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[PMID]:29310025
[Au] Autor:Madhu Sekhar M; Nagarjuna U; Padmavathi V; Padmaja A; Reddy NV; Vijaya T
[Ad] Endereço:Department of Chemistry, Sri Venkateswara University, Tirupati 517 502, Andhra Pradesh, India.
[Ti] Título:Synthesis and antimicrobial activity of pyrimidinyl 1,3,4-oxadiazoles, 1,3,4-thiadiazoles and 1,2,4-triazoles.
[So] Source:Eur J Med Chem;145:1-10, 2018 Feb 10.
[Is] ISSN:1768-3254
[Cp] País de publicação:France
[La] Idioma:eng
[Ab] Resumo:A new class of methylthio linked pyrimidinyl 1,3,4-oxadiazoles, 1,3,4-thiadiazoles and 1,2,4-triazoles were prepared under conventional and ultrasound irradiation methods. All the compounds were obtained in higher yields and in shorter reaction times in ultrasound irradiation method when compared with the conventional method. The title compounds were tested for antimicrobial activity. The compounds 12c and 12f exhibited promising antibacterial activity against P. aeruginosa whereas the compounds 13c and 13f showed pronounced antifungal activity against A. niger.
[Mh] Termos MeSH primário: Antibacterianos/farmacologia
Antifúngicos/farmacologia
Aspergillus niger/efeitos dos fármacos
Oxidiazóis/farmacologia
Pseudomonas aeruginosa/efeitos dos fármacos
Pirimidinas/farmacologia
Tiadiazóis/farmacologia
Triazóis/farmacologia
[Mh] Termos MeSH secundário: Antibacterianos/síntese química
Antibacterianos/química
Antifúngicos/síntese química
Antifúngicos/química
Relação Dose-Resposta a Droga
Testes de Sensibilidade Microbiana
Estrutura Molecular
Oxidiazóis/síntese química
Oxidiazóis/química
Pirimidinas/síntese química
Pirimidinas/química
Relação Estrutura-Atividade
Tiadiazóis/síntese química
Tiadiazóis/química
Triazóis/síntese química
Triazóis/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anti-Bacterial Agents); 0 (Antifungal Agents); 0 (Oxadiazoles); 0 (Pyrimidines); 0 (Thiadiazoles); 0 (Triazoles); 14IAC3GH7G (1,3,4-thiadiazole)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180227
[Lr] Data última revisão:
180227
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180109
[St] Status:MEDLINE


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[PMID]:29334221
[Au] Autor:Liu L; Gong W; Sun X; Chen G; Wang L
[Ad] Endereço:State Key Laboratory of Microbial Technology, Shandong University , 27 Shandanan Road, Jinan 250100, China.
[Ti] Título:Extracellular Enzyme Composition and Functional Characteristics of Aspergillus niger An-76 Induced by Food Processing Byproducts and Based on Integrated Functional Omics.
[So] Source:J Agric Food Chem;66(5):1285-1295, 2018 Feb 07.
[Is] ISSN:1520-5118
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Byproducts of food processing can be utilized for the production of high-value-added enzyme cocktails. In this study, we utilized integrated functional omics technology to analyze composition and functional characteristics of extracellular enzymes produced by Aspergillus niger grown on food processing byproducts. The results showed that oligosaccharides constituted by arabinose, xylose, and glucose in wheat bran were able to efficiently induce the production of extracellular enzymes of A. niger. Compared with other substrates, wheat bran was more effective at inducing the secretion of ß-glucosidases from GH1 and GH3 families, as well as >50% of proteases from A1-family aspartic proteases. Compared with proteins induced by single wheat bran or soybean dregs, the protein yield induced by their mixture was doubled, and the time required to reach peak enzyme activity was shortened by 25%. This study provided a technical platform for the complex formulation of various substrates and functional analysis of extracellular enzymes.
[Mh] Termos MeSH primário: Aspergillus niger/enzimologia
Aspergillus niger/crescimento & desenvolvimento
Indução Enzimática/efeitos dos fármacos
Manipulação de Alimentos
Oligossacarídeos/farmacologia
Resíduos
[Mh] Termos MeSH secundário: Arabinose/farmacologia
Ácido Aspártico Proteases/biossíntese
Celulases/biossíntese
Fibras na Dieta/análise
Grãos Comestíveis/química
Fermentação
Glucose/farmacologia
Glicosídeo Hidrolases/biossíntese
Peptídeo Hidrolases/biossíntese
Xilose/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Dietary Fiber); 0 (Oligosaccharides); 0 (Waste Products); A1TA934AKO (Xylose); B40ROO395Z (Arabinose); EC 3.2.1.- (Cellulases); EC 3.2.1.- (Glycoside Hydrolases); EC 3.4.- (Aspartic Acid Proteases); EC 3.4.- (Peptide Hydrolases); IY9XDZ35W2 (Glucose)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180226
[Lr] Data última revisão:
180226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180116
[St] Status:MEDLINE
[do] DOI:10.1021/acs.jafc.7b05164


  3 / 4802 MEDLINE  
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[PMID]:29184998
[Au] Autor:Cürten C; Anders N; Juchem N; Ihling N; Volkenborn K; Knapp A; Jaeger KE; Büchs J; Spiess AC
[Ad] Endereço:Aachener Verfahrenstechnik-Enzyme Process Technology, RWTH Aachen University, Worringer Weg 1, 52074, Aachen, Germany.
[Ti] Título:Fast automated online xylanase activity assay using HPAEC-PAD.
[So] Source:Anal Bioanal Chem;410(1):57-69, 2018 Jan.
[Is] ISSN:1618-2650
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:In contrast to biochemical reactions, which are often carried out under automatic control and maintained overnight, the automation of chemical analysis is usually neglected. Samples are either analyzed in a rudimentary fashion using in situ techniques, or aliquots are withdrawn and stored to facilitate more precise offline measurements, which can result in sampling and storage errors. Therefore, in this study, we implemented automated reaction control, sampling, and analysis. As an example, the activities of xylanases on xylotetraose and soluble xylan were examined using high-performance anion exchange chromatography with pulsed amperometric detection (HPAEC-PAD). The reaction was performed in HPLC vials inside a temperature-controlled Dionex™ AS-AP autosampler. It was started automatically when the autosampler pipetted substrate and enzyme solution into the reaction vial. Afterwards, samples from the reaction vial were injected repeatedly for 60 min onto a CarboPac™ PA100 column for analysis. Due to the rapidity of the reaction, the analytical method and the gradient elution of 200 mM sodium hydroxide solution and 100 mM sodium hydroxide with 500 mM sodium acetate were adapted to allow for an overall separation time of 13 min and a detection limit of 0.35-1.83 mg/L (depending on the xylooligomer). This analytical method was applied to measure the soluble short-chain products (xylose, xylobiose, xylotriose, xylotetraose, xylopentaose, and longer xylooligomers) that arise during enzymatic hydrolysis. Based on that, the activities of three endoxylanases (EX) were determined as 294 U/mg for EX from Aspergillus niger, 1.69 U/mg for EX from Bacillus stearothermophilus, and 0.36 U/mg for EX from Bacillus subtilis. Graphical abstract Xylanase activity assay automation.
[Mh] Termos MeSH primário: Aspergillus niger/enzimologia
Cromatografia por Troca Iônica/métodos
Endo-1,4-beta-Xilanases/metabolismo
Ensaios Enzimáticos/métodos
Geobacillus stearothermophilus/enzimologia
[Mh] Termos MeSH secundário: Cromatografia Líquida de Alta Pressão/métodos
Cromatografia por Troca Iônica/economia
Endo-1,4-beta-Xilanases/análise
Ensaios Enzimáticos/economia
Hidrólise
Limite de Detecção
Fatores de Tempo
Xilanos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Xylans); EC 3.2.1.8 (Endo-1,4-beta Xylanases)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180226
[Lr] Data última revisão:
180226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171130
[St] Status:MEDLINE
[do] DOI:10.1007/s00216-017-0712-0


  4 / 4802 MEDLINE  
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[PMID]:29301523
[Au] Autor:Fierascu I; Ungureanu C; Avramescu SM; Cimpeanu C; Georgescu MI; Fierascu RC; Ortan A; Sutan AN; Anuta V; Zanfirescu A; Dinu-Pirvu CE; Velescu BS
[Ad] Endereço:The National Institute for Research & Development in Chemistry and Petrochemistry, ICECHIM, 202 Spl. Independentei, 060021, Bucharest, Romania.
[Ti] Título:Genoprotective, antioxidant, antifungal and anti-inflammatory evaluation of hydroalcoholic extract of wild-growing Juniperus communis L. (Cupressaceae) native to Romanian southern sub-Carpathian hills.
[So] Source:BMC Complement Altern Med;18(1):3, 2018 Jan 04.
[Is] ISSN:1472-6882
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Juniperus communis L. represents a multi-purpose crop used in the pharmaceutical, food, and cosmetic industry. Several studies present the possible medicinal properties of different Juniperus taxa native to specific geographical area. The present study aims to evaluate the genoprotective, antioxidant, antifungal and anti-inflammatory potential of hydroalcoholic extract of wild-growing Juniperus communis L. (Cupressaceae) native to Romanian southern sub-Carpathian hills. METHODS: The prepared hydroethanolic extract of Juniperus communis L. was characterized by GC-MS, HPLC, UV-Vis spectrometry and phytochemical assays. The antioxidant potential was evaluated using the DPPH assay, the antifungal effect was studied on Aspergillus niger ATCC 15475 and Penicillium hirsutum ATCC 52323, while the genoprotective effect was evaluated using the Allium cepa assay. The anti-inflammatory effect was evaluated in two inflammation experimental models (dextran and kaolin) by plethysmometry. Male Wistar rats were treated by gavage with distilled water (negative control), the microemulsion (positive control), diclofenac sodium aqueous solution (reference) and microemulsions containing juniper extract (experimental group). The initial paw volume and the paw volumes at 1, 2, 3, 4, 5 and 24 h were measured. RESULTS: Total terpenoids, phenolics and flavonoids were estimated to be 13.44 ± 0.14 mg linalool equivalent, 19.23 ± 1.32 mg gallic acid equivalent, and 5109.6 ± 21.47 mg rutin equivalent per 100 g of extract, respectively. GC-MS characterization of the juniper extract identified 57 volatile compounds in the sample, while the HPLC analysis revealed the presence of the selected compounds (α-pinene, chlorogenic acid, rutin, apigenin, quercitin). The antioxidant potential of the crude extract was found to be 81.63 ± 0.38% (measured by the DPPH method). The results of the antifungal activity assay (for Aspergillus niger and Penicillium hirsutum) were 21.6 mm, respectively 17.2 mm as inhibition zone. Test results demonstrated the genoprotective potential of J. communis undiluted extract, inhibiting the mitodepressive effect of ethanol. The anti-inflammatory action of the juniper extract, administered as microemulsion in acute-dextran model was increased when compared to kaolin subacute inflammation induced model. CONCLUSION: The hydroalcoholic extract obtained from wild-growing Juniperus communis native to Romanian southern sub-Carpathian hills has genoprotective, antioxidant, antifungal and anti-inflammatory properties.
[Mh] Termos MeSH primário: Anti-Inflamatórios/farmacologia
Antifúngicos/farmacologia
Juniperus/química
Extratos Vegetais/farmacologia
Substâncias Protetoras/farmacologia
[Mh] Termos MeSH secundário: Animais
Anti-Inflamatórios/química
Antifúngicos/química
Aspergillus niger/efeitos dos fármacos
Compostos de Bifenilo/análise
Compostos de Bifenilo/metabolismo
Flavonoides/química
Flavonoides/farmacologia
Inflamação/metabolismo
Masculino
Penicillium/efeitos dos fármacos
Fenóis/química
Fenóis/farmacologia
Picratos/análise
Picratos/metabolismo
Extratos Vegetais/química
Substâncias Protetoras/química
Ratos
Ratos Wistar
Romênia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anti-Inflammatory Agents); 0 (Antifungal Agents); 0 (Biphenyl Compounds); 0 (Flavonoids); 0 (Phenols); 0 (Picrates); 0 (Plant Extracts); 0 (Protective Agents); DFD3H4VGDH (1,1-diphenyl-2-picrylhydrazyl)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180216
[Lr] Data última revisão:
180216
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180106
[St] Status:MEDLINE
[do] DOI:10.1186/s12906-017-2066-8


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[PMID]:28745425
[Au] Autor:Filipov Y; Domanskyi S; Wood ML; Gamella M; Privman V; Katz E
[Ad] Endereço:Department of Chemistry and Biomolecular Science, Clarkson University, Potsdam, NY, 13699, USA.
[Ti] Título:Experimental Realization of a High-Quality Biochemical XOR Gate.
[So] Source:Chemphyschem;18(20):2908-2915, 2017 Oct 19.
[Is] ISSN:1439-7641
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:We report an experimental realization of a biochemical XOR gate function that avoids many of the pitfalls of earlier realizations based on biocatalytic cascades. Inputs-represented by pairs of chemicals-cross-react to largely cancel out when both are nearly equal. The cross-reaction can be designed to also optimize gate functioning for noise handling. When not equal, the residual inputs are further processed to result in the output of the XOR type, by biocatalytic steps that allow for further gate-function optimization. The quality of the realized XOR gate is theoretically analyzed.
[Mh] Termos MeSH primário: Álcool Desidrogenase/metabolismo
Oxirredutases do Álcool/metabolismo
Biocatálise
Glucose Oxidase/metabolismo
Hexoquinase/metabolismo
NAD/metabolismo
Peroxidase/metabolismo
[Mh] Termos MeSH secundário: Armoracia/enzimologia
Aspergillus niger/enzimologia
Modelos Moleculares
Pichia/enzimologia
Saccharomyces cerevisiae/enzimologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0U46U6E8UK (NAD); EC 1.1.- (Alcohol Oxidoreductases); EC 1.1.1.1 (Alcohol Dehydrogenase); EC 1.1.3.13 (alcohol oxidase); EC 1.1.3.4 (Glucose Oxidase); EC 1.11.1.7 (Peroxidase); EC 2.7.1.1 (Hexokinase)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180215
[Lr] Data última revisão:
180215
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170727
[St] Status:MEDLINE
[do] DOI:10.1002/cphc.201700705


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[PMID]:29304048
[Au] Autor:Pu S; Ma H; Deng D; Xue S; Zhu R; Zhou Y; Xiong X
[Ad] Endereço:State Key Laboratory of Geohazard Prevention and Geoenvironment Protection (Chengdu University of Technology), Chengdu, Sichuan, P.R. China.
[Ti] Título:Isolation, identification, and characterization of an Aspergillus niger bioflocculant-producing strain using potato starch wastewater as nutrilite and its application.
[So] Source:PLoS One;13(1):e0190236, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:A bioflocculant (MBFA18) was produced by Aspergillus niger (A18) using potato starch wastewater (PSW) as nutrients. The cultivation processes and flocculating treatment for PSW purification were systematically studied. The flocculating rate of the MBFA 18 achieved 90.06% (kaolin clay) under the optimal cultivation condition (PSW with 5950 mg/L COD, 20 g/L glucose, 0.2 g/L urea and without phosphorus source addition and pH adjustment). Furthermore, effects of flocculant dosage, initial pH, coagulant aid (CaCl2) addition and sedimentation time on the PSW treatment were discussed and studied in detail. The optimum flocculation treatment conditions were determined according to the treatment efficiency, cost and flocculation conditions. During the PSW treatment, 2 mL/L bioflocculant (1.89 g/L) dosage and 0.5 mol/L coagulant aid addition were applied without pH adjustment and 91.15% COD and 60.22% turbidity removal rate could be achieved within 20 min. The comparative study between the bioflocculant and conventional chemical flocculants showed excellent flocculating efficiency of MBFA 18 with lower cost (4.7 yuan/t), which indicated that the bioflocculant MBFA 18 produced in PSW substrate has a great potential to be an alternative flocculant in PSW treatment.
[Mh] Termos MeSH primário: Aspergillus niger/isolamento & purificação
Solanum tuberosum/metabolismo
Amido/metabolismo
Águas Residuais
[Mh] Termos MeSH secundário: Aspergillus niger/metabolismo
Floculação
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Waste Water); 9005-25-8 (Starch)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180210
[Lr] Data última revisão:
180210
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180106
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0190236


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[PMID]:29281693
[Au] Autor:Amaike Campen S; Lynn J; Sibert SJ; Srikrishnan S; Phatale P; Feldman T; Guenther JM; Hiras J; Tran YTA; Singer SW; Adams PD; Sale KL; Simmons BA; Baker SE; Magnuson JK; Gladden JM
[Ad] Endereço:Joint BioEnergy Institute (JBEI), Biological Systems & Engineering Division, Lawrence Berkeley National Laboratory, California, United States of America.
[Ti] Título:Expression of naturally ionic liquid-tolerant thermophilic cellulases in Aspergillus niger.
[So] Source:PLoS One;12(12):e0189604, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Efficient deconstruction of plant biomass is a major barrier to the development of viable lignocellulosic biofuels. Pretreatment with ionic liquids reduces lignocellulose recalcitrance to enzymatic hydrolysis, increasing yields of sugars for conversion into biofuels. However, commercial cellulases are not compatible with many ionic liquids, necessitating extensive water washing of pretreated biomass prior to hydrolysis. To circumvent this issue, previous research has demonstrated that several thermophilic bacterial cellulases can efficiently deconstruct lignocellulose in the presence of the ionic liquid, 1-ethyl-3-methylimadizolium acetate. As promising as these enzymes are, they would need to be produced at high titer in an industrial enzyme production host before they could be considered a viable alternative to current commercial cellulases. Aspergillus niger has been used to produce high titers of secreted enzymes in industry and therefore, we assessed the potential of this organism to be used as an expression host for these ionic liquid-tolerant cellulases. We demonstrated that 29 of these cellulases were expressed at detectable levels in a wild-type strain of A. niger, indicating a basic level of compatibility and potential to be produced at high levels in a host engineered to produce high titers of enzymes. We then profiled one of these enzymes in detail, the ß-glucosidase A5IL97, and compared versions expressed in both A. niger and Escherichia coli. This comparison revealed the enzymatic activity of A5IL97 purified from E. coli and A. niger is equivalent, suggesting that A. niger could be an excellent enzyme production host for enzymes originally characterized in E. coli, facilitating the transition from the laboratory to industry.
[Mh] Termos MeSH primário: Aspergillus niger/enzimologia
Celulases/metabolismo
Líquidos Iônicos/metabolismo
[Mh] Termos MeSH secundário: Biomassa
Celulases/genética
Escherichia coli/genética
Fermentação
Hidrólise
Proteínas Recombinantes/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
0 (Ionic Liquids); 0 (Recombinant Proteins); EC 3.2.1.- (Cellulases)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180129
[Lr] Data última revisão:
180129
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171228
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0189604


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[PMID]:27770422
[Au] Autor:Hickey DP
[Ad] Endereço:Department of Chemistry, University of Utah, 315 S 1400 E, Salt Lake City, UT, 84112, USA. dhickeychem@gmail.com.
[Ti] Título:Ferrocene-Modified Linear Poly(ethylenimine) for Enzymatic Immobilization and Electron Mediation.
[So] Source:Methods Mol Biol;1504:181-191, 2017.
[Is] ISSN:1940-6029
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Enzymatic glucose biosensors and biofuel cells make use of the electrochemical transduction between an oxidoreductase enzyme, such as glucose oxidase (GOx), and an electrode to either quantify the amount of glucose in a solution or generate electrical energy. However, many enzymes including GOx are not able to electrochemically interact with an electrode surface directly, but require an external electrochemical relay to shuttle electrons to the electrode. Ferrocene-modified linear poly(ethylenimine) (Fc-LPEI) redox polymers have been designed to simultaneously immobilize glucose oxidase (GOx) at an electrode and mediate electron transfer from their flavin adenine dinucleotide (FAD) active site to the electrode surface. Cross-linked films of Fc-LPEI create hydrogel networks that allow for rapid transport of glucose, while the covalently bound ferrocene moieties are able to facilitate rapid electron transfer due to the ability of ferrocene to exchange electrons between adjacent ferrocene residues. For these reasons, Fc-LPEI films have been widely used in the development of high current density bioanode materials. This chapter describes the synthesis of a commonly used dimethylferrocene-modified linear poly(ethylenimine), as well as the subsequent preparation and electrochemical characterization of a GOx bioanode film utilizing the synthesized polymer.
[Mh] Termos MeSH primário: Aspergillus niger/enzimologia
Técnicas Biossensoriais/métodos
Enzimas Imobilizadas/química
Compostos Ferrosos/química
Glucose Oxidase/química
Glucose/análise
Metalocenos/química
Polietilenoimina/análogos & derivados
[Mh] Termos MeSH secundário: Aspergillus niger/química
Aspergillus niger/metabolismo
Eletrodos
Transporte de Elétrons
Elétrons
Enzimas Imobilizadas/metabolismo
Glucose/metabolismo
Glucose Oxidase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Enzymes, Immobilized); 0 (Ferrous Compounds); 0 (Metallocenes); 9002-98-6 (Polyethyleneimine); EC 1.1.3.4 (Glucose Oxidase); IY9XDZ35W2 (Glucose); U96PKG90JQ (ferrocene)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180115
[Lr] Data última revisão:
180115
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161023
[St] Status:MEDLINE


  9 / 4802 MEDLINE  
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[PMID]:27770424
[Au] Autor:Suroviec AH
[Ad] Endereço:Department of Chemistry and Biochemistry, Berry College, 2277 Martha Berry Highway, Mt. Berry, GA, 30149-4005, USA. asuroviec@berry.edu.
[Ti] Título:Layer-by-Layer Assembly of Glucose Oxidase on Carbon Nanotube Modified Electrodes.
[So] Source:Methods Mol Biol;1504:203-213, 2017.
[Is] ISSN:1940-6029
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The use of enzymatically modified electrodes for the detection of glucose or other non-electrochemically active analytes is becoming increasingly common. Direct heterogeneous electron transfer to glucose oxidase has been shown to be kinetically difficult, which is why electron transfer mediators or indirect detection is usually used for monitoring glucose with electrochemical sensors. It has been found, however, that electrodes modified with single or multi-walled carbon nanotubes (CNTs) demonstrate fast heterogeneous electron transfer kinetics as compared to that found for traditional electrodes. Incorporating CNTs into the assembly of electrochemical glucose sensors, therefore, affords the possibility of facile electron transfer to glucose oxidase, and a more direct determination of glucose. This chapter describes the methods used to use CNTs in a layer-by-layer structure along with glucose oxidase to produce an enzymatically modified electrode with high turnover rates, increased stability and shelf-life.
[Mh] Termos MeSH primário: Aspergillus niger/enzimologia
Enzimas Imobilizadas/química
Glucose Oxidase/química
Nanotubos de Carbono/química
[Mh] Termos MeSH secundário: Aspergillus niger/química
Aspergillus niger/metabolismo
Técnicas Biossensoriais/métodos
Técnicas Eletroquímicas/métodos
Eletrodos
Transporte de Elétrons
Enzimas Imobilizadas/metabolismo
Glucose/análise
Glucose/metabolismo
Glucose Oxidase/metabolismo
Modelos Moleculares
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Enzymes, Immobilized); 0 (Nanotubes, Carbon); EC 1.1.3.4 (Glucose Oxidase); IY9XDZ35W2 (Glucose)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180115
[Lr] Data última revisão:
180115
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161023
[St] Status:MEDLINE


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[PMID]:27770421
[Au] Autor:VandeZande GR; Olvany JM; Rutherford JL; Rasmussen M
[Ad] Endereço:Chemistry Department, Lebanon Valley College, 101 N College Avenue, Annville, PA, 17003-1400, USA.
[Ti] Título:Enzyme Immobilization and Mediation with Osmium Redox Polymers.
[So] Source:Methods Mol Biol;1504:165-179, 2017.
[Is] ISSN:1940-6029
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Enzymatic electrodes are becoming increasingly common for energy production and sensing applications. Research over the past several decades has addressed a major issue that can occur when using these biocatalysts, i.e., slow heterogeneous electron transfer, by incorporation of a redox active species to act as an electron shuttle. There are several advantages to immobilizing both the enzyme and mediator at the enzyme surface, including increased electron transfer rates, decreased enzyme leaching, and minimized diffusion limitations. Redox polymers consisting of a redox active center attached to a polymer backbone are a particularly attractive option because they have high self-exchange rates for electron transfer and tunable redox potential. Osmium (Os) polymers are the most well studied of this type of polymer for bioelectrocatalysis. Here, we describe the methods to synthesize one of the most common Os redox polymers and how it can be used to fabricate glucose oxidase electrodes. Procedures are also outlined for evaluating the enzymatic electrodes.
[Mh] Termos MeSH primário: 2,2´-Dipiridil/análogos & derivados
Aspergillus niger/enzimologia
Enzimas Imobilizadas/química
Glucose Oxidase/química
Osmio/química
Polímeros/química
[Mh] Termos MeSH secundário: Aspergillus niger/química
Aspergillus niger/metabolismo
Técnicas Biossensoriais/métodos
Técnicas Eletroquímicas/métodos
Eletrodos
Transporte de Elétrons
Enzimas Imobilizadas/metabolismo
Glucose/análise
Glucose/metabolismo
Glucose Oxidase/metabolismo
Imidazóis/química
Modelos Moleculares
Oxirredução
Polivinil/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Enzymes, Immobilized); 0 (Imidazoles); 0 (Polymers); 0 (Polyvinyls); 0 (poly(1-vinylimidazole)); 2E7M255OPY (Osmium); 551W113ZEP (2,2'-Dipyridyl); EC 1.1.3.4 (Glucose Oxidase); IY9XDZ35W2 (Glucose)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180115
[Lr] Data última revisão:
180115
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161023
[St] Status:MEDLINE



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