Base de dados : LILACS
Pesquisa : B03.300.390.400.158.400 [Categoria DeCS]
Referências encontradas : 3 [refinar]
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Id: biblio-1047727
Autor: Nadeem, Muhammad Shahid; Al-Ghamdi, Maryam A; Khan, Jalaluddin Azam; Sadath, Saida; Al-Malki, Abdulaziz.
Título: Recombinant production and biochemical and in silico characterization of lactate dehydrogenase from Geobacillus thermodenitrificans DSM-465
Fonte: Electron. j. biotechnol;35:18-24, sept. 2018. ilus, tab, graf.
Idioma: en.
Resumo: Background: Lactate dehydrogenase (LDH) is an enzyme of glycolytic pathway, ubiquitously found in living organisms. Increased glycolysis and LDH activity are associated with many pathologic conditions including inflammation and cancer, thereby making the enzyme a suitable drug target. Studies on conserved structural and functional domains of LDH from various species reveal novel inhibitory molecules. Our study describes Escherichia coli production and characterization of a moderately thermostable LDH (LDH-GT) from Geobacillus thermodenitrificans DSM-465. An in silico 3D model of recombinant enzyme and molecular docking with a set of potential inhibitors are also described. Results: The recombinant enzyme was overexpressed in E. coli and purified to electrophoretic homogeneity. The molecular weight of the enzyme determined by MALDI-TOF was 34,798.96 Da. It exhibited maximum activity at 65°C and pH 7.5 with a KM value for pyruvate as 45 µM. LDH-GT and human LDH-A have only 35.6% identity in the amino acid sequence. On the contrary, comparison by in silico structural alignment reveals that LDH-GT monomer has approximately 80% identity to that of truncated LDH-A. The amino acids "GEHGD" as well as His179 and His193 in the active site are conserved. Docking studies have shown the binding free energy changes of potential inhibitors with LDH-A and LDH-GT ranging from −407.11 to −127.31 kJ mol−1 . Conclusions: By highlighting the conserved structural and functional domains of LDH from two entirely different species, this study has graded potential inhibitory molecules on the basis of their binding affinities so that they can be applied for in vivo anticancer studies
Descritores: Geobacillus/enzimologia
L-Lactato Desidrogenase/metabolismo
-Simulação por Computador
Estabilidade Enzimática
Reação em Cadeia da Polimerase
Clonagem Molecular
Escherichia coli/metabolismo
Simulação de Acoplamento Molecular
Glicólise
L-Lactato Desidrogenase/genética
Responsável: CL1.1 - Biblioteca Central


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Id: biblio-839336
Autor: Petkauskaite, Raimonda; Blom, Jochen; Goesmann, Alexander; Kuisiene, Nomeda.
Título: Draft genome sequence of pectic polysaccharide-degrading moderate thermophilic bacterium Geobacillus thermodenitrificans DSM 101594
Fonte: Braz. j. microbiol;48(1):7-8, Jan.-Mar. 2017. tab.
Idioma: en.
Projeto: “TermozymOS’ project of the National Research Programme “Healthy and Safe Food” by the Lithuanian Science Council.
Resumo: Abstract Geobacillus thermodenitrificans DSM 101594 was isolated as a producer of extracellular thermostable pectic polysaccharide degrading enzymes. The completely sequenced genome was 3.6 Mb in length with GC content of 48.86%. A number of genes encoding enzymatic active against the high molecular weight polysaccharides of potential biotechnological importance were identified in the genome.
Descritores: Genoma Bacteriano
Genômica
Geobacillus/genética
Sequenciamento de Nucleotídeos em Larga Escala
-Pectinas/metabolismo
Biologia Computacional/métodos
Genômica/métodos
Geobacillus/metabolismo
Anotação de Sequência Molecular
Responsável: BR1.1 - BIREME


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Id: biblio-1017382
Autor: Mamimin, Chonticha; Prasertsan, Poonsuk; Kongjan, Prawit; O-Thong, Sompong.
Título: Effects of volatile fatty acids in biohydrogen effluent on biohythane production from palm oil mill effluent under thermophilic condition
Fonte: Electron. j. biotechnol;29:78-85, sept. 2017. tab, graf, ilus.
Idioma: en.
Projeto: Khon Kaen University; . Thailand Research Fund.
Resumo: Background: Biohydrogen effluent contains a high concentration of volatile fatty acid (VFA) mainly as butyric, acetic, lactic and propionic acids. The presence of various VFAs (mixture VFAs) and their cooperative effects on two-stage biohythane production need to be further studied. The effect of VFA concentrations in biohydrogen effluent of palm oil mill effluent (POME) on methane yield in methane stage of biohythane production was investigated. Results: The methane yield obtained in low VFA loading (0.9 and 1.8 g/L) was 15­20% times greater than that of high VFA loading (3.6 and 4.7 g/L). Butyric acid at high concentrations (8 g/L) has the individual significantly negative effect the methane production process (P b 0.05). Lactic, acetic and butyric acid mixed with propionic acid at a concentration higher than 0.5 g/L has an interaction significantly negative effect on the methanogenesis process (P b 0.05). Inhibition condition had a negative effect on both bacteria and archaea with inhibited on Geobacillus sp., Thermoanaerobacterium thermosaccharolyticum, Methanoculleus thermophilus and Methanothermobacter delfuvii resulting in low methane yield. Conclusion: Preventing the high concentration of butyric acid, and propionic acid in the hydrogenic effluent could enhance methane production in two-stage anaerobic digestion for biohythane production.
Descritores: Propionatos/metabolismo
Butiratos/metabolismo
Águas Residuárias/microbiologia
Metano/biossíntese
-Propionatos/análise
Butiratos/análise
Óleo de Palmeira
Methanobacteriaceae
Archaea
Methanomicrobiaceae
Geobacillus
Fermentação
Águas Residuárias/análise
Hidrogênio
Anaerobiose
Responsável: CL1.1 - Biblioteca Central



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