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Search results for: anticancer enzyme

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text-center" style="font-size:1.6rem;">Search results for: anticancer enzyme</h1> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">1181</span> Isolation, Characterization, and Optimization of Immobilized L-Asparginase- Anticancer Enzyme from Aspergillus.Niger</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Supriya%20Chatla">Supriya Chatla</a>, <a href="https://publications.waset.org/abstracts/search?q=Anjana%20Male"> Anjana Male</a>, <a href="https://publications.waset.org/abstracts/search?q=Srikala%20Kamireddy"> Srikala Kamireddy</a> </p> <p class="card-text"><strong>Abstract:</strong></p> L-asparaginase (E.C.3.5.1.1) is an anti-cancer enzyme that has been purified and characterized for decades to study and evaluate its anti-carcinogenic activity against Hodgkin’s lymphoma. The present investigation deals with screening, isolation and optimization of L-asparaginase giving fungal strain of soil samples from different areas of AP, India. L-Aspariginase activity was estimated on the basis of the pink color surrounding the growing colony. A total of 132 colonies were screened and isolated from different samples. Based on the zone diameter, L-asparaginase activity is determined, L- asparaginase activity is optimized at 28oc and Immobilized Aspariginase had more potency than the free enzymes. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=aspariginase" title="aspariginase">aspariginase</a>, <a href="https://publications.waset.org/abstracts/search?q=anticancer%20enzyme" title=" anticancer enzyme"> anticancer enzyme</a>, <a href="https://publications.waset.org/abstracts/search?q=Isolation" title=" Isolation"> Isolation</a>, <a href="https://publications.waset.org/abstracts/search?q=optimization" title=" optimization"> optimization</a> </p> <a href="https://publications.waset.org/abstracts/161845/isolation-characterization-and-optimization-of-immobilized-l-asparginase-anticancer-enzyme-from-aspergillusniger" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/161845.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">80</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">1180</span> Binding Studies of Complexes of Anticancer Drugs with DNA and Enzymes Involved in DNA Replication Using Molecular Docking and Cell Culture Techniques</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Fouzia%20Perveen">Fouzia Perveen</a>, <a href="https://publications.waset.org/abstracts/search?q=Rumana%20Qureshi"> Rumana Qureshi</a> </p> <p class="card-text"><strong>Abstract:</strong></p> The presently studied twelve anticancer drugs are the cytotoxic agents which inhibit the replication of DNA and activity of enzymes involved in DNA replication namely topoisomerase-II, polymerase and helicase and have shown remarkable anticancer activity in clinical trials. In this study, we performed molecular docking studies of twelve antitumor drugs against DNA and DNA enzymes in the presence and absence of ascorbic acid (AA) and developed the quantitative structure-activity relationship (QSAR) model for anticancer activity screening. A number of electronic and steric descriptors were calculated using MOE software package. QSAR was established showing a correlation of binding strength with various physicochemical descriptors. Out of these twelve, eight cytotoxic drugs were tested on Non-Small Cell Lung Cancer cell lines (H-157 and H-1299) in the absence and presence of ascorbic acid and experimental IC50 values were calculated. From the docking studies, binding constants were calculated indicating the strength of drug-DNA and drug-enzyme complex formation and it was correlated to the IC50 values (both experimental and theoretical). These results can offer useful references for directing the molecular design of DNA enzyme inhibitor with improved anticancer activity. <p class="card-text"><strong>Keywords:</strong> <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=binding%20constant" title=" binding constant"> binding constant</a>, <a href="https://publications.waset.org/abstracts/search?q=cytotoxic%20agents" title=" cytotoxic agents"> cytotoxic agents</a>, <a href="https://publications.waset.org/abstracts/search?q=cell%20culture" title=" cell culture"> cell culture</a>, <a href="https://publications.waset.org/abstracts/search?q=DNA" title=" DNA"> DNA</a>, <a href="https://publications.waset.org/abstracts/search?q=DNA%20enzymes" title=" DNA enzymes"> DNA enzymes</a>, <a href="https://publications.waset.org/abstracts/search?q=molecular%20docking" title=" molecular docking"> molecular docking</a> </p> <a href="https://publications.waset.org/abstracts/23535/binding-studies-of-complexes-of-anticancer-drugs-with-dna-and-enzymes-involved-in-dna-replication-using-molecular-docking-and-cell-culture-techniques" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/23535.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">427</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">1179</span> Synthesis and Molecular Docking Studies of Hydrazone Derivatives Potent Inhibitors as a Human Carbonic Anhydrase IX</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Sema%20%C5%9Eeno%C4%9Flu">Sema Şenoğlu</a>, <a href="https://publications.waset.org/abstracts/search?q=Sevgi%20Karaku%C5%9F"> Sevgi Karakuş</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Hydrazone scaffold is important to design new drug groups and is found to possess numerous uses in pharmaceutical chemistry. Besides, hydrazone derivatives are also known for biological activities such as anticancer, antimicrobial, antiviral, and antifungal. Hydrazone derivatives are promising anticancer agents because they inhibit cancer proliferation and induce apoptosis. Human carbonic anhydrase IX has a high potential to be an antiproliferative drug target, and targeting this protein is also important for obtaining potential anticancer inhibitors. The protein construct was retrieved as a PDB file from the RCSB protein database. This binding interaction of proteins and ligands was performed using Discovery Studio Visualizer. In vitro inhibitory activity of hydrazone derivatives was tested against enzyme carbonic anhydrase IX on the PyRx programme. Most of these molecules showed remarkable human carbonic anhydrase IX inhibitory activity compared to the acetazolamide. As a result, these compounds appear to be a potential target in drug design against human carbonic anhydrase IX. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=cancer" title="cancer">cancer</a>, <a href="https://publications.waset.org/abstracts/search?q=carbonic%20anhydrase%20IX%20enzyme" title=" carbonic anhydrase IX enzyme"> carbonic anhydrase IX enzyme</a>, <a href="https://publications.waset.org/abstracts/search?q=docking" title=" docking"> docking</a>, <a href="https://publications.waset.org/abstracts/search?q=hydrazone" title=" hydrazone"> hydrazone</a> </p> <a href="https://publications.waset.org/abstracts/171356/synthesis-and-molecular-docking-studies-of-hydrazone-derivatives-potent-inhibitors-as-a-human-carbonic-anhydrase-ix" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/171356.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">82</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">1178</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">1177</span> The Marker Active Compound Identification of Calotropis gigantea Roots Extract as an Anticancer</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Roihatul%20Mutiah">Roihatul Mutiah</a>, <a href="https://publications.waset.org/abstracts/search?q=Sukardiman"> Sukardiman</a>, <a href="https://publications.waset.org/abstracts/search?q=Aty%20Widyawaruyanti"> Aty Widyawaruyanti</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Calotropis gigantiea (L.) R. Br (Apocynaceae) commonly called as “Biduri” or “giant milk weed” is a well-known weed to many cultures for treating various disorders. Several studies reported that C.gigantea roots has anticancer activity. The main aim of this research was to isolate and identify an active marker compound of C.gigantea roots for quality control purpose of its extract in the development as anticancer natural product. The isolation methods was bioactivity guided column chromatography, TLC, and HPLC. Evaluated anticancer activity of there substances using MTT assay methods. Identification structure active compound by UV, 1HNMR, 13CNMR, HMBC, HMQC spectral and other references. The result showed that the marker active compound was identical as Calotropin. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=calotropin" title="calotropin">calotropin</a>, <a href="https://publications.waset.org/abstracts/search?q=Calotropis%20gigantea" title=" Calotropis gigantea"> Calotropis gigantea</a>, <a href="https://publications.waset.org/abstracts/search?q=anticancer" title=" anticancer"> anticancer</a>, <a href="https://publications.waset.org/abstracts/search?q=marker%20active" title=" marker active"> marker active</a> </p> <a href="https://publications.waset.org/abstracts/59024/the-marker-active-compound-identification-of-calotropis-gigantea-roots-extract-as-an-anticancer" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/59024.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">335</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">1176</span> Prediction of Anticancer Potential of Curcumin Nanoparticles by Means of Quasi-Qsar Analysis Using Monte Carlo Method</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Ruchika%20Goyal">Ruchika Goyal</a>, <a href="https://publications.waset.org/abstracts/search?q=Ashwani%20Kumar"> Ashwani Kumar</a>, <a href="https://publications.waset.org/abstracts/search?q=Sandeep%20Jain"> Sandeep Jain</a> </p> <p class="card-text"><strong>Abstract:</strong></p> The experimental data for anticancer potential of curcumin nanoparticles was calculated by means of eclectic data. The optimal descriptors were examined using Monte Carlo method based CORAL SEA software. The statistical quality of the model is following: n = 14, R² = 0.6809, Q² = 0.5943, s = 0.175, MAE = 0.114, F = 26 (sub-training set), n =5, R²= 0.9529, Q² = 0.7982, s = 0.086, MAE = 0.068, F = 61, Av Rm² = 0.7601, ∆R²m = 0.0840, k = 0.9856 and kk = 1.0146 (test set) and n = 5, R² = 0.6075 (validation set). This data can be used to build predictive QSAR models for anticancer activity. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=anticancer%20potential" title="anticancer potential">anticancer potential</a>, <a href="https://publications.waset.org/abstracts/search?q=curcumin" title=" curcumin"> curcumin</a>, <a href="https://publications.waset.org/abstracts/search?q=model" title=" model"> model</a>, <a href="https://publications.waset.org/abstracts/search?q=nanoparticles" title=" nanoparticles"> nanoparticles</a>, <a href="https://publications.waset.org/abstracts/search?q=optimal%20descriptors" title=" optimal descriptors"> optimal descriptors</a>, <a href="https://publications.waset.org/abstracts/search?q=QSAR" title=" QSAR"> QSAR</a> </p> <a href="https://publications.waset.org/abstracts/54615/prediction-of-anticancer-potential-of-curcumin-nanoparticles-by-means-of-quasi-qsar-analysis-using-monte-carlo-method" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/54615.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">318</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">1175</span> Design, Synthesis and Pharmacological Investigation of Novel 2-Phenazinamine Derivatives as a Mutant BCR-ABL (T315I) Inhibitor</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Gajanan%20M.%20Sonwane">Gajanan M. Sonwane</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Nowadays, the entire pharmaceutical industry is facing the challenge of increasing efficiency and innovation. The major hurdles are the growing cost of research and development and a concurrent stagnating number of new chemical entities (NCEs). Hence, the challenge is to select the most druggable targets and to search the equivalent drug-like compounds, which also possess specific pharmacokinetic and toxicological properties that allow them to be developed as drugs. The present research work includes the studies of developing new anticancer heterocycles by using molecular modeling techniques. The heterocycles synthesized through such methodology are much effective as various physicochemical parameters have been already studied and the structure has been optimized for its best fit in the receptor. Hence, on the basis of the literature survey and considering the need to develop newer anticancer agents, new phenazinamine derivatives were designed by subjecting the nucleus to molecular modeling, viz., GQSAR analysis and docking studies. Simultaneously, these designed derivatives were subjected to in silico prediction of biological activity through PASS studies and then in silico toxicity risk assessment studies. In PASS studies, it was found that all the derivatives exhibited a good spectrum of biological activities confirming its anticancer potential. The toxicity risk assessment studies revealed that all the derivatives obey Lipinski’s rule. Amongst these series, compounds 4c, 5b and 6c were found to possess logP and drug-likeness values comparable with the standard Imatinib (used for anticancer activity studies) and also with the standard drug methotrexate (used for antimitotic activity studies). One of the most notable mutations is the threonine to isoleucine mutation at codon 315 (T315I), which is known to be resistant to all currently available TKI. Enzyme assay planned for confirmation of target selective activity. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=drug%20design" title="drug design">drug design</a>, <a href="https://publications.waset.org/abstracts/search?q=tyrosine%20kinases" title=" tyrosine kinases"> tyrosine kinases</a>, <a href="https://publications.waset.org/abstracts/search?q=anticancer" title=" anticancer"> anticancer</a>, <a href="https://publications.waset.org/abstracts/search?q=Phenazinamine" title=" Phenazinamine"> Phenazinamine</a> </p> <a href="https://publications.waset.org/abstracts/148609/design-synthesis-and-pharmacological-investigation-of-novel-2-phenazinamine-derivatives-as-a-mutant-bcr-abl-t315i-inhibitor" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/148609.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">116</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">1174</span> Isolation, Characterization and Quantitation of Anticancer Constituent from Chloroform Extract of N. arbortristis L. Leaves</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Parul%20Grover">Parul Grover</a>, <a href="https://publications.waset.org/abstracts/search?q=K.%20A.%20Suri"> K. A. Suri</a>, <a href="https://publications.waset.org/abstracts/search?q=Raj%20Kumar"> Raj Kumar</a>, <a href="https://publications.waset.org/abstracts/search?q=Gulshan%20Bansal"> Gulshan Bansal</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Background: Nyctanthes arbortristis Linn is traditionally used as anticancer herb in Indian system of medicine, but its introduction into modern system of medicine is still awaited due to lack of systematic scientific studies. Objective: The objective of the present study was to isolate and characterize anticancer phytoconstituents from N. arbortristis L. leaves based on bioactivity guided fractionation. Method: Different extracts of the leaves of the plant were prepared by Soxhlet extractor. Each extract was evaluated for anticancer activity against HL-60 cell lines. Chloroform and HA extract showed potent anticancer activity and hence were selected for fractionation. Fraction C1 from chloroform extract was found to be most potent amongst all when tested against three cell lines (HL-60, A-549, and HCT-116) and thus was selected for further fractionation and a pure compound CP-01 was isolated. RP-HPLC method has been developed for quantification of isolated compound by using Kinetex C-18 column with gradient elution at 0.7 mL/min using mobile phase containing potassium dihydrogen phosphate (0.01 M, pH 3.0) with acetonitrile. The wavelength of maximum absorption (λₘₐₓ) selected was 210 nm. Results: The structure of potent anticancer CP-01 was determined on the basis spectroscopic methods like IR, 1H-NMR, ¹³C-NMR and Mass Spectrometry and it was characterized as 1,1,2-tris(2’,4’-di-tert-butylbenzene)-4,4-dimethyl-pent-1-ene. The content of CP-01 was found to be 0.88 %w/w of chloroform extract and 0.08 %w/w of N.arbortristis leaves. Conclusion: The study supports the traditional use of N. arbortristis as anticancer herb & the identified compound CP-01 can serve as an excellent lead to develop potent and safe anticancer drugs. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=anticancer" title="anticancer">anticancer</a>, <a href="https://publications.waset.org/abstracts/search?q=HL-60%20cell%20lines" title=" HL-60 cell lines"> HL-60 cell lines</a>, <a href="https://publications.waset.org/abstracts/search?q=Nyctanthes%20arbor-tristis" title=" Nyctanthes arbor-tristis"> Nyctanthes arbor-tristis</a>, <a href="https://publications.waset.org/abstracts/search?q=RP-HPLC" title=" RP-HPLC"> RP-HPLC</a> </p> <a href="https://publications.waset.org/abstracts/104616/isolation-characterization-and-quantitation-of-anticancer-constituent-from-chloroform-extract-of-n-arbortristis-l-leaves" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/104616.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">147</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">1173</span> The Enzyme Inhibitory Potentials of Different Extracts from Linaria genistifolia subsp. genistifolia</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Gokhan%20Zengin">Gokhan Zengin</a>, <a href="https://publications.waset.org/abstracts/search?q=Abdurrahman%20Aktumsek"> Abdurrahman Aktumsek</a> </p> <p class="card-text"><strong>Abstract:</strong></p> The key enzyme inhibitory theory is one of the most accepted strategies in the treatment of global health problems including Alzheimer’s Disease and Diabetes mellitus. For this reason, the enzyme inhibitory potentials of different solvent extracts from Linaria genistifolia subsp. genistifolia were investigated against cholinesterase, and tyrosinase. The in vitro enzyme inhibitory potentials were measured with a microplate reader. The acetone and methanol extracts exhibited the strongest enzyme inhibitory effects on cholinesterase. However, the water extract was only active on tyrosinase. The results suggested that Linaria genistifolia subsp. genistifolia could be considered as a source of natural enzyme inhibitors for the treatment of major health problems. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=enzyme%20inhibitors" title="enzyme inhibitors">enzyme inhibitors</a>, <a href="https://publications.waset.org/abstracts/search?q=cholinesterase" title=" cholinesterase"> cholinesterase</a>, <a href="https://publications.waset.org/abstracts/search?q=tyrosinase" title=" tyrosinase"> tyrosinase</a>, <a href="https://publications.waset.org/abstracts/search?q=linaria" title=" linaria"> linaria</a>, <a href="https://publications.waset.org/abstracts/search?q=Turkey" title=" Turkey"> Turkey</a> </p> <a href="https://publications.waset.org/abstracts/46806/the-enzyme-inhibitory-potentials-of-different-extracts-from-linaria-genistifolia-subsp-genistifolia" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/46806.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">310</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">1172</span> Cytotoxic Effect of Purified and Crude Hyaluronidase Enzyme on Hep G2 Cell Line</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Furqan%20M.%20Kadhum">Furqan M. Kadhum</a>, <a href="https://publications.waset.org/abstracts/search?q=Asmaa%20A.%20Hussein"> Asmaa A. Hussein</a>, <a href="https://publications.waset.org/abstracts/search?q=Maysaa%20Ch.%20Hatem"> Maysaa Ch. Hatem</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Hyaluronidase enzyme was purified from the clinical isolate Staphyloccus aureus in three purification steps, first by precipitation with 90% saturated ammonium sulfate, ion exchange chromatography on DEAE-Cellulose, and gel filtration chromatography throughout Sephacryl S-300. Specific activity of the purified enzyme was reached 930 U/mg protein with 7.4 folds of purification and 46.5% recovery. The enzyme has an average molecular weight of about 69 kDa, with an optimum pH of enzyme activity and stability at pH 7, also the optimum temperature for activity was 37oC. The enzyme was stable with full activity at a temperature ranged between 30-40 oC. Metal ions showed variable inhibitory degree with the strongest effect for Fe+3, however, the chelating and reducing agents had no or little effects. Cytotoxic studies for purified and crude hyaluronidase against cancer cell Hep G2 type at different enzyme concentrations and exposure times showed that the inhibition effect of both crude and purified enzyme increased by increasing the enzyme concentration with no change was observed at 24hr, while at 48 and 72 hrs the same inhibition rate were observed for purified enzyme and differ for the crude filtrate. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=hyaluronidase" title="hyaluronidase">hyaluronidase</a>, <a href="https://publications.waset.org/abstracts/search?q=S.%20aureus" title=" S. aureus"> S. aureus</a>, <a href="https://publications.waset.org/abstracts/search?q=metal%20ions" title=" metal ions"> metal ions</a>, <a href="https://publications.waset.org/abstracts/search?q=cytotoxicity" title=" cytotoxicity"> cytotoxicity</a> </p> <a href="https://publications.waset.org/abstracts/16485/cytotoxic-effect-of-purified-and-crude-hyaluronidase-enzyme-on-hep-g2-cell-line" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/16485.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">447</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">1171</span> Anti-cancer Activity of Cassava Leaves (Manihot esculenta Crantz.) Against Colon Cancer (WiDr) Cells in vitro</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Fatma%20Zuhrotun%20Nisa">Fatma Zuhrotun Nisa</a>, <a href="https://publications.waset.org/abstracts/search?q=Aprilina%20Ratriany"> Aprilina Ratriany</a>, <a href="https://publications.waset.org/abstracts/search?q=Agus%20Wijanarka"> Agus Wijanarka</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Background: Cassava leaves are widely used by the people of Indonesia as a vegetable and treat various diseases, including anticancer believed as food. However, not much research on the anticancer activity of cassava leaves, especially in colon cancer. Objectives: the aim of this study is to investigate anti-cancer activity of cassava leaves (Manihot esculanta C.) against colon cancer (WiDr) cells in vitro. Methods: effect of crude aqueous extract of leaves of cassava and cassava leaves boiled tested in colon cancer cells widr. Determination of Anticancer uses the MTT method with parameters such as the percentage of deaths. Results: raw cassava leaf water extract gave IC50 of 63.1 mg / ml. While the water extract of boiled cassava leaves gave IC50 of 79.4 mg/ml. However, there is no difference anticancer activity of raw cassava leaves or cancer (p> 0.05). Conclusion: Cassava leaves contain a variety of compounds that have previously been reported to have anticancer activity. Linamarin, β-carotene, vitamin C, and fiber were thought to affect the IC50 cassava leaf extract against colon cancer cells WiDr. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=boiled%20cassava%20leaves" title="boiled cassava leaves">boiled cassava leaves</a>, <a href="https://publications.waset.org/abstracts/search?q=cassava%20leaves%20raw" title=" cassava leaves raw"> cassava leaves raw</a>, <a href="https://publications.waset.org/abstracts/search?q=anticancer%20activity" title=" anticancer activity"> anticancer activity</a>, <a href="https://publications.waset.org/abstracts/search?q=colon%20cancer" title=" colon cancer"> colon cancer</a>, <a href="https://publications.waset.org/abstracts/search?q=IC50" title=" IC50 "> IC50 </a> </p> <a href="https://publications.waset.org/abstracts/19756/anti-cancer-activity-of-cassava-leaves-manihot-esculenta-crantz-against-colon-cancer-widr-cells-in-vitro" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/19756.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">551</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">1170</span> Isolation and Identification of Cytotoxic Compounds from Fruticose Lichen Roccella montagnei, and It’s in Silico Docking Study against CDK-10</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Tripti%20Mishra">Tripti Mishra</a>, <a href="https://publications.waset.org/abstracts/search?q=Shipra%20Shukla"> Shipra Shukla</a>, <a href="https://publications.waset.org/abstracts/search?q=Sanjeev%20Meena"> Sanjeev Meena</a>, <a href="https://publications.waset.org/abstracts/search?q="></a>, <a href="https://publications.waset.org/abstracts/search?q=Ruchi%20Singh"> Ruchi Singh</a>, <a href="https://publications.waset.org/abstracts/search?q=Mahesh%20Pal"> Mahesh Pal</a>, <a href="https://publications.waset.org/abstracts/search?q=D.%20K.%20Upreti"> D. K. Upreti</a>, <a href="https://publications.waset.org/abstracts/search?q=Dipak%20Datta"> Dipak Datta</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Roccella montagnei belongs to lichen family Roccelleceae growing luxuriantly along the coastal regions of India. As Roccella has been shown to be bioactive, we prepared methanolic extract and assessed its anticancer potential. The methanolic extract showed significant in vitro cytotoxic activity against four human cancer cell lines such as Colon (DLD-1, SW-620), Breast (MCF-7), Head and Neck (FaDu). This prompted us to isolate bioactive compounds through column chromatography. Two compounds Roccellic acid and Everninic acid have been isolated, out of which Everninic acid is reported for the first time. Both the compounds have been tested for in vitro cytotoxic activity in which Roccellic acid showed strong anticancer activity as compared to the Everninic acid. CDK-10 (Cyclin-dependent kinase) contributes to proliferation of cancer cells, and aberrant activity of these kinases has been reported in a wide variety of human cancers. These kinases, therefore, constitute biomarkers of proliferation and attractive pharmacological targets for the development of anticancer therapeutics. Therefore both the isolated compounds were tested for in silico molecular docking study against CDK-10 isomer enzyme to support the cytotoxic activity. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=cytotoxic%20activity" title="cytotoxic activity">cytotoxic activity</a>, <a href="https://publications.waset.org/abstracts/search?q=everninic%20acid" title=" everninic acid"> everninic acid</a>, <a href="https://publications.waset.org/abstracts/search?q=roccellic%20acid" title=" roccellic acid"> roccellic acid</a>, <a href="https://publications.waset.org/abstracts/search?q=R.%20montagnei" title=" R. montagnei"> R. montagnei</a> </p> <a href="https://publications.waset.org/abstracts/56792/isolation-and-identification-of-cytotoxic-compounds-from-fruticose-lichen-roccella-montagnei-and-its-in-silico-docking-study-against-cdk-10" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/56792.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">326</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">1169</span> Production of Linamarase from Lactobacillus delbrueckii NRRL B-763</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Ogbonnaya%20Nwokoro">Ogbonnaya Nwokoro</a>, <a href="https://publications.waset.org/abstracts/search?q=Florence%20O.%20Anya"> Florence O. Anya</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Nutritional factors relating to the production of linamarase from Lactobacillus delbrueckii NRRL B–763 were investigated. The microorganism was cultivated in a medium containing 1% linamarin. Enzyme was produced using a variety of carbon substrates but the highest enzyme activity was detected in the presence of salicin (522 U/ml) after 48 h while the lowest yield was observed with CM cellulose (38 U/ml) after 72 h. Enzyme was not produced in the presence of cellobiose. Among a variety of nitrogen substrates tested, peptone supported maximum enzyme production (412 U/ml) after 48 h. Lowest enzyme production was observed with urea (40 U/ml). Organic nitrogen substrates generally supported higher enzyme productivity than inorganic nitrogen substrates. Enzyme activity was observed in the presence of Mn2+ (% relative activity = 216) while Hg2+ was inhibitory (% relative activity = 28). Locally-formulated media were comparable to MRS broth in supporting linamarase production by the bacterium. Higher enzyme activity was produced in media with surfactant than in media without surfactant. The enzyme may be useful in enhanced degradation of cassava cyanide. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=linamarase" title="linamarase">linamarase</a>, <a href="https://publications.waset.org/abstracts/search?q=locally%20formulated%20media" title=" locally formulated media"> locally formulated media</a>, <a href="https://publications.waset.org/abstracts/search?q=carbon%20substrates" title=" carbon substrates"> carbon substrates</a>, <a href="https://publications.waset.org/abstracts/search?q=nitrogen%20substrates" title=" nitrogen substrates"> nitrogen substrates</a>, <a href="https://publications.waset.org/abstracts/search?q=metal%20ions" title=" metal ions "> metal ions </a> </p> <a href="https://publications.waset.org/abstracts/14419/production-of-linamarase-from-lactobacillus-delbrueckii-nrrl-b-763" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/14419.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">427</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">1168</span> Effect of Ethanol Concentration and Enzyme Pre-Treatment on Bioactive Compounds from Ginger Extract</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=S.%20Lekhavat">S. Lekhavat</a>, <a href="https://publications.waset.org/abstracts/search?q=T.%20Kajsongkram"> T. Kajsongkram</a>, <a href="https://publications.waset.org/abstracts/search?q=S.%20Sang-han"> S. Sang-han</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Dried ginger was extracted and investigated the effect of ethanol concentration and enzyme pre-treatment on its bioactive compounds in solvent extraction process. Sliced fresh gingers were dried by oven dryer at 70 °C for 24 hours and ground to powder using grinder which their size were controlled by passing through a 20-mesh sieve. In enzyme pre-treatment process, ginger powder was sprayed with 1 % (w/w) cellulase and then was incubated at 45 °C for 2 hours following by extraction process using ethanol at concentration of 0, 20, 40, 60 and 80 % (v/v), respectively. The ratio of ginger powder and ethanol are 1:9 and extracting conditions were controlled at 80 °C for 2 hours. Bioactive compounds extracted from ginger, either enzyme-treated or non enzyme-treated samples, such as total phenolic content (TPC), 6-Gingerol (6 G), 6-Shogaols (6 S) and antioxidant activity (IC50 using DPPH assay), were examined. Regardless of enzyme treatment, the results showed that 60 % ethanol provided the highest TPC (20.36 GAE mg /g. dried ginger), 6G (0.77%), 6S (0.036 %) and the lowest IC50 (625 μg/ml) compared to other ratios of ethanol. Considering the effect of enzyme on bioactive compounds and antioxidant activity, it was found that enzyme-treated sample has more 6G (0.17-0.77 %) and 6S (0.020-0.036 %) than non enzyme-treated samples (0.13-0.77 % 6G, 0.015-0.036 % 6S). However, the results showed that non enzyme-treated extracts provided higher TPC (6.76-20.36 GAE mg /g. dried ginger) and Lowest IC50 (625-1494 μg/ml ) than enzyme-treated extracts (TPC 5.36-17.50 GAE mg /g. dried ginger, IC50 793-2146 μg/ml). <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=antioxidant%20activity" title="antioxidant activity">antioxidant activity</a>, <a href="https://publications.waset.org/abstracts/search?q=enzyme" title=" enzyme"> enzyme</a>, <a href="https://publications.waset.org/abstracts/search?q=extraction" title=" extraction"> extraction</a>, <a href="https://publications.waset.org/abstracts/search?q=ginger" title=" ginger"> ginger</a> </p> <a href="https://publications.waset.org/abstracts/53148/effect-of-ethanol-concentration-and-enzyme-pre-treatment-on-bioactive-compounds-from-ginger-extract" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/53148.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">256</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">1167</span> Synthetic Coumarin Derivatives and Their Anticancer Properties</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Kabange%20Kasumbwe">Kabange Kasumbwe</a>, <a href="https://publications.waset.org/abstracts/search?q=Viresh%20Mohanlall"> Viresh Mohanlall</a>, <a href="https://publications.waset.org/abstracts/search?q=Bharti%20Odhav"> Bharti Odhav</a>, <a href="https://publications.waset.org/abstracts/search?q=Venu%20Narayanaswamy"> Venu Narayanaswamy</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Coumarins are naturally occurring plant metabolites known for their pharmacological properties such as anticoagulant, antimicrobial, anticancer, antioxidant, anti-inflammatory and antiviral properties. The pharmacological and biochemical properties and curative applications of coumarins depend on the substitution around the coumarin core structure. In the present study, seven halogenated coumarins CMRN1-CMRN7 were synthesized and evaluated for their anticancer activity. The cytotoxicity potential of the test compounds was evaluated against UACC62 (Melanoma), MCF-7 (Breast cancer) and PBM (Peripheral Blood Mononuclear) cell lines using MTT assay keeping doxorubicin as standard drug. The apoptotic potential of the coumarin compounds was evaluated against UACC62 (Melanoma) cell by assessing their morphological changes, membrane change, mitochondria membrane potential; pro-apoptotic changes were investigated using the AnnexinV-PI staining, JC-1, caspase-3 enzyme kits respectively on flow cytometer. The synthetic coumarin has strongly suppressed the cell proliferation of UACC-62 (Melanoma) and MCF-7 (Breast) Cancer cells, the higher toxicity of these compounds against UACC-62 (Melanoma) and MCF-7 (Breast) were CMRN3, CMRN4, CMRN5, CMRN6. However, compounds CMRN1, CMRN2, and CMRN7 had no significant inhibitory effect. Furthermore the active compounds CMRN3, CMRN4, CMRN5, CMRN6 exerted antiproliferative effects through apoptosis induction against UACC-62 (Melanoma), suggesting their potential could be considered as attractive lead molecules in the future for the development of potential anticancer agents since one of the important criteria in the development of therapeutic drugs for cancer treatment is to have high selectivity and less or no side-effects on normal cells and these compounds had no inhibitory effect against the PBMC cells. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=coumarin" title="coumarin">coumarin</a>, <a href="https://publications.waset.org/abstracts/search?q=MTT" title=" MTT"> MTT</a>, <a href="https://publications.waset.org/abstracts/search?q=apoptosis" title=" apoptosis"> apoptosis</a>, <a href="https://publications.waset.org/abstracts/search?q=cytotoxicity" title=" cytotoxicity"> cytotoxicity</a> </p> <a href="https://publications.waset.org/abstracts/59987/synthetic-coumarin-derivatives-and-their-anticancer-properties" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/59987.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">238</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">1166</span> Anticancer Activity of Gnidia glauca Extracts in Human Breast Cancer Cells</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Vandana%20Gawande">Vandana Gawande</a>, <a href="https://publications.waset.org/abstracts/search?q=Chandani%20Satija"> Chandani Satija</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Gnidia glauca is a semi-woody herb of thymelaeaceae family traditionally used as fish poison in India. It is also found in Sri lanka and Africa. In the present study, potential anticancer effect of n-hexane and ethanolic extracts of Gnidia glauca in human breast cancer cells was investigated. Human breast cancer cells (MCF-7) were cultured as monolayers in RPMI 1640 medium. The cells were cultured for 48 hours to allow growth and achieve about 80% confluence in 96-well culture plates. The cells were treated with various concentrations of Gnidia glauca (0.1-100 mg/mL) for 72 hours. Percentage of viable cells after treatment was assessed using a sulforhodamine B colorimetric assay. Both n-hexane and ethanolic extract showed significant cytotoxic activity on MCF-7 cancer cells. This study supports the notion of using Gnidia glauca as a novel anticancer agent for breast cancer. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=96%20well%20plate" title="96 well plate">96 well plate</a>, <a href="https://publications.waset.org/abstracts/search?q=anticancer%20activity" title=" anticancer activity"> anticancer activity</a>, <a href="https://publications.waset.org/abstracts/search?q=Gnidia%20glauca" title=" Gnidia glauca"> Gnidia glauca</a>, <a href="https://publications.waset.org/abstracts/search?q=MCF-7" title=" MCF-7"> MCF-7</a> </p> <a href="https://publications.waset.org/abstracts/8569/anticancer-activity-of-gnidia-glauca-extracts-in-human-breast-cancer-cells" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/8569.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">290</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">1165</span> Activation of Caspase 3 by Terpenoids and Flavonoids in Cancer Cell Lines</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Nusrat%20Masood">Nusrat Masood</a>, <a href="https://publications.waset.org/abstracts/search?q=Vijaya%20Dubey"> Vijaya Dubey</a>, <a href="https://publications.waset.org/abstracts/search?q=Suaib%20Luqman"> Suaib Luqman</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Caspase 3, a member of cysteine-aspartic acid protease family, is an imperative indicator for cell death particularly when substantiating apoptosis. Thus, caspase 3 is an interesting target for the discovery and development of anticancer agent. We adopted a four level assessment of both terpenoids and flavonoids and thus experimentally performed the enzymatic assay in cell free system as well as in cancer cell line which was validated through real time expression and molecular interaction studies. A significant difference was observed with both the class of natural products indicating terpenoids as better activators of caspase 3 compared to flavonoids both in the cell free system as well as in cell lines. The expression analysis, activation constant and binding energy also correlate well with the enzyme activity. Overall, terpenoids had an unswerving effect on caspase 3 in all the tested system while flavonoids indirectly affect enzyme activity. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=Caspase%203" title="Caspase 3">Caspase 3</a>, <a href="https://publications.waset.org/abstracts/search?q=terpenoids" title=" terpenoids"> terpenoids</a>, <a href="https://publications.waset.org/abstracts/search?q=flavonoids" title=" flavonoids"> flavonoids</a>, <a href="https://publications.waset.org/abstracts/search?q=activation%20constant" title=" activation constant"> activation constant</a>, <a href="https://publications.waset.org/abstracts/search?q=binding%20energy" title=" binding energy"> binding energy</a> </p> <a href="https://publications.waset.org/abstracts/72938/activation-of-caspase-3-by-terpenoids-and-flavonoids-in-cancer-cell-lines" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/72938.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">238</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">1164</span> The Modeling of Viscous Microenvironment for the Coupled Enzyme System of Bioluminescence Bacteria </h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Irina%20E.%20Sukovataya">Irina E. Sukovataya</a>, <a href="https://publications.waset.org/abstracts/search?q=Oleg%20S.%20Sutormin"> Oleg S. Sutormin</a>, <a href="https://publications.waset.org/abstracts/search?q=Valentina%20A.%20Kratasyuk"> Valentina A. Kratasyuk </a> </p> <p class="card-text"><strong>Abstract:</strong></p> Effect of viscosity of media on kinetic parameters of the coupled enzyme system NADH:FMN-oxidoreductase–luciferase was investigated with addition of organic solvents (glycerol and sucrose), because bioluminescent enzyme systems based on bacterial luciferases offer a unique and general tool for analysis of the many analytes and enzymes in the environment, research, and clinical laboratories and other fields. The possibility of stabilization and increase of activity of the coupled enzyme system NADH:FMN-oxidoreductase–luciferase activity in vicious aqueous-organic mixtures have been shown. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=coupled%20enzyme%20system%20of%20bioluminescence%20bacteria%20NAD%28P%29H%3AFMN-oxidoreductase%E2%80%93luciferase" title="coupled enzyme system of bioluminescence bacteria NAD(P)H:FMN-oxidoreductase–luciferase">coupled enzyme system of bioluminescence bacteria NAD(P)H:FMN-oxidoreductase–luciferase</a>, <a href="https://publications.waset.org/abstracts/search?q=glycerol" title=" glycerol"> glycerol</a>, <a href="https://publications.waset.org/abstracts/search?q=stabilization%20of%20enzymes" title=" stabilization of enzymes"> stabilization of enzymes</a>, <a href="https://publications.waset.org/abstracts/search?q=sucrose" title=" sucrose"> sucrose</a> </p> <a href="https://publications.waset.org/abstracts/2372/the-modeling-of-viscous-microenvironment-for-the-coupled-enzyme-system-of-bioluminescence-bacteria" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/2372.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">1163</span> Indenyl and Allyl Palladates: Synthesis, Bonding, and Anticancer Activity</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=T.%20Scattolin">T. Scattolin</a>, <a href="https://publications.waset.org/abstracts/search?q=E.%20Cavarzerani"> E. Cavarzerani</a>, <a href="https://publications.waset.org/abstracts/search?q=F.%20Visentin"> F. Visentin</a>, <a href="https://publications.waset.org/abstracts/search?q=F.%20Rizzolio"> F. Rizzolio</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Organopalladium compounds have recently attracted attention for their high stability even under physiological conditions and, above all, for their remarkable in vitro cytotoxicity towards cisplatin-resistant cell lines. Among the organopalladium derivatives, those bearing at least one N-heterocyclic carbene ligand (NHC) and the Pd(II)-η³-allyl fragment have exhibited IC₅₀ values in the micro and sub-micromolar range towards several cancer cell lines in vitro and in some cases selectivity towards cancerous vs. non-tumorigenic cells. Herein, a selection of allyl and indenyl palladates were synthesized using a solvent-free method consisting of grinding the corresponding palladium precursors with different saturated and unsaturated azolium salts. All compounds have been fully characterized by NMR, XRD and elemental analyses. The intramolecular H, Cl interaction has been elucidated and quantified using the Voronoi Deformation Density scheme. Most of the complexes showed excellent cytotoxicity towards ovarian cancer cell lines, with I₅₀ values comparable to or even lower than cisplatin. Interestingly, the potent anticancer activity was also confirmed in a high-serous ovarian cancer (HGSOC) patient-derived tumoroid, with a clear superiority of this class of compounds over classical platinum-based agents. Finally, preliminary enzyme inhibition studies of the synthesized palladate complexes against the model TrxR show that the compounds have high activity comparable to or even higher than auranofin and classical Au(I) NHC complexes. Based on such promising data, further in vitro and in vivo experiments and in-depth mechanistic studies are ongoing in our laboratories. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=anticancer%20activity" title="anticancer activity">anticancer activity</a>, <a href="https://publications.waset.org/abstracts/search?q=palladium%20complexes" title=" palladium complexes"> palladium complexes</a>, <a href="https://publications.waset.org/abstracts/search?q=organoids" title=" organoids"> organoids</a>, <a href="https://publications.waset.org/abstracts/search?q=indenyl%20and%20allyl%20ligands" title=" indenyl and allyl ligands"> indenyl and allyl ligands</a> </p> <a href="https://publications.waset.org/abstracts/148846/indenyl-and-allyl-palladates-synthesis-bonding-and-anticancer-activity" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/148846.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">94</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">1162</span> Quality of Low Fat Traditional Pork Sausage Containing Transglutaminase</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Jiraporn%20Burakorn">Jiraporn Burakorn</a>, <a href="https://publications.waset.org/abstracts/search?q=Pran%20Pinthong"> Pran Pinthong</a>, <a href="https://publications.waset.org/abstracts/search?q=Supida%20Hutabaedya"> Supida Hutabaedya</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Commercial traditional pork sausages (Moo Yaw) were produced by added more than 30% of pork fat for appetite customer. The pork sausages texture were softness, firmness, juiciness and smooth. If the pork sausages contained less fat, their textures were hardness, dryness and incoherence. This research investigated production of low fat traditional pork sausage containing transglutaminase for improved its sensory properties and nutritive values. The enzyme pork sausage composed of transglutaminase, soybean cake, rice bran oil and other ingredients. Consumer acceptance test was done by comparing the enzyme pork sausage with the 3 commercial pork sausage with 95 consumer. The enzyme pork sausage was accepted 92.6% and was preferred in all attributes over the 3 commercial pork sausages such as appearance, color, flavor, taste, firmness and overall liking. The enzyme pork sausage was high protein but low total calories, calories from fat, total fat, saturated fat, cholesterol and carbohydrate. The enzyme pork sausage was lower calorie (90 kcal) than the commercial reference pork sausage (150 kcal) 64%. The morphological texture of the enzyme pork sausage was smooth and consistency when analyzed by SEM. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=low%20fat" title="low fat">low fat</a>, <a href="https://publications.waset.org/abstracts/search?q=Moo%20Yaw" title=" Moo Yaw"> Moo Yaw</a>, <a href="https://publications.waset.org/abstracts/search?q=pork%20sausage" title=" pork sausage"> pork sausage</a>, <a href="https://publications.waset.org/abstracts/search?q=transglutaminase" title=" transglutaminase"> transglutaminase</a> </p> <a href="https://publications.waset.org/abstracts/58317/quality-of-low-fat-traditional-pork-sausage-containing-transglutaminase" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/58317.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">230</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">1161</span> Enzyme Immobilization on Functionalized Polystyrene Nanofibersfor Bioprocessing Applications</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Mailin%20Misson">Mailin Misson</a>, <a href="https://publications.waset.org/abstracts/search?q=Bo%20Jin"> Bo Jin</a>, <a href="https://publications.waset.org/abstracts/search?q=Sheng%20Dai"> Sheng Dai</a>, <a href="https://publications.waset.org/abstracts/search?q=Hu%20Zhang"> Hu Zhang</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Advances in biotechnology have witnessed a growing interest in enzyme applications for the development of green and sustainable bio processes. While known as powerful bio catalysts, enzymes are no longer of economic value when extended to large commercialization. Alternatively, immobilization technology allows enzyme recovery and continuous reuse which subsequently compensates high operating costs. Employment of enzymes on nano structured materials has been recognized as a promising approach to enhance enzyme catalytic performances. High porosity, inter connectivity and self-assembling behaviors endow nano fibers as exciting candidate for enzyme carrier in bio reactor systems. In this study, nano fibers were successfully fabricated via electro spinning system by optimizing the polymer concentration (10-30 %, w/v), applied voltage (10-30 kV) and discharge distance (11-26 cm). Microscopic images have confirmed the quality as homogeneous and good fiber alignment. The nano fibers surface was modified using strong oxidizing agent to facilitate bio molecule binding. Bovine serum albumin and β-galactosidase enzyme were employed as model bio catalysts and immobilized onto the oxidized surfaces through covalent binding. Maximum enzyme adsorption capacity of the modified nano fibers was 3000 mg/g, 3-fold higher than the unmodified counterpart (1000 mg/g). The highest immobilization yield was 80% and reached the saturation point at 2 mg/ml of enzyme concentration. The results indicate a significant increase of activity retention by the enzyme-bound modified nano fibers (80%) as compared to the nascent one (60%), signifying excellent enzyme-nano carrier bio compatibility. The immobilized enzyme was further used for the bio conversion of dairy wastes into value-added products. This study demonstrates great potential of acid-modified electrospun polystyrene nano fibers as enzyme carriers. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=immobilization" title="immobilization">immobilization</a>, <a href="https://publications.waset.org/abstracts/search?q=enzyme" title=" enzyme"> enzyme</a>, <a href="https://publications.waset.org/abstracts/search?q=nanocarrier" title=" nanocarrier"> nanocarrier</a>, <a href="https://publications.waset.org/abstracts/search?q=nanofibers" title=" nanofibers"> nanofibers</a> </p> <a href="https://publications.waset.org/abstracts/15802/enzyme-immobilization-on-functionalized-polystyrene-nanofibersfor-bioprocessing-applications" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/15802.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">293</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">1160</span> Evaluation of Antioxidant and Anticancer Activity of Tinospora cordifolia against Ehrlich Ascites Carcinoma: In Vitro, in vivo and in silico Approach</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Anik%20Barua">Anik Barua</a>, <a href="https://publications.waset.org/abstracts/search?q=Rabiul%20Hossain"> Rabiul Hossain</a>, <a href="https://publications.waset.org/abstracts/search?q=Labonno%20Barua"> Labonno Barua</a>, <a href="https://publications.waset.org/abstracts/search?q=Rashadul%20Hossain"> Rashadul Hossain</a>, <a href="https://publications.waset.org/abstracts/search?q=Nurul%20Absar"> Nurul Absar</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Background: Globally, the burden of cancer is increasing consistently. Modern cancer therapies include lots of toxicity in the non-targeted organs reducing the life expectancy of the patients. Hence, scientists are trying to seek noble compounds from natural sources to treat cancer. Objectives: The objectives of the present study are to evaluate the phytochemicals, in vitro antioxidants, and in vivo and in silico anticancer study of various solvent fractions of Tinospora cordifolia (Willd.). Methodology: In this experiment, standard quantitative and qualitative assay methods were used to analyze the phytochemicals. The antioxidant activity was measured using the DPPH and ABTS scavenging methods. The in vivo antitumor activity is evaluated against Ehrlich ascites carcinoma (EAC) cell bearing in Swiss albino mice. In-silico ADME/T and molecular docking study were performed to assess the potential of stated phytochemicals against Transcription Factor STAT3b/DNA Complex of adenocarcinoma. Findings: Phytochemical screening confirmed the presence of flavonoids, alkaloids, glycosides, tannins, and carbohydrates. A significant amount of phenolic (20.19±0.3 mg/g GAE) and flavonoids (9.46±0.18 mg/g GAE) were found in methanolic extract in quantitative screening. Tinospora cordifolia methanolic extract showed promising DPPH and ABTS scavenging activity with the IC50 value of 1222.99 µg/mL and 1534.34 µg/mL, respectively, which was concentration dependent. In vivo anticancer activity in EAC cell-bearing mice showed significant (P < 0.05) percent inhibition of cell growth (60.12±1.22) was found at the highest dose compared with standard drug 5-Fluorouracil (81.18±1.28). Forty-two phytochemicals exhibit notable pharmacokinetics properties and passed drug-likeness screening tests in silico. In molecular docking study, (25S)-3Beta-acetoxy-5-alpha-22-beta-spirost-9(11)-en-12-beta-ol showed docking score (-8.5 kJ/mol) with significant non-bonding interactions with target enzyme. Conclusions: The results were found to be significant and confirmed that the methanolic extract of Tinospora cordifolia has remarkable antitumor activity with antioxidant potential. The Tinospora cordifolia methanolic extract may be considered a potent anticancer agent for advanced research. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=anticancer" title="anticancer">anticancer</a>, <a href="https://publications.waset.org/abstracts/search?q=antioxidant" title=" antioxidant"> antioxidant</a>, <a href="https://publications.waset.org/abstracts/search?q=Tinospora%20cordifolia" title=" Tinospora cordifolia"> Tinospora cordifolia</a>, <a href="https://publications.waset.org/abstracts/search?q=EAC%20cell" title=" EAC cell"> EAC cell</a> </p> <a href="https://publications.waset.org/abstracts/157005/evaluation-of-antioxidant-and-anticancer-activity-of-tinospora-cordifolia-against-ehrlich-ascites-carcinoma-in-vitro-in-vivo-and-in-silico-approach" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/157005.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">129</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">1159</span> Hexane Extract of Thymus serpyllum L.: GC-MS Profile, Antioxidant Potential and Anticancer Impact on HepG2 (Liver Carcinoma) Cell Line</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Salma%20Baig">Salma Baig</a>, <a href="https://publications.waset.org/abstracts/search?q=Bakrudeen%20Ali%20Ahmad"> Bakrudeen Ali Ahmad</a>, <a href="https://publications.waset.org/abstracts/search?q=Ainnul%20Hamidah%20Syahadah%20Azizan"> Ainnul Hamidah Syahadah Azizan</a>, <a href="https://publications.waset.org/abstracts/search?q=Hapipah%20Mohd%20Ali"> Hapipah Mohd Ali</a>, <a href="https://publications.waset.org/abstracts/search?q=Elham%20Rouhollahi"> Elham Rouhollahi</a>, <a href="https://publications.waset.org/abstracts/search?q=Mahmood%20Ameen%20Abdulla"> Mahmood Ameen Abdulla</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Free radical damage induced by reactive oxygen species (ROS) contributes to etiology of many chronic diseases, cancer being one of them. Recent studies have been successful in ROS targeted therapies via antioxidants using mouse models in cancer therapeutics. The present study was designed to scrutinize anticancer activity, antioxidant activity of 5 different extracts of Thymus serpyllum in MDA-MB-231, MCF-7, HepG2, HCT-116, PC3, and A549. Identification of the phytochemicals present in the most active extract of Thymus serpyllum was conducted using gas chromatography coupled with mass spectrophotometry and antioxidant activity was measured by using DPPH radical scavenging and FRAP assay. Anticancer impact of the extract in terms of IC50 was evaluated using MTT cell viability assay. Results revealed that the hexane extract showed the best anticancer activity in HepG2 (Liver Carcinoma Cell Line) with an IC50 value of 23 ± 0.14 µg/ml followed by 25 µg/ml in HCT-116 (Colon Cancer Cell Line), 30 µm/ml in MCF-7 (Breast Cancer Cell Line), 35 µg/ml in MDA-MB-231 (Breast Cancer Cell Line), 57 µg/ml in PC3 (Prostate Cancer Cell Line) and 60 µg/ml in A549 (Lung Carcinoma Cell Line). GC-MS profile of the hexane extract showed the presence of 31 compounds with carvacrol, thymol and thymoquione being the major compounds. Phenolics such as Vitamin E, terpinen-4-ol, borneol and phytol were also identified. Hence, here we present the first report on cytotoxicity of hexane extract of Thymus serpyllum extract in HepG2 cell line with a robust anticancer activity with an IC50 of 23 ± 0.14 µg/ml. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=Thymus%20serpyllum%20L." title="Thymus serpyllum L.">Thymus serpyllum L.</a>, <a href="https://publications.waset.org/abstracts/search?q=hexane%20extract" title=" hexane extract"> hexane extract</a>, <a href="https://publications.waset.org/abstracts/search?q=GC-MS%20profile" title=" GC-MS profile"> GC-MS profile</a>, <a href="https://publications.waset.org/abstracts/search?q=antioxidant%20activity" title=" antioxidant activity"> antioxidant activity</a>, <a href="https://publications.waset.org/abstracts/search?q=anticancer%20activity" title=" anticancer activity"> anticancer activity</a>, <a href="https://publications.waset.org/abstracts/search?q=HepG2%20cell%20line" title=" HepG2 cell line"> HepG2 cell line</a> </p> <a href="https://publications.waset.org/abstracts/13474/hexane-extract-of-thymus-serpyllum-l-gc-ms-profile-antioxidant-potential-and-anticancer-impact-on-hepg2-liver-carcinoma-cell-line" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/13474.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">517</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">1158</span> Biosynthesis of L-Xylose from Xylitol Using a Dual Enzyme Cascade in Escherichia coli</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Mesfin%20Angaw%20Tesfay">Mesfin Angaw Tesfay</a> </p> <p class="card-text"><strong>Abstract:</strong></p> L-xylose is an important intermediate in the pharmaceutical industry, playing a key role in the production of various antiviral and anticancer drugs. Despite its significance, L-xylose is a rare and costly sugar with limited availability in nature. In recent years, enzymatic production methods have garnered considerable attention due to their benefits over conventional chemical synthesis. In this research, a dual enzyme cascade system was developed to synthesize L-xylose from an inexpensive substrate, xylitol. The study involved cloning and co-expressing two key genes: the L-fucose isomerase (L-fucI) gene from Escherichia coli K-12 and the xylitol-4-dehydrogenase (xdh) gene from Pantoea ananatis ATCC 43072 in Escherichia coli. The resulting recombinant cells, engineered with the PET28a-xdh/L-fucI vector, were able to effectively convert xylitol to L-xylose. The system showed optimal performance at 40°C and a pH of 10.0. Moreover, Zn²⁺ (7.5 mM) enhanced the catalytic activity by 1.34 times. This approach yielded 52.2 g/L of L-xylose from an initial 80 g/L xylitol concentration, with a 65% conversion efficiency and a productivity rate of 1.86. The study highlights a practical method for producing L-xylose from xylitol through a co-expression system carrying the L-fucI and xdh genes. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=l-fucose%20isomerase" title="l-fucose isomerase">l-fucose isomerase</a>, <a href="https://publications.waset.org/abstracts/search?q=xylitol-4-dehydrogenase" title=" xylitol-4-dehydrogenase"> xylitol-4-dehydrogenase</a>, <a href="https://publications.waset.org/abstracts/search?q=l-xylose" title=" l-xylose"> l-xylose</a>, <a href="https://publications.waset.org/abstracts/search?q=xylitol" title=" xylitol"> xylitol</a>, <a href="https://publications.waset.org/abstracts/search?q=co-expression" title=" co-expression"> co-expression</a> </p> <a href="https://publications.waset.org/abstracts/192338/biosynthesis-of-l-xylose-from-xylitol-using-a-dual-enzyme-cascade-in-escherichia-coli" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/192338.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">25</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">1157</span> Development of Self Emulsifying Drug Delivery Systems (SEDDS) of Anticancer Agents Used in AYUSH System of Medicine for Improved Oral Bioavailability Followed by Their Pharmacological Evaluation Using Biotechnological Techniques</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Meenu%20Mehta">Meenu Mehta</a>, <a href="https://publications.waset.org/abstracts/search?q=Munish%20Garg"> Munish Garg</a> </p> <p class="card-text"><strong>Abstract:</strong></p> The use of oral anticancer drugs from AYUSH system of medicine is widely increased among the society due to their low cost, enhanced efficacy, increased patient preference, lack of inconveniences related to infusion and they provide an opportunity to develop chronic treatment regimens. However, oral delivery of these drugs usually laid down by the limited bioavailability of the drug, which is associated with a wide variation. As most of the cytotoxic agents have a narrow therapeutic window and are dosed at or near the maximum tolerated dose, a wide variability in the bioavailability can negatively affect treatment result. It is estimated that 40% of active substances are poorly soluble in water. The improvement of bio-availability of drugs with such properties presents one of the greatest challenges in drug formulations. There are several techniques reported in literature. Among all these Self Emulsifying Drug Delivery System (SEDDS) has gained more attention due to enhanced oral bio-availability enabling a reduction in dose. Thus, SEDDS anticancer drugs will have the increased bioavailability and efficacy. These dosage form will provide societal benefit in a cost-effective manner as compared to other oral dosage forms. Present study reflects on the formulation strategies as SEDDS for oral anticancer agents of AYUSH system for enhanced bioavailability with proven efficacy by cancer cell lines. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=anticancer%20agents" title="anticancer agents">anticancer agents</a>, <a href="https://publications.waset.org/abstracts/search?q=AYUSH%20system" title=" AYUSH system"> AYUSH system</a>, <a href="https://publications.waset.org/abstracts/search?q=bioavailability" title=" bioavailability"> bioavailability</a>, <a href="https://publications.waset.org/abstracts/search?q=SEDDS" title=" SEDDS"> SEDDS</a> </p> <a href="https://publications.waset.org/abstracts/58981/development-of-self-emulsifying-drug-delivery-systems-sedds-of-anticancer-agents-used-in-ayush-system-of-medicine-for-improved-oral-bioavailability-followed-by-their-pharmacological-evaluation-using-biotechnological-techniques" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/58981.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">306</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">1156</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">1155</span> In-House Enzyme Blends from Polyporus ciliatus CBS 366.74 for Enzymatic Saccharification of Pretreated Corn Stover</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Joseph%20A.%20Bentil">Joseph A. Bentil</a>, <a href="https://publications.waset.org/abstracts/search?q=Anders%20Thygesen"> Anders Thygesen</a>, <a href="https://publications.waset.org/abstracts/search?q=Lene%20Langea"> Lene Langea</a>, <a href="https://publications.waset.org/abstracts/search?q=Moses%20Mensah"> Moses Mensah</a>, <a href="https://publications.waset.org/abstracts/search?q=Anne%20Meyer"> Anne Meyer</a> </p> <p class="card-text"><strong>Abstract:</strong></p> The study investigated the saccharification potential of in-house enzymes produced from a white-rot basidiomycete strain, Polyporus ciliatus CBS 366.74. The in-house enzymes were produced by growing the fungus on mono and composite substrates of cocoa pod husk (CPH) and green seaweed (GS) (Ulva lactuca sp.) with and without the addition of 25mM ammonium nitrate at 4%w/v substrate concentration in submerged condition for 144 hours. The crude enzyme extracts preparations (CEE 1-5 and CEE 1-5+AN) obtained from the fungal cultivation process were sterile-filtered and used as enzyme sources for enzymatic hydrolysis of hydrothermally pretreated corn stover using a commercial cocktail enzyme, Cellic Ctec3, as benchmark. The hydrolysis was conducted at 50ᵒC with 50mM sodium acetate buffer, pH 5 based on enzyme dosages of 5 and 10 CMCase Units/g biomass at 1%w/v dry weight substrate concentration at time points of 6, 24, and 72 hours. The enzyme activity profile of the in-house enzymes varied among the growth substrates with the composite substrates (50-75% GS and AN inclusion), yielding better enzyme activities, especially endoglucanases (0.4-0.5U/mL), β-glucosidases (0.1-0.2 U/mL), and xylanases (3-10 U/mL). However, nitrogen supplementation had no significant effect on enzyme activities of crude extracts from 100% GS substituted substrates. From the enzymatic hydrolysis, it was observed that the in-house enzymes were capable of hydrolysing the pretreated corn stover at varying degrees; however, the saccharification yield was less than 10%. Consequently, theoretical glucose yield was ten times lower than Cellic Ctec3 at both dosage levels. There was no linear correlation between glucose yield and enzyme dosage for the in-house enzymes, unlike the benchmark enzyme. It is therefore recommended that the in-house enzymes are used to complement the dosage of commercial enzymes to reduce the cost of biomass saccharification. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=enzyme%20production" title="enzyme production">enzyme production</a>, <a href="https://publications.waset.org/abstracts/search?q=hydrolysis%20yield" title=" hydrolysis yield"> hydrolysis yield</a>, <a href="https://publications.waset.org/abstracts/search?q=feedstock" title=" feedstock"> feedstock</a>, <a href="https://publications.waset.org/abstracts/search?q=enzyme%20blend" title=" enzyme blend"> enzyme blend</a>, <a href="https://publications.waset.org/abstracts/search?q=Polyporus%20ciliatus" title=" Polyporus ciliatus"> Polyporus ciliatus</a> </p> <a href="https://publications.waset.org/abstracts/138804/in-house-enzyme-blends-from-polyporus-ciliatus-cbs-36674-for-enzymatic-saccharification-of-pretreated-corn-stover" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/138804.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">267</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">1154</span> Metal-Based Anticancer Agents: In vitro DNA Binding, Cleavage and Cytotoxicity</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Mala%20Nath">Mala Nath</a>, <a href="https://publications.waset.org/abstracts/search?q=Nagamani%20Kompelli"> Nagamani Kompelli</a>, <a href="https://publications.waset.org/abstracts/search?q=Partha%20Roy"> Partha Roy</a>, <a href="https://publications.waset.org/abstracts/search?q=Snehasish%20Das"> Snehasish Das</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Two new metal-based anticancer chemotherapeutic agents, [(Ph2Sn)2(HGuO)2(phen)Cl2] 1 and [(Ph3Sn)(HGuO)(phen)]- Cl.CH3OH.H2O 2, were designed, prepared and characterized by analytical and spectral (IR, ESI-Mass, 1H, 13C and 119Sn NMR) techniques. The proposed geometry of Sn(IV) in 1 and 2 is distorted octahedral and distorted trigonal-bipyramidal, respectively. Both 1 and 2 exhibit potential cytotoxicity in vitro against MCF-7, HepG-2 and DU-145 cell lines. The intrinsic binding constant (Kb) values of 1 (2.33 × 105 M-1) and 2 (2.46 × 105 M-1) evaluated from UV-Visible absorption studies suggest non-classical electrostatic mode of interaction via phosphate backbone of DNA double helix. The Stern-Volmer quenching constant (Ksv) of 1 (9.74 × 105 M-1) and 2 (2.9 × 106 M-1) determined by fluorescence studies suggests the groove binding and intercalation mode for 1 and 2, respectively. Effective cleavage of pBR322 DNA is induced by 1. Their interaction with DNA of cancer cells may account for potency. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=anticancer%20agents" title="anticancer agents">anticancer agents</a>, <a href="https://publications.waset.org/abstracts/search?q=DNA%20binding%20studies" title=" DNA binding studies"> DNA binding studies</a>, <a href="https://publications.waset.org/abstracts/search?q=NMR%20spectroscopy" title=" NMR spectroscopy"> NMR spectroscopy</a>, <a href="https://publications.waset.org/abstracts/search?q=organotin" title=" organotin"> organotin</a> </p> <a href="https://publications.waset.org/abstracts/7525/metal-based-anticancer-agents-in-vitro-dna-binding-cleavage-and-cytotoxicity" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/7525.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">257</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">1153</span> Characterization of the Catalytic and Structural Roles of the Human Hexokinase 2 in Cancer Progression</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Mir%20Hussain%20Nawaz">Mir Hussain Nawaz</a>, <a href="https://publications.waset.org/abstracts/search?q=Lyudmila%20Nedyalkova"> Lyudmila Nedyalkova</a>, <a href="https://publications.waset.org/abstracts/search?q=Haizhong%20Zhu"> Haizhong Zhu</a>, <a href="https://publications.waset.org/abstracts/search?q=Wael%20M.%20Rabeh"> Wael M. Rabeh</a> </p> <p class="card-text"><strong>Abstract:</strong></p> In this study, we aim to biochemically and structurally characterize the interactions of human HK2 with the mitochondria in addition to the role of its N-terminal domain in catalysis and stability of the full-length enzyme. Here, we solved the crystal structure of human HK2 in complex with glucose and glucose-6-phosphate (PDB code: 2NZT), where it is a homodimer with catalytically active N- and C-terminal domains linked by a seven-turn α-helix. Different from the inactive N-terminal domains of isozymes 1 and 3, the N- domain of HK2 not only capable to catalyze a reaction but it is responsible for the thermodynamic stabilizes of the full-length enzyme. Deletion of first α-helix of the N-domain that binds to the mitochondria altered the stability and catalytic activity of the full-length HK2. In addition, we found the linker helix between the N- and C-terminal domains to play an important role in controlling the catalytic activity of the N-terminal domain. HK2 is a major step in the regulation of glucose metabolism in cancer making it an ideal target for the development of new anticancer therapeutics. Characterizing the structural and molecular mechanisms of human HK2 and its role in cancer metabolism will accelerate the design and development of new cancer therapeutics that are safe and cancer specific. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=cancer%20metabolism" title="cancer metabolism">cancer metabolism</a>, <a href="https://publications.waset.org/abstracts/search?q=enzymology" title=" enzymology"> enzymology</a>, <a href="https://publications.waset.org/abstracts/search?q=drug%20discovery" title=" drug discovery"> drug discovery</a>, <a href="https://publications.waset.org/abstracts/search?q=protein%20stability" title=" protein stability"> protein stability</a> </p> <a href="https://publications.waset.org/abstracts/62099/characterization-of-the-catalytic-and-structural-roles-of-the-human-hexokinase-2-in-cancer-progression" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/62099.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">1152</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> <ul class="pagination"> <li class="page-item disabled"><span class="page-link">&lsaquo;</span></li> <li class="page-item active"><span class="page-link">1</span></li> <li class="page-item"><a class="page-link" href="https://publications.waset.org/abstracts/search?q=anticancer%20enzyme&amp;page=2">2</a></li> <li class="page-item"><a class="page-link" href="https://publications.waset.org/abstracts/search?q=anticancer%20enzyme&amp;page=3">3</a></li> <li class="page-item"><a class="page-link" href="https://publications.waset.org/abstracts/search?q=anticancer%20enzyme&amp;page=4">4</a></li> <li class="page-item"><a class="page-link" href="https://publications.waset.org/abstracts/search?q=anticancer%20enzyme&amp;page=5">5</a></li> <li class="page-item"><a class="page-link" href="https://publications.waset.org/abstracts/search?q=anticancer%20enzyme&amp;page=6">6</a></li> <li class="page-item"><a class="page-link" href="https://publications.waset.org/abstracts/search?q=anticancer%20enzyme&amp;page=7">7</a></li> <li class="page-item"><a class="page-link" href="https://publications.waset.org/abstracts/search?q=anticancer%20enzyme&amp;page=8">8</a></li> <li class="page-item"><a class="page-link" href="https://publications.waset.org/abstracts/search?q=anticancer%20enzyme&amp;page=9">9</a></li> <li class="page-item"><a class="page-link" href="https://publications.waset.org/abstracts/search?q=anticancer%20enzyme&amp;page=10">10</a></li> <li class="page-item disabled"><span class="page-link">...</span></li> <li class="page-item"><a class="page-link" href="https://publications.waset.org/abstracts/search?q=anticancer%20enzyme&amp;page=39">39</a></li> <li class="page-item"><a class="page-link" href="https://publications.waset.org/abstracts/search?q=anticancer%20enzyme&amp;page=40">40</a></li> <li class="page-item"><a class="page-link" href="https://publications.waset.org/abstracts/search?q=anticancer%20enzyme&amp;page=2" rel="next">&rsaquo;</a></li> </ul> </div> </main> <footer> <div id="infolinks" class="pt-3 pb-2"> <div class="container"> <div style="background-color:#f5f5f5;" class="p-3"> <div class="row"> <div class="col-md-2"> <ul class="list-unstyled"> About <li><a href="https://waset.org/page/support">About Us</a></li> <li><a href="https://waset.org/page/support#legal-information">Legal</a></li> <li><a target="_blank" rel="nofollow" href="https://publications.waset.org/static/files/WASET-16th-foundational-anniversary.pdf">WASET celebrates its 16th foundational anniversary</a></li> </ul> </div> <div class="col-md-2"> <ul class="list-unstyled"> Account <li><a href="https://waset.org/profile">My Account</a></li> </ul> </div> <div class="col-md-2"> <ul 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