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Pesquisa : D08.811.682.047.150.270 [Categoria DeCS]
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[PMID]:28667014
[Au] Autor:Corkins ME; Wilson S; Cocuron JC; Alonso AP; Bird AJ
[Ad] Endereço:From the Department of Molecular Genetics.
[Ti] Título:The gluconate shunt is an alternative route for directing glucose into the pentose phosphate pathway in fission yeast.
[So] Source:J Biol Chem;292(33):13823-13832, 2017 Aug 18.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Glycolysis and the pentose phosphate pathway both play a central role in the degradation of glucose in all domains of life. Another metabolic route that can facilitate glucose breakdown is the gluconate shunt. In this shunt glucose dehydrogenase and gluconate kinase catalyze the two-step conversion of glucose into the pentose phosphate pathway intermediate 6-phosphogluconate. Despite the presence of these enzymes in many organisms, their only established role is in the production of 6-phosphogluconate for the Entner-Doudoroff pathway. In this report we performed metabolic profiling on a strain of lacking the zinc-responsive transcriptional repressor Loz1 with the goal of identifying metabolic pathways that were altered by cellular zinc status. This profiling revealed that Δ cells accumulate higher levels of gluconate. We show that the altered gluconate levels in Δ cells result from increased expression of By analyzing the activity of recombinant Gcd1 and by measuring gluconate levels in strains lacking enzymes of the gluconate shunt we demonstrate that Gcd1 encodes a novel NADP -dependent glucose dehydrogenase that acts in a pathway with the Idn1 gluconate kinase. We also find that cells lacking and , which encode the first enzyme in the pentose phosphate pathway, have a more severe growth phenotype than cells lacking We propose that in Gcd1 and Idn1 act together to shunt glucose into the pentose phosphate pathway, creating an alternative route for directing glucose into the pentose phosphate pathway that bypasses hexokinase and the rate-limiting enzyme glucose-6-phosphate dehydrogenase.
[Mh] Termos MeSH primário: Glucose Desidrogenase/metabolismo
Glucosefosfato Desidrogenase/metabolismo
Via de Pentose Fosfato
Fosfotransferases (Aceptor do Grupo Álcool)/metabolismo
Proteínas de Schizosaccharomyces pombe/metabolismo
Schizosaccharomyces/enzimologia
Fatores de Transcrição/metabolismo
[Mh] Termos MeSH secundário: Metabolismo Energético
Deleção de Genes
Gluconatos/metabolismo
Glucose Desidrogenase/genética
Glucosefosfato Desidrogenase/genética
Metabolômica/métodos
Fosfotransferases (Aceptor do Grupo Álcool)/genética
Proteínas Recombinantes/metabolismo
Schizosaccharomyces/crescimento & desenvolvimento
Schizosaccharomyces/metabolismo
Proteínas de Schizosaccharomyces pombe/genética
Fatores de Transcrição/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Gluconates); 0 (Loz1 protein, S pombe); 0 (Recombinant Proteins); 0 (Schizosaccharomyces pombe Proteins); 0 (Transcription Factors); EC 1.1.1.- (Gcd1 protein, S pombe); EC 1.1.1.- (Glucose Dehydrogenases); EC 1.1.1.49 (Glucosephosphate Dehydrogenase); EC 1.1.1.49 (Zwf1 protein, S pombe); EC 2.7.1.- (Idn1 protein, S pombe); EC 2.7.1.- (Phosphotransferases (Alcohol Group Acceptor)); EC 2.7.1.12 (gluconokinase); R4R8J0Q44B (gluconic acid)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170906
[Lr] Data última revisão:
170906
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170702
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.798488


  2 / 521 MEDLINE  
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[PMID]:28287419
[Au] Autor:Tsuruoka N; Sadakane T; Hayashi R; Tsujimura S
[Ad] Endereço:Division of Materials Science, Faculty of Pure and Applied Sciences, University of Tsukuba, 1-1-1 Tennodai, Tsukuba, Ibaraki 305-8573, Japan. nozomu.tsuruoka1@gmail.com.
[Ti] Título:Bimolecular Rate Constants for FAD-Dependent Glucose Dehydrogenase from Aspergillus terreus and Organic Electron Acceptors.
[So] Source:Int J Mol Sci;18(3), 2017 Mar 10.
[Is] ISSN:1422-0067
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:The flavin adenine dinucleotide-dependent glucose dehydrogenase (FAD-GDH) from species require suitable redox mediators to transfer electrons from the enzyme to the electrode surface for the application of bioelectrical devices. Although several mediators for FAD-GDH are already in use, they are still far from optimum in view of potential, kinetics, sustainability, and cost-effectiveness. Herein, we investigated the efficiency of various phenothiazines and quinones in the electrochemical oxidation of FAD-GDH from . At pH 7.0, the logarithm of the bimolecular oxidation rate constants appeared to depend on the redox potentials of all the mediators tested. Notably, the rate constant of each molecule for FAD-GDH was approximately 2.5 orders of magnitude higher than that for glucose oxidase from sp. The results suggest that the electron transfer kinetics is mainly determined by the formal potential of the mediator, the driving force of electron transfer, and the electron transfer distance between the redox active site of the mediator and the FAD, affected by the steric or chemical interactions. Higher 2 values were found for ortho-quinones than for para-quinones in the reactions with FAD-GDH and glucose oxidase, which was likely due to less steric hindrance in the active site in the case of the ortho-quinones.
[Mh] Termos MeSH primário: Aspergillus/enzimologia
Flavina-Adenina Dinucleotídeo/metabolismo
Proteínas Fúngicas/metabolismo
Glucose Desidrogenase/metabolismo
[Mh] Termos MeSH secundário: Benzoquinonas/metabolismo
Cinética
Oxirredução
Fenotiazinas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Benzoquinones); 0 (Fungal Proteins); 0 (Phenothiazines); 146-14-5 (Flavin-Adenine Dinucleotide); 3T006GV98U (quinone); EC 1.1.1.- (Glucose Dehydrogenases); GS9EX7QNU6 (phenothiazine)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170420
[Lr] Data última revisão:
170420
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170314
[St] Status:MEDLINE


  3 / 521 MEDLINE  
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[PMID]:28044272
[Au] Autor:Zhang JF; Chen WQ; Chen H
[Ad] Endereço:College of Biology and Environmental Engineering, Zhejiang Shuren University, Hangzhou, 310015, China. grace_zjf@126.com.
[Ti] Título:Gene cloning and expression of a glucoside 3-dehydrogenase from Sphingobacterium faecium ZJF-D6, and used it to produce N-p-nitrophenyl-3-ketovalidamine.
[So] Source:World J Microbiol Biotechnol;33(2):21, 2017 Feb.
[Is] ISSN:1573-0972
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:In this study, we report the cloning and expression of a functional glucoside 3-dehydrogenase (G3DH) gene from Sphingobacterium faecium ZJF-D6. This gene is 1686 bp in length and encodes a peptide of 562 amino acids. The G3DH gene was successfully expressed in E. coli, and the recombinant enzyme could oxidize glucosides, galactosides and analogues at C-3 position. The sequence and multiple alignment analysis showed that the enzyme has highest identity with G3DHs from Paraglaciecola polaris LMG 21857, Aliiglaciecola lipolytica E3 and Halomonas sp. alpha-15. The recombinant G3DH was purified on Ni-NTA column and exhibited the highest activity at pH 7.6 and 30 °C. It was sensitive to acid and alkali, and showed well thermostability. The SfG3DH could oxidize a wild range of sugars. When recombinant E. coli BL21 cells were used as catalyst, a high rate of conversion to N-p-nitrophenyl-3-ketovalidamine was achieved, and no p-nitroaniline was detected. This process offers a promising approach to fulfill substrate of 3-ketovalidoxylamine A C-N lyase production.
[Mh] Termos MeSH primário: Clonagem Molecular/métodos
Glucose Desidrogenase/genética
Glucose Desidrogenase/metabolismo
Nitrofenóis/metabolismo
Sphingobacterium/enzimologia
[Mh] Termos MeSH secundário: Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Escherichia coli/genética
Escherichia coli/metabolismo
Galactosídeos/metabolismo
Glucosídeos/metabolismo
Concentração de Íons de Hidrogênio
Proteínas Recombinantes/metabolismo
Homologia de Sequência de Aminoácidos
Sphingobacterium/genética
Especificidade por Substrato
Temperatura Ambiente
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Galactosides); 0 (Glucosides); 0 (N-p-nitrophenyl-3-ketovalidamine); 0 (Nitrophenols); 0 (Recombinant Proteins); EC 1.1.1.- (Glucose Dehydrogenases); EC 1.1.99.13 (glucoside 3-dehydrogenase)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:171102
[Lr] Data última revisão:
171102
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170104
[St] Status:MEDLINE
[do] DOI:10.1007/s11274-016-2187-0


  4 / 521 MEDLINE  
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[PMID]:27573296
[Au] Autor:Sode K; Loew N; Ohnishi Y; Tsuruta H; Mori K; Kojima K; Tsugawa W; LaBelle JT; Klonoff DC
[Ad] Endereço:Department of Biotechnology, Graduate School of Engineering, Tokyo University of Agriculture and Technology, 2-24-16 Naka-cho, Koganei, Tokyo 184-8588, Japan; Institute of Global Innovation Research, Tokyo University of Agriculture and Technology, 3-8-1 Harumi-cho, Fuchu, Tokyo 183-8538, Japan; Ulti
[Ti] Título:Novel fungal FAD glucose dehydrogenase derived from Aspergillus niger for glucose enzyme sensor strips.
[So] Source:Biosens Bioelectron;87:305-311, 2017 Jan 15.
[Is] ISSN:1873-4235
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:In this study, a novel fungus FAD dependent glucose dehydrogenase, derived from Aspergillus niger (AnGDH), was characterized. This enzyme's potential for the use as the enzyme for blood glucose monitor enzyme sensor strips was evaluated, especially by investigating the effect of the presence of xylose during glucose measurements. The substrate specificity of AnGDH towards glucose was investigated, and only xylose was found as a competing substrate. The specific catalytic efficiency for xylose compared to glucose was 1.8%. The specific activity of AnGDH for xylose at 5mM concentration compared to glucose was 3.5%. No other sugars were used as substrate by this enzyme. The superior substrate specificity of AnGDH was also demonstrated in the performance of enzyme sensor strips. The impact of spiking xylose in a sample with physiological glucose concentrations on the sensor signals was investigated, and it was found that enzyme sensor strips using AnGDH were not affected at all by 5mM (75mg/dL) xylose. This is the first report of an enzyme sensor strip using a fungus derived FADGDH, which did not show any positive bias at a therapeutic level xylose concentration on the signal for a glucose sample. This clearly indicates the superiority of AnGDH over other conventionally used fungi derived FADGDHs in the application for SMBG sensor strips. The negligible activity of AnGDH towards xylose was also explained on the basis of a 3D structural model, which was compared to the 3D structures of A. flavus derived FADGDH and of two glucose oxidases.
[Mh] Termos MeSH primário: Aspergillus niger/enzimologia
Técnicas Biossensoriais/métodos
Flavina-Adenina Dinucleotídeo/metabolismo
Glucose Desidrogenase/metabolismo
Glucose/análise
[Mh] Termos MeSH secundário: Aspergillus niger/química
Aspergillus niger/metabolismo
Glucose/metabolismo
Glucose Desidrogenase/química
Seres Humanos
Modelos Moleculares
Especificidade por Substrato
Xilose/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
146-14-5 (Flavin-Adenine Dinucleotide); A1TA934AKO (Xylose); EC 1.1.1.- (Glucose Dehydrogenases); IY9XDZ35W2 (Glucose)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:170816
[Lr] Data última revisão:
170816
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160831
[St] Status:MEDLINE


  5 / 521 MEDLINE  
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[PMID]:27510979
[Au] Autor:Ozawa K; Iwasa H; Sasaki N; Kinoshita N; Hiratsuka A; Yokoyama K
[Ad] Endereço:Nanomaterials Research Institute, National Institute of Advanced Industrial Science and Technology, 1-1-1 Higashi, Tsukuba, Ibaraki, 305-8565, Japan.
[Ti] Título:Identification and characterization of thermostable glucose dehydrogenases from thermophilic filamentous fungi.
[So] Source:Appl Microbiol Biotechnol;101(1):173-183, 2017 Jan.
[Is] ISSN:1432-0614
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:FAD-dependent glucose dehydrogenase (FAD-GDH), which contains FAD as a cofactor, catalyzes the oxidation of D-glucose to D-glucono-1,5-lactone, and plays an important role in biosensors measuring blood glucose levels. In order to obtain a novel FAD-GDH gene homolog, we performed degenerate PCR screening of genomic DNAs from 17 species of thermophilic filamentous fungi. Two FAD-GDH gene homologs were identified and cloned from Talaromyces emersonii NBRC 31232 and Thermoascus crustaceus NBRC 9129. We then prepared the recombinant enzymes produced by Escherichia coli and Pichia pastoris. Absorption spectra and enzymatic assays revealed that the resulting enzymes contained oxidized FAD as a cofactor and exhibited glucose dehydrogenase activity. The transition midpoint temperatures (T ) were 66.4 and 62.5 °C for glycosylated FAD-GDHs of T. emersonii and T. crustaceus prepared by using P. pastoris as a host, respectively. Therefore, both FAD-GDHs exhibited high thermostability. In conclusion, we propose that these thermostable FAD-GDHs could be ideal enzymes for use as thermotolerant glucose sensors with high accuracy.
[Mh] Termos MeSH primário: Fungos/enzimologia
Glucose Desidrogenase/isolamento & purificação
Glucose Desidrogenase/metabolismo
Temperatura Alta
Talaromyces/enzimologia
Thermoascus/enzimologia
[Mh] Termos MeSH secundário: Clonagem Molecular
Coenzimas/análise
Estabilidade Enzimática
Escherichia coli/genética
Escherichia coli/metabolismo
Flavina-Adenina Dinucleotídeo/análise
Fungos/genética
Expressão Gênica
Glucose Desidrogenase/química
Glucose Desidrogenase/genética
Pichia/genética
Pichia/metabolismo
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/isolamento & purificação
Proteínas Recombinantes/metabolismo
Análise Espectral
Talaromyces/genética
Thermoascus/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Coenzymes); 0 (Recombinant Proteins); 146-14-5 (Flavin-Adenine Dinucleotide); EC 1.1.1.- (Glucose Dehydrogenases)
[Em] Mês de entrada:1701
[Cu] Atualização por classe:170620
[Lr] Data última revisão:
170620
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160812
[St] Status:MEDLINE
[do] DOI:10.1007/s00253-016-7754-7


  6 / 521 MEDLINE  
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[PMID]:27491947
[Au] Autor:Duine JA; Strampraad MJ; Hagen WR; de Vries S
[Ad] Endereço:Department of Biotechnology, Delft University of Technology, The Netherlands. j.a.duine@tudelft.nl.
[Ti] Título:The cooperativity effect in the reaction of soluble quinoprotein (PQQ-containing) glucose dehydrogenase is not due to subunit interaction but to substrate-assisted catalysis.
[So] Source:FEBS J;283(19):3604-3612, 2016 Oct.
[Is] ISSN:1742-4658
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Soluble quinoprotein (PQQ-containing) glucose dehydrogenase (sGDH, EC 1.1.99.35) catalyzes the oxidation of ß-d-glucose to d-glucono-δ-lactone. Although sGDH has many analytical applications, the relationship between activity and substrate concentration is not well established. Previous steady-state kinetic studies revealed a negative cooperativity effect which has recently been ascribed to subunit interaction. To investigate this conclusion, stopped-flow kinetic experiments were carried out on the reaction in which oxidized enzyme (E ) was reduced with substrates to E . The appearance of E is observed to be preceded by formation of an intermediate enzyme form, Int, which is mono-exponentially formed from E . However, the rate of conversion of Int into E depends hyperbolically on the concentration of substrate (leading to a 35-fold stimulation in the case of glucose). Evidence is provided that substrate not only binds to E but also to Int and E as well, and that the binding to Int causes the significant stimulation of Int decay. It is proposed that a proton shuffling step is involved in the decay, which is facilitated by binding of substrate to Int. Substituting the PQQ-activating Ca by a Ba ion lowered all reaction rates but did not change the stimulation factor. In summary, the previous proposal that the cooperativity effect of sGDH is due to interaction between its substrate-loaded subunits is incorrect; it is due to substrate-assisted catalysis of the enzyme. ENZYMES: EC 1.1.99.35 - soluble quinoprotein glucose dehydrogenase.
[Mh] Termos MeSH primário: Glucose Desidrogenase/química
Glucose Desidrogenase/metabolismo
[Mh] Termos MeSH secundário: Bário/química
Biocatálise
Glucose/metabolismo
Cinética
Cofator PQQ/química
Subunidades Proteicas/química
Subunidades Proteicas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Protein Subunits); 24GP945V5T (Barium); 72909-34-3 (PQQ Cofactor); EC 1.1.1.- (Glucose Dehydrogenases); IY9XDZ35W2 (Glucose)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170629
[Lr] Data última revisão:
170629
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160806
[St] Status:MEDLINE
[do] DOI:10.1111/febs.13829


  7 / 521 MEDLINE  
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[PMID]:27464830
[Au] Autor:Si Z; Zhu J; Wang W; Huang L; Wei P; Cai J; Xu Z
[Ad] Endereço:Key Laboratory of Biomass Chemical Engineering (Ministry of Education), College of Chemical and Biological Engineering, Zhejiang University, Hangzhou, 310027, People's Republic of China.
[Ti] Título:Novel and efficient screening of PQQ high-yielding strains and subsequent cultivation optimization.
[So] Source:Appl Microbiol Biotechnol;100(24):10321-10330, 2016 Dec.
[Is] ISSN:1432-0614
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:A novel and efficient screening method for pyrroloquinoline quinone (PQQ) high-yielding methylotrophic strains was developed by using glucose dehydrogenase apoenzyme (GDHA) which depended on PQQ as the cofactor. Using this high-throughput method, PQQ high-yielding strains were rapidly screened out from thousands of methylotrophic colonies at a time. The comprehensive phylogenetic analysis revealed that the highest PQQ-producing strain zju323 (CCTCC M 2016079) could be assigned to a novel species in the genus Methylobacillus of the Betaproteobacteria. After systematic optimization of different medium components and cultivation conditions, about 33.4 mg/L of PQQ was obtained after 48 h of cultivation with Methylobacillus sp. zju323 at the shake flask scale. Further cultivations of Methylobacillus sp. zju323 were carried out to investigate the biosynthesis of PQQ in 10-L bench-top fermenters. In the batch operation, the PQQ accumulation reached 78 mg/L in the broth after 53 h of cultivation. By adopting methanol feeding strategy, the highest PQQ concentration was improved up to 162.2 mg/L after 75 h of cultivation. This work developed a high-throughput strategy of screening PQQ-producing strains from soil samples and also demonstrated one potential bioprocess for large-scale PQQ production with the isolated PQQ strain.
[Mh] Termos MeSH primário: Programas de Rastreamento/métodos
Methylobacillus/crescimento & desenvolvimento
Methylobacillus/metabolismo
Cofator PQQ/metabolismo
[Mh] Termos MeSH secundário: Meios de Cultura/química
Fermentação
Glucose Desidrogenase/metabolismo
Methylobacillus/classificação
Methylobacillus/genética
Técnicas Microbiológicas/métodos
Filogenia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Culture Media); 72909-34-3 (PQQ Cofactor); EC 1.1.1.- (Glucose Dehydrogenases); EC 1.1.5.2 (glucose dehydrogenase (pyrroloquinoline-quinone))
[Em] Mês de entrada:1701
[Cu] Atualização por classe:170124
[Lr] Data última revisão:
170124
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160729
[St] Status:MEDLINE


  8 / 521 MEDLINE  
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[PMID]:26929043
[Au] Autor:Pinyou P; Ruff A; Pöller S; Ma S; Ludwig R; Schuhmann W
[Ad] Endereço:Analytical Chemistry, Center for Electrochemical Sciences (CES), Ruhr-Universität-Bochum, Universitätsstrasse 150, 44780, Bochum, Germany.
[Ti] Título:Design of an Os Complex-Modified Hydrogel with Optimized Redox Potential for Biosensors and Biofuel Cells.
[So] Source:Chemistry;22(15):5319-26, 2016 Apr 04.
[Is] ISSN:1521-3765
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Multistep synthesis and electrochemical characterization of an Os complex-modified redox hydrogel exhibiting a redox potential ≈+30 mV (vs. Ag/AgCl 3 M KCl) is demonstrated. The careful selection of bipyridine-based ligands bearing N,N-dimethylamino moieties and an amino-linker for the covalent attachment to the polymer backbone ensures the formation of a stable redox polymer with an envisaged redox potential close to 0 V. Most importantly, the formation of an octahedral N6-coordination sphere around the Os central atoms provides improved stability concomitantly with the low formal potential, a low reorganization energy during the Os(3+/2+) redox conversion and a negligible impact on oxygen reduction. By wiring a variety of enzymes such as pyrroloquinoline quinone (PQQ)-dependent glucose dehydrogenase, flavin adenine dinucleotide (FAD)-dependent glucose dehydrogenase and the FAD-dependent dehydrogenase domain of cellobiose dehydrogenase, low-potential glucose biosensors could be obtained with negligible co-oxidation of common interfering compounds such as uric acid or ascorbic acid. In combination with a bilirubin oxidase-based biocathode, enzymatic biofuel cells with open-circuit voltages of up to 0.54 V were obtained.
[Mh] Termos MeSH primário: Desidrogenases de Carboidrato/química
Complexos de Coordenação/química
Complexos de Coordenação/síntese química
Flavina-Adenina Dinucleotídeo/química
Glucose Desidrogenase/química
Hidrogel de Polietilenoglicol-Dimetacrilato/química
Osmio/química
Oxirredutases atuantes sobre Doadores de Grupo CH-CH/química
[Mh] Termos MeSH secundário: Fontes de Energia Bioelétrica
Técnicas Biossensoriais
Eletrodos
Oxirredução
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Coordination Complexes); 146-14-5 (Flavin-Adenine Dinucleotide); 25852-47-5 (Hydrogel, Polyethylene Glycol Dimethacrylate); 2E7M255OPY (Osmium); EC 1.1.- (Carbohydrate Dehydrogenases); EC 1.1.1.- (Glucose Dehydrogenases); EC 1.1.5.2 (glucose dehydrogenase (pyrroloquinoline-quinone)); EC 1.1.99.18 (cellobiose-quinone oxidoreductase); EC 1.3.- (Oxidoreductases Acting on CH-CH Group Donors); EC 1.3.3.5 (bilirubin oxidase)
[Em] Mês de entrada:1608
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160302
[St] Status:MEDLINE
[do] DOI:10.1002/chem.201504591


  9 / 521 MEDLINE  
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[PMID]:26822141
[Au] Autor:Gladisch J; Sarauli D; Schäfer D; Dietzel B; Schulz B; Lisdat F
[Ad] Endereço:Biosystems Technology, Institute for Applied Life Sciences, Technical University of Applied Sciences Wildau, Hochschulring 1, D-15745, Wildau, Germany.
[Ti] Título:Towards a novel bioelectrocatalytic platform based on "wiring" of pyrroloquinoline quinone-dependent glucose dehydrogenase with an electrospun conductive polymeric fiber architecture.
[So] Source:Sci Rep;6:19858, 2016 Jan 29.
[Is] ISSN:2045-2322
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Electrospinning is known as a fabrication technique for electrode architectures that serve as immobilization matrices for biomolecules. The current work demonstrates a novel approach to construct a conductive polymeric platform, capable not only of immobilization, but also of electrical connection of the biomolecule with the electrode. It is produced upon electrospinning from mixtures of three different highly conductive sulfonated polyanilines and polyacrylonitrile on ITO electrodes. The resulting fiber mats are with a well-retained conductivity. After coupling the enzyme pyrroloquinoline quinone-dependent glucose dehydrogenase (PQQ-GDH) to polymeric structures and addition of the substrate glucose an efficient bioelectrocatalysis is demonstrated. Depending on the choice of the sulfonated polyanilline mediatorless bioelectrocatalysis starts at low potentials; no large overpotential is needed to drive the reaction. Thus, the electrospun conductive immobilization matrix acts here as a transducing element, representing a promising strategy to use 3D polymeric scaffolds as wiring agents for active enzymes. In addition, the mild and well reproducible fabrication process and the active role of the polymer film in withdrawing electrons from the reduced PQQ-GDH lead to a system with high stability. This could provide access to a larger group of enzymes for bioelectrochemical applications including biosensors and biofuel cells.
[Mh] Termos MeSH primário: Fontes de Energia Bioelétrica
Técnicas Biossensoriais/métodos
Enzimas Imobilizadas/química
Glucose Desidrogenase/química
[Mh] Termos MeSH secundário: Condutividade Elétrica
Eletrodos
Nanotubos de Carbono/química
Cofator PQQ/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Enzymes, Immobilized); 0 (Nanotubes, Carbon); 72909-34-3 (PQQ Cofactor); EC 1.1.1.- (Glucose Dehydrogenases); EC 1.1.5.2 (glucose dehydrogenase (pyrroloquinoline-quinone))
[Em] Mês de entrada:1612
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160130
[St] Status:MEDLINE
[do] DOI:10.1038/srep19858


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[PMID]:26573634
[Au] Autor:Zeng Q; Wu X; Wen X
[Ad] Endereço:Co-Innovation Center for Sustainable Forestry in Southern China, College of Forestry, Nanjing Forestry University, Nanjing, China. qwzeng2@gmail.com.
[Ti] Título:Effects of Soluble Phosphate on Phosphate-Solubilizing Characteristics and Expression of gcd Gene in Pseudomonas frederiksbergensis JW-SD2.
[So] Source:Curr Microbiol;72(2):198-206, 2016 Feb.
[Is] ISSN:1432-0991
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Phosphate-solubilizing bacteria have the ability of solubilizing mineral phosphate in soil and promoting growth of plants, but the activity of phosphate solubilization is influenced by exogenous soluble phosphate. In the present study, the effects of soluble phosphate on the activity of phosphate solubilization, acidification of media, growth, and organic acid secretion of phosphate-solubilizing bacterium Pseudomonas frederiksbergensis JW-SD2 were investigated under six levels of soluble phosphate conditions. The activity of phosphate solubilization decreased with the increase of soluble phosphate concentration, accompanying with the increase of media pH. However, the growth was promoted by adding soluble phosphate. Production of gluconic, tartaric, and oxalic acids by the strain was reduced with the increase of concentration of soluble phosphate, while acetic and pyruvic acids showed a remarkable increase. Gluconic acid predominantly produced by the strain at low levels of soluble phosphate showed that this acid was the most efficient organic acid in phosphate solubilization. Pyrroloquinoline quinone-glucose dehydrogenase gene gcd (pg5SD2) was cloned from the strain, and the expressions of pg5SD2 gene were repressed gradually with the increase of concentration of soluble phosphate. The soluble phosphate regulating the transcription of the gcd gene is speculated to underlie the regulation of the secretion of gluconic acid and subsequently the regulation of the activity of phosphate solubilization. Future research needs to consider a molecular engineering strategy to reduce the sensitivity of PSB strain to soluble phosphate via modification of the regulatory mechanism of gcd gene, which could improve the scope of PSB strains' application.
[Mh] Termos MeSH primário: Regulação da Expressão Gênica/efeitos dos fármacos
Glucose Desidrogenase/biossíntese
Fosfatos/metabolismo
Pseudomonas/genética
Pseudomonas/metabolismo
[Mh] Termos MeSH secundário: Ácidos Carboxílicos/metabolismo
Clonagem Molecular
Meios de Cultura/química
Perfilação da Expressão Gênica
Concentração de Íons de Hidrogênio
Pseudomonas/crescimento & desenvolvimento
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Carboxylic Acids); 0 (Culture Media); 0 (Phosphates); EC 1.1.1.- (Glucose Dehydrogenases); EC 1.1.5.2 (glucose dehydrogenase (pyrroloquinoline-quinone))
[Em] Mês de entrada:1610
[Cu] Atualização por classe:170927
[Lr] Data última revisão:
170927
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151118
[St] Status:MEDLINE
[do] DOI:10.1007/s00284-015-0938-z



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