https://publications.waset.org/abstracts/search?q=polyphenol%20oxidase" title=" polyphenol oxidase"> polyphenol oxidase</a>, <a href="https://publications.waset.org/abstracts/search?q=peroxidase" title=" peroxidase"> peroxidase</a>, <a href="https://publications.waset.org/abstracts/search?q=total%20phenolic%20content" title=" total phenolic content"> total phenolic content</a> </p> <a href="https://publications.waset.org/abstracts/80545/high-pressure-processing-of-jackfruit-bulbs-effect-on-color-nutrient-profile-and-enzyme-inactivation" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/80545.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">174</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">4102</span> The Improved Biofuel Cell for Electrical Power Generation from Wastewaters</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=M.%20S.%20Kilic">M. S. Kilic</a>, <a href="https://publications.waset.org/abstracts/search?q=S.%20Korkut"> S. Korkut</a>, <a href="https://publications.waset.org/abstracts/search?q=B.%20Hazer"> B. Hazer</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Newly synthesized Polypropylene-g-Polyethylene glycol polymer was first time used for a compartment-less enzymatic fuel cell. Working electrodes based on Polypropylene-g-Polyethylene glycol were operated as unmediated and mediated system (with ferrocene and gold/cobalt oxide nanoparticles). Glucose oxidase and bilirubin oxidase was selected as anodic and cathodic enzyme, respectively. Glucose was used as fuel in a single-compartment and membrane-less cell. Maximum power density was obtained as 0.65 nW cm-2, 65 nW cm-2, and 23500 nW cm-2 from the unmediated, ferrocene and gold/cobalt oxide modified polymeric film, respectively. Power density was calculated to be ~16000 nW cm-2 for undiluted wastewater sample with gold/cobalt oxide nanoparticles including system. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=bilirubin%20oxidase" title="bilirubin oxidase">bilirubin oxidase</a>, <a href="https://publications.waset.org/abstracts/search?q=enzymatic%20fuel%20cell" title=" enzymatic fuel cell"> enzymatic fuel cell</a>, <a href="https://publications.waset.org/abstracts/search?q=glucose%20oxidase" title=" glucose oxidase"> glucose oxidase</a>, <a href="https://publications.waset.org/abstracts/search?q=nanoparticles" title=" nanoparticles"> nanoparticles</a> </p> <a href="https://publications.waset.org/abstracts/16725/the-improved-biofuel-cell-for-electrical-power-generation-from-wastewaters" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/16725.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">263</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">4101</span> Reusability of Coimmobilized Enzymes</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Aleksandra%20%C5%81ochowicz">Aleksandra Łochowicz</a>, <a href="https://publications.waset.org/abstracts/search?q=Daria%20%C5%9Awi%C4%99tochowska"> Daria Świętochowska</a>, <a href="https://publications.waset.org/abstracts/search?q=Loredano%20Pollegioni"> Loredano Pollegioni</a>, <a href="https://publications.waset.org/abstracts/search?q=Nazim%20Ocal"> Nazim Ocal</a>, <a href="https://publications.waset.org/abstracts/search?q=Franck%20Charmantray"> Franck Charmantray</a>, <a href="https://publications.waset.org/abstracts/search?q=Laurence%20Hecquet"> Laurence Hecquet</a>, <a href="https://publications.waset.org/abstracts/search?q=Katarzyna%20Szyma%C5%84ska"> Katarzyna Szymańska</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Multienzymatic cascade reactions are nowadays widely used in pharmaceutical, chemical and cosmetics industries to produce high valuable compounds. They can be carried out in two ways, step by step and one-pot. If two or more enzymes are in the same reaction vessel is necessary to work out the compromise to run the reaction in optimal conditions for each enzyme. So far most of the reports of multienzymatic cascades concern on usage of free enzymes. Unfortunately using free enzymes as catalysts of reactions accomplish high cost. What is more, free enzymes are soluble in solvents which makes reuse impossible. To overcome this obstacle enzymes can be immobilized what provides heterogeneity of biocatalyst that enables reuse and easy separation of the enzyme from solvents and reaction products. Usually, immobilization increase also the thermal and operational stability of enzyme. The advantages of using immobilized multienzymes are enhanced enzyme stability, improved cascade enzymatic activity via substrate channeling, and ease of recovery for reuse. The one-pot immobilized multienzymatic cascade can be carried out in mixed or coimmobilized type. When biocatalysts are coimmobilized on the same carrier the are in close contact to each other which increase the reaction rate and catalytic efficiency, and eliminate the lag time. However, in this type providing the optimal conditions both in the process of immobilization and cascade reaction for each enzyme is complicated. Herein, we examined immobilization of 3 enzymes: D-amino acid oxidase from Rhodotorula gracilis, commercially available catalase and transketolase from Geobacillus stearothermophilus. As a support we used silica monoliths with hierarchical structure of pores. Then we checked their stability and reusability in one-pot cascade of L-erythrulose and hydroxypuryvate acid synthesis. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=biocatalysts" title="biocatalysts">biocatalysts</a>, <a href="https://publications.waset.org/abstracts/search?q=enzyme%20immobilization" title=" enzyme immobilization"> enzyme immobilization</a>, <a href="https://publications.waset.org/abstracts/search?q=multienzymatic%20reaction" title=" multienzymatic reaction"> multienzymatic reaction</a>, <a href="https://publications.waset.org/abstracts/search?q=silica%20carriers" title=" silica carriers"> silica carriers</a> </p> <a href="https://publications.waset.org/abstracts/152282/reusability-of-coimmobilized-enzymes" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/152282.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">150</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">4100</span> Spectrophotometric Detection of Histidine Using Enzyme Reaction and Examination of Reaction Conditions</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Akimitsu%20Kugimiya">Akimitsu Kugimiya</a>, <a href="https://publications.waset.org/abstracts/search?q=Kouhei%20Iwato"> Kouhei Iwato</a>, <a href="https://publications.waset.org/abstracts/search?q=Toru%20Saito"> Toru Saito</a>, <a href="https://publications.waset.org/abstracts/search?q=Jiro%20Kohda"> Jiro Kohda</a>, <a href="https://publications.waset.org/abstracts/search?q=Yasuhisa%20Nakano"> Yasuhisa Nakano</a>, <a href="https://publications.waset.org/abstracts/search?q=Yu%20Takano"> Yu Takano</a> </p> <p class="card-text"><strong>Abstract:</strong></p> The measurement of amino acid content is reported to be useful for the diagnosis of several types of diseases, including lung cancer, gastric cancer, colorectal cancer, breast cancer, prostate cancer, and diabetes. The conventional detection methods for amino acid are high-performance liquid chromatography (HPLC) and liquid chromatography-mass spectrometry (LC-MS), but they have several drawbacks as the equipment is cumbersome and the techniques are costly in terms of time and costs. In contrast, biosensors and biosensing methods provide more rapid and facile detection strategies that use simple equipment. The authors have reported a novel approach for the detection of each amino acid that involved the use of aminoacyl-tRNA synthetase (aaRS) as a molecular recognition element because aaRS is expected to a selective binding ability for corresponding amino acid. The consecutive enzymatic reactions used in this study are as follows: aaRS binds to its cognate amino acid and releases inorganic pyrophosphate. Hydrogen peroxide (H₂O₂) was produced by the enzyme reactions of inorganic pyrophosphatase and pyruvate oxidase. The Trinder’s reagent was added into the reaction mixture, and the absorbance change at 556 nm was measured using a microplate reader. In this study, an amino acid-sensing method using histidyl-tRNA synthetase (HisRS; histidine-specific aaRS) as molecular recognition element in combination with the Trinder’s reagent spectrophotometric method was developed. The quantitative performance and selectivity of the method were evaluated, and the optimal enzyme reaction and detection conditions were determined. The authors developed a simple and rapid method for detecting histidine with a combination of enzymatic reaction and spectrophotometric detection. In this study, HisRS was used to detect histidine, and the reaction and detection conditions were optimized for quantitation of these amino acids in the ranges of 1–100 µM histidine. The detection limits are sufficient to analyze these amino acids in biological fluids. This work was partly supported by Hiroshima City University Grant for Special Academic Research (General Studies). <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=amino%20acid" title="amino acid">amino acid</a>, <a href="https://publications.waset.org/abstracts/search?q=aminoacyl-tRNA%20synthetase" title=" aminoacyl-tRNA synthetase"> aminoacyl-tRNA synthetase</a>, <a href="https://publications.waset.org/abstracts/search?q=biosensing" title=" biosensing"> biosensing</a>, <a href="https://publications.waset.org/abstracts/search?q=enzyme%20reaction" title=" enzyme reaction"> enzyme reaction</a> </p> <a href="https://publications.waset.org/abstracts/70824/spectrophotometric-detection-of-histidine-using-enzyme-reaction-and-examination-of-reaction-conditions" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/70824.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">284</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">4099</span> Synthesis and Anti-Inflammatory Activity of Pyrazol-3-yl Thiazole 4-Carboxylic Acid Derivatives Targeting Enzyme in the Leukotriene Pathway</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Shweta%20Sinha">Shweta Sinha</a>, <a href="https://publications.waset.org/abstracts/search?q=Mukesh%20Doble"> Mukesh Doble</a>, <a href="https://publications.waset.org/abstracts/search?q=Manju%20S.%20L."> Manju S. L.</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Pyrazole scaffold is an important group of compound in heterocyclic chemistry and is found to possess numerous uses in chemistry. Pyrazole derivatives are also known to possess important biological activities including antitumor, antimicrobial, antiviral, antifungal, anticancer and anti-inflammatory. Inflammation is associated with pain, allergy and asthma. Leukotrienes are mediators of various inflammatory and allergic disorders. 5-Lipoxygenase (5-LOX) is an important enzyme involved in the biosynthesis of leukotrienes and metabolism of arachidonic acid (AA) and thus targeted for anti-inflammation. In vitro inhibitory activity of pyrazol-3-yl thiazole 4-carboxylic acid derivatives is tested against enzyme 5-LOX. Most of these compounds exhibit good inhibitory activity against this enzyme. Binding mode study of these compounds is determined by computational tool. Further experiments are being done to understand the mechanism of action of these compounds in inhibiting this enzyme. To conclude, these compounds appear to be a promising target in drug design against 5-LOX. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=inflammation" title="inflammation">inflammation</a>, <a href="https://publications.waset.org/abstracts/search?q=inhibition" title=" inhibition"> inhibition</a>, <a href="https://publications.waset.org/abstracts/search?q=5-lipoxygenase" title=" 5-lipoxygenase"> 5-lipoxygenase</a>, <a href="https://publications.waset.org/abstracts/search?q=pyrazole" title=" pyrazole"> pyrazole</a> </p> <a href="https://publications.waset.org/abstracts/71661/synthesis-and-anti-inflammatory-activity-of-pyrazol-3-yl-thiazole-4-carboxylic-acid-derivatives-targeting-enzyme-in-the-leukotriene-pathway" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/71661.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">244</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">4098</span> The Creation of a Yeast Model for 5-oxoproline Accumulation</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Pratiksha%20Dubey">Pratiksha Dubey</a>, <a href="https://publications.waset.org/abstracts/search?q=Praveen%20Singh"> Praveen Singh</a>, <a href="https://publications.waset.org/abstracts/search?q=Shantanu%20Sen%20Gupta"> Shantanu Sen Gupta</a>, <a href="https://publications.waset.org/abstracts/search?q=Anand%20K.%20Bachhawat"> Anand K. Bachhawat</a> </p> <p class="card-text"><strong>Abstract:</strong></p> 5-oxoproline (pyroglutamic acid) is a cyclic lactam of glutamic acid. In the cell, it can be produced by several different pathways and is metabolized into glutamate with the help of the 5-oxoprolinase enzyme (OPLAH or OXP1). The inhibition of 5-oxoprolinase enzyme in mammals was found to result in heart failure and is thought to be a consequence of oxidative stress [1]. To analyze the consequences of 5-oxoproline accumulation more clearly, we are generating models for 5-oxoproline accumulation in yeast. The 5-oxoproline accumulation model in yeast is being developed by two different strategies. The first one is by overexpression of the mouse  -glutamylcyclotransferase enzyme. It degrades -glu-met dipeptide into 5-oxoproline and methionine taken by the cell from the medium. The second strategy is by providing high concentration of 5-oxoproline externally to the yeast cells. The intracellular 5-oxoproline levels in both models are being evaluated. In addition, the metabolic and cellular consequences are being investigated. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=5-oxoproline" title="5-oxoproline">5-oxoproline</a>, <a href="https://publications.waset.org/abstracts/search?q=pyroglutamic%20acid" title=" pyroglutamic acid"> pyroglutamic acid</a>, <a href="https://publications.waset.org/abstracts/search?q=yeast" title=" yeast"> yeast</a>, <a href="https://publications.waset.org/abstracts/search?q=genetics" title=" genetics"> genetics</a> </p> <a href="https://publications.waset.org/abstracts/171881/the-creation-of-a-yeast-model-for-5-oxoproline-accumulation" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/171881.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">86</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">4097</span> Efficient L-Xylulose Production Using Whole-Cell Biocatalyst With NAD+ Regeneration System Through Co-Expression of Xylitol Dehydrogenase and NADH Oxidase in Escherichia Coli</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Mesfin%20Angaw%20Tesfay">Mesfin Angaw Tesfay</a> </p> <p class="card-text"><strong>Abstract:</strong></p> L-Xylulose is a potentially valuable rare sugar used as starting material for antiviral and anticancer drug development in pharmaceutical industries. L-Xylulose exist in a very low concentration in nature and have to be synthesized from cheap starting materials such as xylitol through biotechnological approaches. In this study, cofactor engineering and deep eutectic solvent were applied to improve the efficiency of L-xylulose production from xylitol. A water-forming NAD+ regeneration enzyme (NADH oxidase) from Streptococcus mutans ATCC 25175 was introduced into E. coli with xylitol-4-dehydrogenase (XDH) of Pantoea ananatis resulting in recombinant cells harboring the vector pETDuet-xdh-SmNox. Further, three deep eutectic solvents (DES) including, Choline chloride/glycerol (ChCl/G), Choline chloride/urea (ChCl/U), and Choline chloride/ethylene glycol (ChCl/EG) have been employed to facilitate the conversion efficiency of L-xylulose from xylitol. The co-expression system exhibited optimal activity at a temperature of 37 ℃ and pH 8.5, and the addition of Mg2+ enhanced the catalytic activity by 1.19-fold. Co-expression of NADH oxidase with XDH enzyme resulted in increased L-xylulose concentration and productivity from xylitol as well as the intracellular NAD+ concentration. Two of the DES used (ChCl/U and ChCl/EG) show positive effects on product yield and the ChCl/G has inhibiting effects. The optimum concentration of ChCl/U was 2.5%, which increased the L-xylulose yields compared to the control without DES. In a 1 L fermenter the final concentration and productivity of L-xylulose from 50 g/L of xylitol reached 48.45 g/L, and 2.42 g/L.h respectively, which was the highest report. Overall, this study is a suitable approach for large-scale production of L-xylulose from xylitol using the engineered E. coli cell. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=Xylitol-4-dehydrogenase" title="Xylitol-4-dehydrogenase">Xylitol-4-dehydrogenase</a>, <a href="https://publications.waset.org/abstracts/search?q=NADH%20oxidase" title=" NADH oxidase"> NADH oxidase</a>, <a href="https://publications.waset.org/abstracts/search?q=L-xylulose" title=" L-xylulose"> L-xylulose</a>, <a href="https://publications.waset.org/abstracts/search?q=Xylitol" title=" Xylitol"> Xylitol</a>, <a href="https://publications.waset.org/abstracts/search?q=Coexpression" title=" Coexpression"> Coexpression</a>, <a href="https://publications.waset.org/abstracts/search?q=DESs" title=" DESs"> DESs</a> </p> <a href="https://publications.waset.org/abstracts/192242/efficient-l-xylulose-production-using-whole-cell-biocatalyst-with-nad-regeneration-system-through-co-expression-of-xylitol-dehydrogenase-and-nadh-oxidase-in-escherichia-coli" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/192242.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">23</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">4096</span> Inhibition of α-Glucosidase and Xanthine Oxidase by Curcumin and Its Analogs</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Jung-Feng%20Hsieh">Jung-Feng Hsieh</a>, <a href="https://publications.waset.org/abstracts/search?q=Chu%20Ze%20Chen"> Chu Ze Chen</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Curcumin is the main active compound of turmeric that can inhibit the activities of α-glucosidase and xanthine oxidase (XO). α-Glucosidase and XO inhibitors are widely used to treat patients with diabetes mellitus and gout, respectively; therefore, the objective of this research was to evaluate the inhibitory activities of curcumin and its analogs against α-glucosidase and XO. Our results demonstrated that CM-F had the strongest antioxidant activity with a half-maximal effective concentration (EC50) of 9.39 ± 0.16 μM, which was superior to vitamin E (EC50=17.03 ± 0.09 μM). CM-F also exhibited potent inhibitory activity against XO with an IC50 value of 6.14 ± 0.38 μM and enzyme kinetic results revealed competitive inhibition of XO. We also found that CM-1 and CM-2 inhibited α-glucosidase with IC50 values of 21.06 ± 0.92 μM and 5.95 ± 0.09 μM, respectively, and kinetic studies indicated that both CM-1 and CM-2 are mixed competitive inhibitors of α-glucosidase. Furthermore, docking simulation identified five hydrogen bonds between XO and CM-F; however, only one and two hydrogen bonds are involved in CM-1 and CM-2 binding to α-glucosidase, respectively. Accordingly, curcumin and its analogs have the potential to be used in the treatment of patients with diabetes mellitus and gout. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=curcumin" title="curcumin">curcumin</a>, <a href="https://publications.waset.org/abstracts/search?q=%CE%B1-glucosidase" title=" α-glucosidase"> α-glucosidase</a>, <a href="https://publications.waset.org/abstracts/search?q=inhibitor" title=" inhibitor"> inhibitor</a>, <a href="https://publications.waset.org/abstracts/search?q=xanthine%20oxidase" title=" xanthine oxidase"> xanthine oxidase</a> </p> <a href="https://publications.waset.org/abstracts/80143/inhibition-of-a-glucosidase-and-xanthine-oxidase-by-curcumin-and-its-analogs" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/80143.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">204</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">4095</span> Synthesis and Theoretical Calculations of Carbazole Substituted Pyridopyrimidine Urea/Thioure Derivatives and Studies Their PPO Enzyme Activity</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Arleta%20Rifati%20Nixha">Arleta Rifati Nixha</a>, <a href="https://publications.waset.org/abstracts/search?q=Mustafa%20Arslan"> Mustafa Arslan</a>, <a href="https://publications.waset.org/abstracts/search?q=Adem%20Erg%C3%BCn"> Adem Ergün</a>, <a href="https://publications.waset.org/abstracts/search?q=Nahit%20Gencer"> Nahit Gencer </a> </p> <p class="card-text"><strong>Abstract:</strong></p> Polyphenol oxidase (PPO), sometimes referred to as phenol oxidase, catecholase, phenolase, catechol oxidase, or even tyrosinase, is considered to be an o-dipenol. PPO (EC 1.14.18.1), a multifunctional copper containing enzyme, is widely distributed in nature. It catalyzes two distinct reactions of melanin synthesis: a hydroxylation of monophenols to o-diphenols (monophenolase activity) and an oxidation of o-diphenols to o-quinones (diphenolase activity), both using molecular oxygen. Additionaly, investigation demonstrated that various dermatological disorders, such as age spots and freckle, were caused by the accumulation of an excessive level of epidermal pigmentation. Tyrosinase has also been linked to Parkinson’s and other neurodegenerative diseases. Nitrogen heterocycles have received a great deal of attention in the literature because of biological properties. Especially, among these heterocyclic systems, pyridine containing compounds have been the subject of expanding research efforts in heteroaromatic and biological chemistry. The pyrido [2,3-d] pyrimidine heterocycles, which are those annelated to a pyrimidine ring, are important because of their wide range of biological and pharmaceutical applications (i.e., bronchodilators, vasodilators) and their anti-allergic, cardiotonic, antihypertensive, and hepatoprotective activities. In this study series of 12 new carbazole substituted pyridopyrimidine urea(thiourea) derivatives were synthesized and evaluated effect on PPO. Additionally, we presented structure-activity relationship analyses and theoretical calculations of the compounds. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=carbazole" title="carbazole">carbazole</a>, <a href="https://publications.waset.org/abstracts/search?q=pyridopyrimidine" title=" pyridopyrimidine"> pyridopyrimidine</a>, <a href="https://publications.waset.org/abstracts/search?q=urea" title=" urea"> urea</a>, <a href="https://publications.waset.org/abstracts/search?q=thiourea" title=" thiourea"> thiourea</a>, <a href="https://publications.waset.org/abstracts/search?q=tyrosinase%20inhibitors" title=" tyrosinase inhibitors"> tyrosinase inhibitors</a> </p> <a href="https://publications.waset.org/abstracts/17058/synthesis-and-theoretical-calculations-of-carbazole-substituted-pyridopyrimidine-ureathioure-derivatives-and-studies-their-ppo-enzyme-activity" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/17058.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">439</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">4094</span> Kinetics of Inhibition of Xanthine Oxidase by Lycium Arabicum and Its Protective Effect against Oxonate-Induced Hyperuricemia and Renal Dysfunction in Mice</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Naouel%20Boussoualim">Naouel Boussoualim</a>, <a href="https://publications.waset.org/abstracts/search?q=Hayat%20Trabsa"> Hayat Trabsa</a>, <a href="https://publications.waset.org/abstracts/search?q=Imane%20Krache"> Imane Krache</a>, <a href="https://publications.waset.org/abstracts/search?q=Seddik%20Khennouf"> Seddik Khennouf</a>, <a href="https://publications.waset.org/abstracts/search?q=Noureddine%20Charef"> Noureddine Charef</a>, <a href="https://publications.waset.org/abstracts/search?q=Lekhmici%20Arrar"> Lekhmici Arrar</a>, <a href="https://publications.waset.org/abstracts/search?q=Abderrahmane%20Baghiani"> Abderrahmane Baghiani</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Purpose: To evaluate the in-vitro inhibition of xanthine oxidase (purified from bovine milk) by extracts of Lycium arabicum, as well as it is in vivo hypouricemic and renal protective effects. Methods: Four extracts of Lycium arabicum, methanol (CrE), chloroform (ChE), ethyl acetate (EaE) and aqueous (AqE) extracts, were screened for their total phenolics and potential inhibitory effects on purified bovine milk xanthine oxidase (XO) activity by measuring the formation of uric acid or superoxide radical. The mode of inhibition was investigated and compared with the standard drugs, allopurinol, quercitin, and catechin. To evaluate their hypouricemic effect, the extracts were administered to potassium oxonate-induced hyperuricemic mice at a dose of 50 mg/kg body weight. Results: The results showed that EaE had the highest content of phenolic compounds and was the most potent inhibitor of uric acid formation (IC50 = 0.017 ± 0.001 mg/mL) and formation of superoxide (IC50 = 0.035 ± 0.001 mg/ml). Lineweaver-Burk analysis showed that CrE and EaE inhibited XO competitively, whereas the inhibitory activities exerted by ChE and AqE were of a mixed type. Intraperetoneal injection of L. arabicum extracts (50 mg/kg) elicited hypouricemic actions in hyperuricemic mice. Hyperuricemic mice presented a serum uric acid concentration of 4.71 ± 0.29 mg/L but this was reduced to 1.78 ± 0.11 mg/L by EaE, which was the most potent hyporuricemic extract. Conclusion: L. arabicum fractions have a strong inhibitory effect on xanthine oxidase and and also have a significantly lowering effect on serum and liver creatinine and urea levels in hyperuricemic mice. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=lycium%20arabicum" title="lycium arabicum">lycium arabicum</a>, <a href="https://publications.waset.org/abstracts/search?q=uric%20acid" title=" uric acid"> uric acid</a>, <a href="https://publications.waset.org/abstracts/search?q=creatinine" title=" creatinine"> creatinine</a>, <a href="https://publications.waset.org/abstracts/search?q=superoxide" title=" superoxide"> superoxide</a>, <a href="https://publications.waset.org/abstracts/search?q=phenolic%20compounds" title=" phenolic compounds"> phenolic compounds</a>, <a href="https://publications.waset.org/abstracts/search?q=flavonoids" title=" flavonoids"> flavonoids</a>, <a href="https://publications.waset.org/abstracts/search?q=hyperuricemia" title=" hyperuricemia"> hyperuricemia</a> </p> <a href="https://publications.waset.org/abstracts/41766/kinetics-of-inhibition-of-xanthine-oxidase-by-lycium-arabicum-and-its-protective-effect-against-oxonate-induced-hyperuricemia-and-renal-dysfunction-in-mice" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/41766.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">395</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">4093</span> The Construction of a Probiotic Lactic Acid Bacterium Expressing Acid-Resistant Phytase Enzyme</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=R.%20Majidzadeh%20Heravi">R. Majidzadeh Heravi</a>, <a href="https://publications.waset.org/abstracts/search?q=M.%20Sankian"> M. Sankian</a>, <a href="https://publications.waset.org/abstracts/search?q=H.%20Kermanshahi"> H. Kermanshahi</a>, <a href="https://publications.waset.org/abstracts/search?q=M.%20R.%20Nassiri"> M. R. Nassiri</a>, <a href="https://publications.waset.org/abstracts/search?q=A.%20Heravi%20Moussavi"> A. Heravi Moussavi</a>, <a href="https://publications.waset.org/abstracts/search?q=S.%20A.%20Lari"> S. A. Lari</a>, <a href="https://publications.waset.org/abstracts/search?q=A.%20R.%20Varasteh"> A. R. Varasteh</a> </p> <p class="card-text"><strong>Abstract:</strong></p> The use of probiotics engineered to express specific enzymes has been the subject of considerable attention in poultry industry because of increased nutrient availability and reduced cost of enzyme supplementation. Phytase enzyme is commonly added to poultry feed to improve digestibility and availability of phosphorus from plant sources. To construct a probiotic with potential of phytate degradation, phytase gene (<em>appA</em>) from <em>E. coli</em> was cloned and transformed into two probiotic bacteria <em>Lactobacillus salivarius</em> and <em>Lactococcus lactis</em>. <em>L. salivarous</em> showed plasmid instability, unable to express the gene. The expression of <em>appA</em> gene in <em>L. lactis</em> was analyzed by detecting specific RNA and zymography assay. Phytase enzyme was isolated from cellular extracts of recombinant <em>L. lactis, </em>showing a 46 kDa band upon the SDS-PAGE analysis. Zymogram also confirmed the phytase activity of the 46 kDa band corresponding to the enzyme. An enzyme activity of 4.9U/ml was obtained in cell extracts of <em>L. lactis</em>. The growth of native and recombinant <em>L. lactis</em> was similar in the presence of two concentrations of ox bile. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=Lactobacillus%20salivarus" title="Lactobacillus salivarus">Lactobacillus salivarus</a>, <a href="https://publications.waset.org/abstracts/search?q=Lactococcuslactis" title=" Lactococcuslactis"> Lactococcuslactis</a>, <a href="https://publications.waset.org/abstracts/search?q=recombinant" title=" recombinant"> recombinant</a>, <a href="https://publications.waset.org/abstracts/search?q=phytase" title=" phytase"> phytase</a>, <a href="https://publications.waset.org/abstracts/search?q=poultry" title=" poultry"> poultry</a> </p> <a href="https://publications.waset.org/abstracts/30949/the-construction-of-a-probiotic-lactic-acid-bacterium-expressing-acid-resistant-phytase-enzyme" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/30949.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">490</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">4092</span> Improved Reuse and Storage Performances at Room Temperature of a New Environmental-Friendly Lactate Oxidase Biosensor Made by Ambient Electrospray Deposition</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Antonella%20Cartoni">Antonella Cartoni</a>, <a href="https://publications.waset.org/abstracts/search?q=Mattea%20Carmen%20Castrovilli"> Mattea Carmen Castrovilli</a> </p> <p class="card-text"><strong>Abstract:</strong></p> A biosensor for lactate detection has been developed using an environmentally friendly approach. The biosensor is based on lactate oxidase (LOX) and has remarkable capabilities for reuse and storage at room temperature. The manufacturing technique employed is ambient electrospray deposition (ESD), which enables efficient and sustainable immobilization of the LOX enzyme on a cost-effective com-mercial screen-printed Prussian blue/carbon electrode (PB/C-SPE). The study demonstrates that the ESD technology allows the biosensor to be stored at ambient pressure and temperature for extended periods without affecting the enzymatic activity. The biosensor can be stored for up to 90 days without requiring specific storage conditions, and it can be reused for up to 24 measurements on both freshly prepared electrodes and electrodes that are three months old. The LOX-based biosensor exhibits a lin-ear range of lactate detection between 0.1 and 1 mM, with a limit of detection of 0.07±0.02 mM. Ad-ditionally, it does not exhibit any memory effects. The immobilization process does not involve the use of entrapment matrices or hazardous chemicals, making it environmentally sustainable and non-toxic compared to current methods. Furthermore, the application of a electrospray deposition cycle on previously used biosensors rejuvenates their performance, making them comparable to freshly made biosensors. This highlights the excellent recycling potential of the technique, eliminating the waste as-sociated with disposable devices. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=green%20friendly" title="green friendly">green friendly</a>, <a href="https://publications.waset.org/abstracts/search?q=reuse" title=" reuse"> reuse</a>, <a href="https://publications.waset.org/abstracts/search?q=storage%20performance" title=" storage performance"> storage performance</a>, <a href="https://publications.waset.org/abstracts/search?q=immobilization" title=" immobilization"> immobilization</a>, <a href="https://publications.waset.org/abstracts/search?q=matrix-free" title=" matrix-free"> matrix-free</a>, <a href="https://publications.waset.org/abstracts/search?q=electrospray%20deposition" title=" electrospray deposition"> electrospray deposition</a>, <a href="https://publications.waset.org/abstracts/search?q=biosensor" title=" biosensor"> biosensor</a>, <a href="https://publications.waset.org/abstracts/search?q=lactate%20oxidase" title=" lactate oxidase"> lactate oxidase</a>, <a href="https://publications.waset.org/abstracts/search?q=enzyme" title=" enzyme"> enzyme</a> </p> <a href="https://publications.waset.org/abstracts/175645/improved-reuse-and-storage-performances-at-room-temperature-of-a-new-environmental-friendly-lactate-oxidase-biosensor-made-by-ambient-electrospray-deposition" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/175645.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">65</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">4091</span> Inhibition of the Activity of Polyphenol Oxidase Enzyme Present in Annona muricata and Musa acuminata by the Experimentally Identified Natural Anti-Browning Agents</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Michelle%20Belinda%20S.%20Weerawardana">Michelle Belinda S. Weerawardana</a>, <a href="https://publications.waset.org/abstracts/search?q=Gobika%20Thiripuranathar"> Gobika Thiripuranathar</a>, <a href="https://publications.waset.org/abstracts/search?q=Priyani%20A.%20Paranagama"> Priyani A. Paranagama</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Most of fresh vegetables and fruits available in the retail markets undergo a physiological disorder in its appearance and coloration, which indeed discourages consumer purchase. A loss of millions of dollars yearly to the food industry had been due to this pronounced color reaction called Enzymatic Browning which is driven due to the catalytic activity by an oxidoreductase enzyme, polyphenol oxidase (PPO). The enzyme oxidizes the phenolic compounds which are abundantly available in fruits and vegetables as substrates into quinones, which could react with proteins in its surrounding to generate black pigments, called melanins, which are highly UV-active compounds. Annona muricata (Katu anoda) and Musa acuminata (Ash plantains) is a fruit and a vegetable consumed by Sri Lankans widely due to their high nutritional values, medicinal properties and economical importance. The objective of the present study was to evaluate and determine the effective natural anti-browning inhibitors that could prevent PPO activity in the selected fruit and vegetable. Enzyme extracts from Annona muricata (Katu anoda) and Musa acuminata (Ash plantains), were prepared by homogenizing with analytical grade acetone, and pH of each enzyme extract was maintained at 7.0 using a phosphate buffer. The extracts of inhibitors were prepared using powdered ginger rhizomes and essential oil from the bark of Cinnamomum zeylanicum. Water extracts of ginger were prepared and the essential oil from Ceylon cinnamon bark was extracted using steam distillation method. Since the essential oil is not soluble in water, 0.1µl of cinnamon bark oil was mixed with 0.1µl of Triton X-100 emulsifier and 5.00 ml of water. The effect of each inhibitor on the PPO activity was investigated using catechol (0.1 mol dm-3) as the substrate and two samples of enzyme extracts prepared. The dosages of the prepared Cinnamon bark oil, and ginger (2 samples) which were used to measure the activity were 0.0035 g/ml, 0.091 g/ml and 0.087 g/ml respectively. The measurements of the inhibitory activity were obtained at a wavelength of 525 nm using the UV-visible spectrophotometer. The results evaluated thus revealed that % inhibition observed with cinnamon bark oil, and ginger for Annona muricata was 51.97%, and 60.90% respectively. The effects of cinnamon bark oil, and ginger extract on PPO activity of Musa acuminata were 49.51%, and 48.10%. The experimental findings thus revealed that Cinnamomum zeylanicum bark oil was a more effective inhibitor for PPO enzyme present in Musa acuminata and ginger was effective for PPO enzyme present in Annona muricata. Overall both the inhibitors were proven to be more effective towards the activities of PPO enzyme present in both samples. These inhibitors can thus be corroborated as effective, natural, non-toxic, anti-browning extracts, which when added to the above fruit and vegetable will increase the shelf life and also the acceptance of the product by the consumers. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=anti-browning%20agent" title="anti-browning agent">anti-browning agent</a>, <a href="https://publications.waset.org/abstracts/search?q=enzymatic%20browning" title=" enzymatic browning"> enzymatic browning</a>, <a href="https://publications.waset.org/abstracts/search?q=inhibitory%20activity" title=" inhibitory activity"> inhibitory activity</a>, <a href="https://publications.waset.org/abstracts/search?q=polyphenol%20oxidase" title=" polyphenol oxidase"> polyphenol oxidase</a> </p> <a href="https://publications.waset.org/abstracts/41434/inhibition-of-the-activity-of-polyphenol-oxidase-enzyme-present-in-annona-muricata-and-musa-acuminata-by-the-experimentally-identified-natural-anti-browning-agents" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/41434.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">275</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">4090</span> Structure-Based Virtual Screening and in Silico Toxicity Test of Compounds against Mycobacterium tuberculosis 7,8-Diaminopelargonic Acid Aminotransferase (MtbBioA)</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Junie%20B.%20Billones">Junie B. Billones</a>, <a href="https://publications.waset.org/abstracts/search?q=Maria%20Constancia%20O.%20Carrillo"> Maria Constancia O. Carrillo</a>, <a href="https://publications.waset.org/abstracts/search?q=Voltaire%20G.%20Organo"> Voltaire G. Organo</a>, <a href="https://publications.waset.org/abstracts/search?q=Stephani%20Joy%20Y.%20Macalino"> Stephani Joy Y. Macalino</a>, <a href="https://publications.waset.org/abstracts/search?q=Inno%20A.%20Emnacen"> Inno A. Emnacen</a>, <a href="https://publications.waset.org/abstracts/search?q=Jamie%20Bernadette%20A.%20Sy"> Jamie Bernadette A. Sy</a> </p> <p class="card-text"><strong>Abstract:</strong></p> One of the major interferences in the Philippines’ tuberculosis control program is the widespread prevalence of Mtb strains that are resistant to known drugs, such as the MDR-TB (Multi Drug Resistant Tuberculosis) and XDR-TB (Extensively Drug Resistant Tuberculosis). Therefore, there is a pressing need to search for novel Mtb drug targets in order to be able to combat these drug resistant strains. The enzyme 7,8-diaminopelargonic acid aminotransferase enzyme, or more commonly known as BioA, is one such ideal target, as it is known that humans do not possess this enzyme. BioA primarily plays a key role in Mtb’s lipid biosynthesis pathway; more specifically in the synthesis of the enzyme cofactor biotin. In this study, structure-based pharmacophore screening, docking, and ADMET evaluation of compounds obtained from the DrugBank chemical database were performed against the MtbBioA enzyme. Results of the screening, docking, ADMET, and TOPKAT calculations revealed that out of the 6,516 compounds in the library, only 7 compounds indicated more favorable binding energies as compared to the enzyme’s known inhibitor, amiclenomycin (ACM), as well as good solubility and toxicity properties. Moreover, out of these 7 compounds, Molecule 6 exhibited the best solubility and toxicity properties. In the future, these lead compounds may then be subjected to bioactivity assays in vitro or in vivo for further evaluation of its therapeutic efficacy. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=7" title="7">7</a>, <a href="https://publications.waset.org/abstracts/search?q=8-diaminopelargonic%20acid%20aminotransferase" title="8-diaminopelargonic acid aminotransferase">8-diaminopelargonic acid aminotransferase</a>, <a href="https://publications.waset.org/abstracts/search?q=BioA" title=" BioA"> BioA</a>, <a href="https://publications.waset.org/abstracts/search?q=pharmacophore" title=" pharmacophore"> pharmacophore</a>, <a href="https://publications.waset.org/abstracts/search?q=molecular%20docking" title=" molecular docking"> molecular docking</a>, <a href="https://publications.waset.org/abstracts/search?q=ADMET" title=" ADMET"> ADMET</a>, <a href="https://publications.waset.org/abstracts/search?q=TOPKAT" title=" TOPKAT"> TOPKAT</a> </p> <a href="https://publications.waset.org/abstracts/9299/structure-based-virtual-screening-and-in-silico-toxicity-test-of-compounds-against-mycobacterium-tuberculosis-78-diaminopelargonic-acid-aminotransferase-mtbbioa" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/9299.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">458</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">4089</span> Cheese Production at Low Temperatures Using Probiotic L. casei ATCC 393 and Rennin Enzyme Entrapped in Tubular Cellulose</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Eleftheria%20Barouni">Eleftheria Barouni</a>, <a href="https://publications.waset.org/abstracts/search?q=Antonia%20Terpou"> Antonia Terpou</a>, <a href="https://publications.waset.org/abstracts/search?q=Maria%20Kanellaki"> Maria Kanellaki</a>, <a href="https://publications.waset.org/abstracts/search?q=Argyro%20Bekatorou"> Argyro Bekatorou</a>, <a href="https://publications.waset.org/abstracts/search?q=Athanasios%20A.Koutinas"> Athanasios A.Koutinas</a> </p> <p class="card-text"><strong>Abstract:</strong></p> The aim of the present work was to evaluate the production of cheese using a composite filter of tubular cellulose (TC) with [a] entrapped rennin enzyme and [b] immobilized L.casei and entrapped enzyme. Tubular cellulose from sawdust was prepared after lignin removal with 1% NaOH. The biocatalysts were thermally dried at 38oC and used for milk coagulation. The effect of temperature (5,20,37 oC) of the first dried biocatalyst on the pH kinetics of milk coagulation was examined. The optimum temperature (37oC) of the first biocatalyst was used for milk coagulation with the second biocatalyst prepared by entrapment of both rennin enzyme and probiotic lactic acid bacteria in order to introduce a sour taste in cheeses. This co-biocatalyst was used for milk coagulation. Samples were studied as regards its effect on lactic acid formation and its correlation with taste test results in cheeses. For both biocatalysts samples were analyzed for total acidity and lactic acid formation by HPLC. The quality of the produced cheeses was examined through the determination of volatile compounds by SPME GC/MS analysis. Preliminary taste tests and microbiological analysis were performed and encourage us for further research regarding scale up. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=tubular%20cellulose" title="tubular cellulose">tubular cellulose</a>, <a href="https://publications.waset.org/abstracts/search?q=Lactobacillus%20casei" title=" Lactobacillus casei"> Lactobacillus casei</a>, <a href="https://publications.waset.org/abstracts/search?q=rennin%20enzyme" title=" rennin enzyme"> rennin enzyme</a>, <a href="https://publications.waset.org/abstracts/search?q=cheese%20production" title=" cheese production "> cheese production </a> </p> <a href="https://publications.waset.org/abstracts/20867/cheese-production-at-low-temperatures-using-probiotic-l-casei-atcc-393-and-rennin-enzyme-entrapped-in-tubular-cellulose" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/20867.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">358</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">4088</span> High Catalytic Activity and Stability of Ginger Peroxidase Immobilized on Amino Functionalized Silica Coated Titanium Dioxide Nanocomposite: A Promising Tool for Bioremediation</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Misha%20Ali">Misha Ali</a>, <a href="https://publications.waset.org/abstracts/search?q=Qayyum%20Husain"> Qayyum Husain</a>, <a href="https://publications.waset.org/abstracts/search?q=Nida%20Alam"> Nida Alam</a>, <a href="https://publications.waset.org/abstracts/search?q=Masood%20%20Ahmad"> Masood Ahmad</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Improving the activity and stability of the enzyme is an important aspect in bioremediation processes. Immobilization of enzyme is an efficient approach to amend the properties of biocatalyst required during wastewater treatment. The present study was done to immobilize partially purified ginger peroxidase on amino functionalized silica coated titanium dioxide nanocomposite. Interestingly there was an enhancement in enzyme activity after immobilization on nanosupport which was evident from effectiveness factor (η) value of 1.76. Immobilized enzyme was characterized by transmission electron microscopy, scanning electron microscopy and Fourier transform infrared spectroscopy. Immobilized peroxidase exhibited higher activity in a broad range of pH and temperature as compared to free enzyme. Also, the thermostability of peroxidase was strikingly improved upon immobilization. After six repeated uses, the immobilized peroxidase retained around 62% of its dye decolorization activity. There was a 4 fold increase in Vmax of immobilized peroxidase as compared to free enzyme. Circular dichroism spectroscopy demonstrated conformational changes in the secondary structure of enzyme, a possible reason for the enhanced enzyme activity after immobilization. Immobilized peroxidase was highly efficient in the removal of acid yellow 42 dye in a stirred batch process. Our study shows that this bio-remediating system has remarkable potential for treatment of aromatic pollutants present in wastewater. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=acid%20yellow%2042" title="acid yellow 42">acid yellow 42</a>, <a href="https://publications.waset.org/abstracts/search?q=decolorization" title=" decolorization"> decolorization</a>, <a href="https://publications.waset.org/abstracts/search?q=ginger%20peroxidase" title=" ginger peroxidase"> ginger peroxidase</a>, <a href="https://publications.waset.org/abstracts/search?q=immobilization" title=" immobilization"> immobilization</a> </p> <a href="https://publications.waset.org/abstracts/57680/high-catalytic-activity-and-stability-of-ginger-peroxidase-immobilized-on-amino-functionalized-silica-coated-titanium-dioxide-nanocomposite-a-promising-tool-for-bioremediation" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/57680.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">249</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">4087</span> Caffeic Acid in Cosmetic Formulations: An Innovative Assessment</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Caroline%20M.%20Spagnol">Caroline M. Spagnol</a>, <a href="https://publications.waset.org/abstracts/search?q=Vera%20L.%20B.%20Isaac"> Vera L. B. Isaac</a>, <a href="https://publications.waset.org/abstracts/search?q=Marcos%20A.%20Corr%C3%AAa"> Marcos A. Corrêa</a>, <a href="https://publications.waset.org/abstracts/search?q=H%C3%A9rida%20R.%20N.%20Salgado"> Hérida R. N. Salgado</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Phenolic compounds are abundant in the Brazilian plant kingdom and they are part of a large and complex group of organic substances. Cinnamic acids are part of this group of organic compounds, and caffeic acid (CA) is one of its representatives. Antioxidants are compounds which act as free radical scavengers and, in other cases, such as metal chelators, both in the initiation stage and the propagation of oxidative process. The tyrosinase, polyphenol oxidase, is an enzyme that acts at various stages of melanin biosynthesis within the melanocytes and is considered a key molecule in this process. Some phenolic compounds exhibit inhibitory effects on melanogenesis by inhibiting the tyrosinase enzymatic activity and therefore has been the subject of studies. However, few studies have reported the effectiveness of these products and their safety. Objectives: To assess the inhibitory activity of tyrosinase, the antioxidant activity of CA and its cytotoxic potential. The method to evaluate the inhibitory activity of tyrosinase aims to assess the reduction transformation of L-dopa into dopaquinone reactions catalyzed by the enzyme. For evaluating the antioxidant activity was used the analytical methodology of DPPH radical inhibition. The cytotoxicity evaluation was carried out using the MTT method (3-(4,5-dimethyl-2-thiazolyl)-2,5-diphenyl-2H-tetrazolium bromide), a colorimetric assay which determines the amount of insoluble violet crystals formed by the reduction of MTT in the mitochondria of living cells. Based on the results obtained during the study, CA has low activity as a depigmenting agent. However, it is a more potent antioxidant than ascorbic acid (AA), since a lower amount of CA is sufficient to inhibit 50% of DPPH radical. The results are promising since CA concentration that promoted 50% toxicity in HepG2 cells (IC50=781.8 μg/mL) is approximately 330 to 400 times greater than the concentration required to inhibit 50% of DPPH (IC50 DPPH= 2.39 μg/mL) and ABTS (IC50 ABTS= 1.96 μg/mL) radicals scavenging activity, respectively. The maximum concentration of caffeic acid tested (1140 mg /mL) did not reach 50% of cell death in HaCat cells. Thus, it was concluded that the caffeic acid does not cause toxicity in HepG2 and HaCat cells in the concentrations required to promote antioxidant activity in vitro, and it can be applied in topical products. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=caffeic%20acid" title="caffeic acid">caffeic acid</a>, <a href="https://publications.waset.org/abstracts/search?q=antioxidant" title=" antioxidant"> antioxidant</a>, <a href="https://publications.waset.org/abstracts/search?q=cytotoxicity" title=" cytotoxicity"> cytotoxicity</a>, <a href="https://publications.waset.org/abstracts/search?q=cosmetic" title=" cosmetic"> cosmetic</a> </p> <a href="https://publications.waset.org/abstracts/39118/caffeic-acid-in-cosmetic-formulations-an-innovative-assessment" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/39118.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">379</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">4086</span> Production and Characterisation of Lipase from a Novel Streptomyces.sp - Its Molecular Identification</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=C.%20Asha%20Poorna">C. Asha Poorna</a>, <a href="https://publications.waset.org/abstracts/search?q=N.%20S.%20Pradeep"> N. S. Pradeep </a> </p> <p class="card-text"><strong>Abstract:</strong></p> The biological function of lipase is to catalyze the hydrolysis of triacylglycerols to give free fatty acid, diacylglycerols, mono-acylglycerols and glycerol. They constitute the most important group of biocatalysts for biotechnological applications. The aim of the present study was to identify the lipolytic activity of Streptomyces sp. From soil sample collected from the sacred groves of southern Kerala. The culture conditions of the isolate were optimised and the enzyme was purified and characterised. The purification was attempted with acetone precipitation. The isolate observed to have high lipolytic activity and identified to be of Streptomyces strain. The purification was attempted with acetone precipitation. The purified enzyme observed to have an apparent molecular mass of ~60kDa by sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE). The enzyme showed maximum activity at 60oC and pH-8. The lipase showed tolerance towards different organic solvents like ethanol and methanol that are commonly used in transesterification reactions to displace alcohol from triglycerides contained in renewable resources to yield fatty acid alkyl esters known as biodiesel. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=lipase" title="lipase">lipase</a>, <a href="https://publications.waset.org/abstracts/search?q=Streptomyces" title=" Streptomyces"> Streptomyces</a>, <a href="https://publications.waset.org/abstracts/search?q=biodiesel" title=" biodiesel"> biodiesel</a>, <a href="https://publications.waset.org/abstracts/search?q=fatty%20acid" title=" fatty acid"> fatty acid</a>, <a href="https://publications.waset.org/abstracts/search?q=transesterification" title=" transesterification"> transesterification</a> </p> <a href="https://publications.waset.org/abstracts/40517/production-and-characterisation-of-lipase-from-a-novel-streptomycessp-its-molecular-identification" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/40517.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">327</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">4085</span> Design and Development of Small Peptides as Anti-inflammatory Agents</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Palwinder%20Singh">Palwinder Singh</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Beyond the conventional mode of working with anti-inflammatory agents through enzyme inhibition, herein, an alternate substrate of cyclooxygenase-2 was developed. Proline centered pentapeptide iso-conformational to arachidonic acid exhibited appreciable selectivity for COX-2 overcoming acetic acid and formalin induced pain in rats to almost 80% and was treated as a substrate by the enzyme. Remarkably, COX-2 metabolized the pentapeptide into small fragments consisting mainly of di- and tri-peptides that ensured the safe breakdown of the peptide under in-vivo conditions. The kinetic parameter Kcat/Km for COX-2 mediated metabolism of peptide 6.3 x 105 M-1 s-1 was quite similar to 9.5 x 105 M-1 s-1 for arachidonic acid. Evidenced by the dynamic molecular studies and the use of Y385F COX-2, it was observed that the breakage of the pentapeptide has probably taken place through H-bond activation of the peptide bond by the side chains of Y385 and S530. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=small%20peptides" title="small peptides">small peptides</a>, <a href="https://publications.waset.org/abstracts/search?q=anti-inflammatory%20agents" title=" anti-inflammatory agents"> anti-inflammatory agents</a>, <a href="https://publications.waset.org/abstracts/search?q=cyclooxygenase-2" title=" cyclooxygenase-2"> cyclooxygenase-2</a>, <a href="https://publications.waset.org/abstracts/search?q=unnatural%20substrates" title=" unnatural substrates"> unnatural substrates</a> </p> <a href="https://publications.waset.org/abstracts/163697/design-and-development-of-small-peptides-as-anti-inflammatory-agents" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/163697.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">70</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">4084</span> Development of Sulfite Biosensor Based on Sulfite Oxidase Immobilized on 3-Aminoproplytriethoxysilane Modified Indium Tin Oxide Electrode</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Pawasuth%20Saengdee">Pawasuth Saengdee</a>, <a href="https://publications.waset.org/abstracts/search?q=Chamras%20Promptmas"> Chamras Promptmas</a>, <a href="https://publications.waset.org/abstracts/search?q=Ting%20Zeng"> Ting Zeng</a>, <a href="https://publications.waset.org/abstracts/search?q=Silke%20Leimk%C3%BChler"> Silke Leimkühler</a>, <a href="https://publications.waset.org/abstracts/search?q=Ulla%20Wollenberger"> Ulla Wollenberger</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Sulfite has been used as a versatile preservative to limit the microbial growth and to control the taste in some food and beverage. However, it has been reported to cause a wide spectrum of severe adverse reactions. Therefore, it is important to determine the amount of sulfite in food and beverage to ensure consumer safety. An efficient electrocatalytic biosensor for sulfite detection was developed by immobilizing of human sulfite oxidase (hSO) on 3-aminoproplytriethoxysilane (APTES) modified indium tin oxide (ITO) electrode. Cyclic voltammetry was employed to investigate the electrochemical characteristics of the hSO modified ITO electrode for various pretreatment and binding conditions. Amperometry was also utilized to demonstrate the current responses of the sulfite sensor toward sodium sulfite in an aqueous solution at a potential of 0 V (vs. Ag/AgCl 1 M KCl). The proposed sulfite sensor has a linear range between 0.5 to 2 mM with a correlation coefficient 0.972. Then, the additional polymer layer of PVA was introduced to extend the linear range of sulfite sensor and protect the enzyme. The linear range of sulfite sensor with 5% coverage increases from 2.8 to 20 mM at a correlation coefficient of 0.983. In addition, the stability of sulfite sensor with 5% PVA coverage increases until 14 days when kept in 0.5 mM Tris-buffer, pH 7.0 at 4 8C. Therefore, this sensor could be applied for the detection of sulfite in the real sample, especially in food and beverage. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=sulfite%20oxidase" title="sulfite oxidase">sulfite oxidase</a>, <a href="https://publications.waset.org/abstracts/search?q=bioelectrocatalytsis" title=" bioelectrocatalytsis"> bioelectrocatalytsis</a>, <a href="https://publications.waset.org/abstracts/search?q=indium%20tin%20oxide" title=" indium tin oxide"> indium tin oxide</a>, <a href="https://publications.waset.org/abstracts/search?q=direct%20electrochemistry" title=" direct electrochemistry"> direct electrochemistry</a>, <a href="https://publications.waset.org/abstracts/search?q=sulfite%20sensor" title=" sulfite sensor"> sulfite sensor</a> </p> <a href="https://publications.waset.org/abstracts/67534/development-of-sulfite-biosensor-based-on-sulfite-oxidase-immobilized-on-3-aminoproplytriethoxysilane-modified-indium-tin-oxide-electrode" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/67534.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">231</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">4083</span> Malate Dehydrogenase Enabled ZnO Nanowires as an Optical Tool for Malic Acid Detection in Horticultural Products </h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Rana%20Tabassum">Rana Tabassum</a>, <a href="https://publications.waset.org/abstracts/search?q=Ravi%20Kant"> Ravi Kant</a>, <a href="https://publications.waset.org/abstracts/search?q=Banshi%20D.%20Gupta"> Banshi D. Gupta</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Malic acid is an extensively distributed organic acid in numerous horticultural products in minute amounts which significantly contributes towards taste determination by balancing sugar and acid fractions. An enhanced concentration of malic acid is utilized as an indicator of fruit maturity. In addition, malic acid is also a crucial constituent of several cosmetics and pharmaceutical products. An efficient detection and quantification protocol for malic acid is thus highly demanded. In this study, we report a novel detection scheme for malic acid by synergistically collaborating fiber optic surface plasmon resonance (FOSPR) and distinctive features of nanomaterials favorable for sensing applications. The design blueprint involves the deposition of an assembly of malate dehydrogenase enzyme entrapped in ZnO nanowires forming the sensing route over silver coated central unclad core region of an optical fiber. The formation and subsequent decomposition of the enzyme-analyte complex on exposure of the sensing layer to malic acid solutions of diverse concentration results in modification of the dielectric function of the sensing layer which is manifested in terms of shift in resonance wavelength. Optimization of experimental variables such as enzyme concentration entrapped in ZnO nanowires, dip time of probe for deposition of sensing layer and working pH range of the sensing probe have been accomplished through SPR measurements. The optimized sensing probe displays high sensitivity, broad working range and a minimum limit of detection value and has been successfully tested for malic acid determination in real samples of fruit juices. The current work presents a novel perspective towards malic acid determination as the unique and cooperative combination of FOSPR and nanomaterials provides myriad advantages such as enhanced sensitivity, specificity, compactness together with the possibility of online monitoring and remote sensing. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=surface%20plasmon%20resonance" title="surface plasmon resonance">surface plasmon resonance</a>, <a href="https://publications.waset.org/abstracts/search?q=optical%20fiber" title=" optical fiber"> optical fiber</a>, <a href="https://publications.waset.org/abstracts/search?q=sensor" title=" sensor"> sensor</a>, <a href="https://publications.waset.org/abstracts/search?q=malic%20acid" title=" malic acid"> malic acid</a> </p> <a href="https://publications.waset.org/abstracts/73444/malate-dehydrogenase-enabled-zno-nanowires-as-an-optical-tool-for-malic-acid-detection-in-horticultural-products" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/73444.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">380</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">4082</span> Tryptophan and Its Derivative Oxidation via Heme-Dioxygenase Enzyme</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Ali%20Bahri%20Lubis">Ali Bahri Lubis</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Tryptophan oxidation by Heme-dioxygenase enzyme is the initial rate-limiting step in the kynurenine pathway, which leads to the formation of NADH and dangerous metabolites, implicating several severe diseases such as Parkinson’s Disease, Huntington's Disease, poliomyelitis and cataract. This oxidation, generally, allows tryptophan to convert to N-Formylkynurenine (NFK). Observing the catalytic mechanism of Heme dioxygenase in tryptophan oxidation has been a debatably scientific interest since no one has yet proven the mechanism obviously. In this research we have attempted to prove mechanistic steps of tryptophan oxidation via human indoleamine dioxygenase (h-IDO) utilising various substrates: L-tryptophan, L-tryptophan (indole-ring-2-¹³C), L-fully-labelled¹³C-tryptophan, L-N-methyl-tryptophan, L-tryptophanol and 2-amino-3-(benzo(b)thiophene-3-yl) propanoic acid. All enzyme assay experiments were measured using a UV-Vis spectrophotometer, LC-MS, 1H-NMR and HSQC. We also successfully synthesised enzyme products as our control in NMR measurements. The result exhibited that all substrates produced N-formyl kynurenine (NFK), and a side, the minor product of hydroxypyrrolloindoleamine carboxylic acid (HPIC) in cis and trans isomer, except 1-methyl tryptophan only generating cis HPIC. Interestingly, L- tryptophanol was oxidised to form HPIC derivative as a major product and 5-hydroxy tryptophan was converted to NFK derivative instead without any HPIC derivative. The bizarre result of oxidation underwent in 2-amino-3-(benzo(b)thiophene-3-yl) propanoic acid, which produced epoxide cyclic. Those phenomena have been explainable in our research based on the proposed mechanism of how tryptophan is oxidised by human indoleamine dioxygenase. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=tryptophan%20oxidation" title="tryptophan oxidation">tryptophan oxidation</a>, <a href="https://publications.waset.org/abstracts/search?q=heme-dioxygenases" title=" heme-dioxygenases"> heme-dioxygenases</a>, <a href="https://publications.waset.org/abstracts/search?q=human%20indoleamine%20dioxygenases" title=" human indoleamine dioxygenases"> human indoleamine dioxygenases</a>, <a href="https://publications.waset.org/abstracts/search?q=N-formylkynurenine" title=" N-formylkynurenine"> N-formylkynurenine</a>, <a href="https://publications.waset.org/abstracts/search?q=hydroxypyrroloindoleamine%20carboxylic%20acid" title=" hydroxypyrroloindoleamine carboxylic acid"> hydroxypyrroloindoleamine carboxylic acid</a> </p> <a 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