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	Provedor de dados BJM (1) Electron. J. Biotechnol. (1) Autor Choi,Yong-Lark (2) Lee,Yong-Seok (2) Chandra,Muni Ramanna GariSubhosh (1) Chung,Soo-Yeol (1) Kim,Hae-Sun (1) Kim,Keun-Ki (1) Lee,Sang-Cheol (1) Lee,Seung-Jin (1) Park,In-Hye (1) Song,Ok-Ryul (1) Yoo,Ju-Soon (1) Mais... Palavra-chave 2-keto-3-deoxygluconate kinase (1) Burkholderia cepacia (1) Carbohydrate kinase (1) Gluconic acid (1) Glucose dehydrogenase (1) Insoluble phosphate (1) Purification (1) Serratia marcescens KCTC 2172 (1) Mais... Tipo do documento Info:eu-repo/semantics/article (1) Journal article (1) Ano 2009 (1) 2008 (1) País Brazil (1) Chile (1) Idioma Inglês (2)		Ordenar por:  Relevância Autor Título Ano Registros recuperados: 2 Primeira ... 1 ... Última Solubilization of insoluble inorganic phosphate by Burkholderia cepacia DA23 isolated from cultivated soil BJM Song,Ok-Ryul; Lee,Seung-Jin; Lee,Yong-Seok; Lee,Sang-Cheol; Kim,Keun-Ki; Choi,Yong-Lark. A mineral phosphate solubilizing bacterium, Burkholderia cepacia DA23 has been isolated from cultivated soils. Phosphate-solubilizing activities of the strain against three types of insoluble phosphate were quantitatively determined. When 3% of glucose concentration was used for carbon source, the strain had a marked mineral phosphate-solubilizing activity. Mineral phosphate solubilization was directly related to the pH drop by the strain. Analysis of the culture medium by high pressure liquid chromatography identified gluconic acid as the main organic acid released by Burkholderia cepacia DA23. Gluconic acid production was apparently the result of the glucose dehydrogenase activity and glucose dehydrogenase was affected by phosphate regulation. Tipo: Info:eu-repo/semantics/article Palavras-chave: Insoluble phosphate; Gluconic acid; Burkholderia cepacia; Glucose dehydrogenase. Ano: 2008 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822008000100030 Gene expression and characterization of 2-keto-3-deoxy-gluconate kinase, a key enzyme in the modified Entner-Doudoroff pathway of Serratia marcescens KCTC 2172 Electron. J. Biotechnol. Lee,Yong-Seok; Park,In-Hye; Yoo,Ju-Soon; Kim,Hae-Sun; Chung,Soo-Yeol; Chandra,Muni Ramanna GariSubhosh; Choi,Yong-Lark. We cloned 2-keto-3-deoxy-gluconate kinase (KDGK), which catalyzes the phosphorylation of 2-keto-3-deoxygluconate (KDG) to 2-keto-3-deoxy-6-phophogluconate (KDPG) from Serratia marcescens KCTC 2172. The nucleotide sequence revealed a single open reading frame containing 1,208 bp and encoding for 309 amino acids, with a molecular weight of 33,993 Da. The enzyme was purified via GST affinity chromatography. The putative KdgT binding site was detected upstream of the initial codon. The KDG kinase utilized 2-ketogluconate (KG) and KDG as substrates. The optimal temperature and pH for KDGK activity were 50ºC and 8.0, respectively. Tipo: Journal article Palavras-chave: 2-keto-3-deoxygluconate kinase; Carbohydrate kinase; Purification; Serratia marcescens KCTC 2172. Ano: 2009 URL: http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582009000300005 Registros recuperados: 2 Primeira ... 1 ... Última

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