Caracterização bioquímica de lipase extraída de sementes oleaginosas de Pachira aquatica

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

Estudos bioquímicos de tegumento de soja brasileira: isolamento, purificação e caracterização de peroxidase com guaiacol como substrato

Pós-graduação em Biotecnologia - IQ

'Beta'-D-frutofuranosidases de Fusarium graminearum: produção, purificação, imobilização e determinação das propriedades bioquímicas de enzimas solúveis e secas em Spray dryer

Pós-graduação em Biotecnologia - IQ

Produção de tanases por Emericella nivea : purificação e caracterização bioquímica

Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)

Glucoamilases mutantes termoestáveis do fungo Aspergillus awamori expressas em levedura Saccharomyces cerevisiae: Sequenciamento do gene, produção e purificação das enzimas obtidas por fermentação submersa

Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)

Purificação e caracterização da poligalacturonase termoestável produzida pela linhagem fúngica Thermomucor indicae-seudaticae N31 em fermentação em estado sólido e submersa

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

Purificação e caracterização bioquímica de poligalacturonases termoestáveis produzidas pelo fungo Thermoascus aurantiacus através de fermentação submersa e fermentação em estado sólido

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

Produção, purificação e propriedades bioquímicas de lipase ácida de Candida viswanathii

Pós-graduação em Ciências Biológicas (Microbiologia Aplicada) - IBRC

Caracterização funcional e estrutural de uma ?-glucanase GH12 de Aspergillus terreus

Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)

Kinetic role of a histidine residue in the T1 copper site of the laccase from Rigidoporus lignosus

Laccases (benzendiol:oxygen oxidoreductases; EC 1.10.3.2) catalyze the oxidation of a broad range of substrates, such as polyphenols, dyes and pollutants, and thus these enzymes are widely applied in industrial, biotechnological and environmental fields. In order to improve their biotechnological applications, a deep knowledge of structural factors involved in controlling their activity, in various experimental conditions and on different substrates, is required. In the present study, a laccase from the mushroom Rigidoporus lignosus was kinetically characterized. In particular, the stability, the effects of pH, ionic strength and fluoride ion concentration on the kinetic parameters were investigated, using three di-hydroxy-benzene isomers (1,2-dihydroxy-benzene, 1,3-dihydroxy-benzene and 1,4-dihydroxy-benzene) as substrates. The catalytic constant values of the laccase showed a bell-shaped pH profile, with the same optimum pH and pK(a) values for all tested substrates. This behavior appears to be due to the presence of an ionizable residue in the enzyme active site. To identify this residue, the enzyme was derivatized with diethylpyrocarbonate to modify accessible histidine residues, which, according to structural data, are present in the active site of this enzyme. The kinetic behavior of the derivatized laccase was compared with that of the native enzyme and the derivatized residues were identified by mass spectrometry. Mass spectrometry and kinetic results suggest the main role of His-457 in the control of the catalytic activity of laccase from R. lignosus. (C) 2013 Elsevier B.V. All rights reserved.

Cyclodextrin Production by Bacillus lehensis Isolated from Cassava Starch: Characterisation of a Novel Enzyme

The properties of a previously unknown enzyme, denominated cyclodextrin glycosyltransferase, produced from Bacillus lehensis, were evaluated using affinity chromatography for protein purification. Enzyme characteristics (optimum pH and temperature; pH and temperature stability), the influence of substances on the enzyme activity, enzyme kinetics, and cyclodextrin production were analysed. Cyclodextrin glycosyltransferase was purified up to 320.74-fold by affinity chromatography using beta-cyclodextrin as the binder and it exhibited 8.71% activity recovery. This enzyme is a monomer with a molecular weight of 81.27 kDa, as estimated by SDS-PAGE. Optimum temperature and pH for cydodextrin glycosyltransferase were 55 degrees C and 8.0, respectively. The Michaelis-Menten constant was 8.62 g/l during maximum velocity of 0.858 g/l.h.

Production and Characterization of a Milk-clotting Protease Produced in Submerged Fermentation by the Thermophilic Fungus Thermomucor indicae-seudaticae N31

Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)

DIGESTIVE PROTEASES FROM WILD AND FARMED MALE MORPHOTYPES OF THE AMAZON RIVER PRAWN (MACROBRACHIUM AMAZONICUM)

Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)

Molecular and Kinetic Characterization of Two Extracellular Xylanases Isolated from Leucoagaricus gongylophorus

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

Biochemical characterisation and application of lipases produced by Aspergillus sp on solid-state fermentation using three substrates

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)