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	Provedor de dados BJM (2) Autor Greiner,Ralf (1) Guimarães,Valéria M. (1) Konietzny,Ursula (1) Melo,Ricardo R. de (1) Monteiro,Paulo S. (1) Rezende,Sebastião T. de (1) Mais... Palavra-chave Dephosphorylation (2) Bacterial phytase (1) Biotechnological application (1) Occurrence (1) Phosphatase (1) Phytase formation (1) Phytate (1) Phytic acid (1) Mais... Tipo do documento Info:eu-repo/semantics/article (2) Ano 2015 (1) 2004 (1) País Brazil (2) Idioma Inglês (2)		Ordenar por:  Relevância Autor Título Ano Registros recuperados: 2 Primeira ... 1 ... Última Bacterial phytase: potential application, in vivo function and regulation of its synthesis BJM Konietzny,Ursula; Greiner,Ralf. The stepwise release of phosphate from phytate, the major storage form of phosphate in plant seeds and pollen, is initiated by a class of enzymes that have been collectively called phytases. The classification is solely due to the in vitro capability of these enzymes to accept phytate as a substrate. Phytases have been studied intensively in recent years because of the great interest in such enzymes for reducing phytate content in animal feed and food for human consumption. They have a wide distribution in plants, microorganisms, and in some animal tissues. Due to several biological characteristics, such as substrate specificity, resistance to proteolysis and catalytic efficiency, bacterial phytases have considerable potential in commercial applications.... Tipo: Info:eu-repo/semantics/article Palavras-chave: Bacterial phytase; Biotechnological application; Dephosphorylation; Occurrence; Phytase formation; Phytate. Ano: 2004 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822004000100002 Isolation of a thermostable acid phytase from Aspergillus niger UFV-1 with strong proteolysis resistance BJM Monteiro,Paulo S.; Guimarães,Valéria M.; Melo,Ricardo R. de; Rezende,Sebastião T. de. An Aspergillus niger UFV-1 phytase was characterized and made available for industrial application. The enzyme was purified via ultrafiltration followed by acid precipitation, ion exchange and gel filtration chromatography. This protein exhibited a molecular mass of 161 kDa in gel filtration and 81 kDa in sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), indicating that it may be a dimer. It presented an optimum temperature of 60 °C and optimum pH of 2.0. The KM for sodium phytate hydrolysis was 30.9 mM, while the kcat and kcat/KM were 1.46 ×105 s−1 and 4.7 × 106s−1.M−1, respectively. The purified phytase exhibited broad specificity on a range of phosphorylated compounds, presenting activity on sodium phytate, p-NPP, 2-... Tipo: Info:eu-repo/semantics/article Palavras-chave: Phosphatase; Phytic acid; Dephosphorylation. Ano: 2015 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822015000100251 Registros recuperados: 2 Primeira ... 1 ... Última

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