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Registro Completo |
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Biblioteca(s): |
Embrapa Gado de Leite. |
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Data corrente: |
24/04/1992 |
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Data da última atualização: |
24/04/1992 |
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Autoria: |
GUIMARAES, P. J. |
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Título: |
Capim quicuio da Amazonia; bibliografia sinaletica. |
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Ano de publicação: |
1979 |
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Fonte/Imprenta: |
Corumba: EMBRAPA-Uepae Corumba, 1979. |
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Páginas: |
"nao paginado". |
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Idioma: |
Português |
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Palavras-Chave: |
Bibliografia. |
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Thesagro: |
Capim Quicuio. |
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Thesaurus Nal: |
Amazonia. |
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Categoria do assunto: |
-- |
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Marc: |
LEADER 00392nam a2200145 a 4500
001 1583731
005 1992-04-24
008 1979 bl uuuu u0uu1 u #d
100 1 $aGUIMARAES, P. J.
245 $aCapim quicuio da Amazonia; bibliografia sinaletica.
260 $aCorumba: EMBRAPA-Uepae Corumba$c1979
300 $a"nao paginado".
650 $aAmazonia
650 $aCapim Quicuio
653 $aBibliografia
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Registro original: |
Embrapa Gado de Leite (CNPGL) |
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Registro Completo
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Biblioteca(s): |
Embrapa Agroindústria de Alimentos. |
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Data corrente: |
25/02/2010 |
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Data da última atualização: |
26/02/2010 |
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Tipo da produção científica: |
Artigo em Periódico Indexado |
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Circulação/Nível: |
B - 1 |
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Autoria: |
GREINER, R.; SILVA, L. G. da; COURI, S. |
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Afiliação: |
RALF GREINER, Federal Research Institute of Nutrition and Food-Germany; LUCINEIA GOMES DA SILVA, CEFET; SONIA COURI, CTAA. |
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Título: |
Purification and characterisation of an extracellular phytase from Aspergillus niger 11T53A9. |
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Ano de publicação: |
2009 |
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Fonte/Imprenta: |
Brazilian Journal of Microbiology, São Paulo, v. 40, n. 4, p. 795-807, oct./dec. 2009. |
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DOI: |
10.1590/S1517-83822009000400010 |
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Idioma: |
Inglês |
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Conteúdo: |
An extracellular phytase from Aspergillus niger 11T53A9 was purified about 51-fold to apparent homogeneity with a recovery of 20.3% referred to the phytase activity in the crude extract. Purification was achieved by ammonium sulphate precipitation, ion chromataography and gel filtration. The purified enzyme behaved as a monomeric protein with a molecular mass of about 85 kDa and exhibited maximal phytate-degrading activity at pH 5.0. Optimum temperature for the degradation of phytate was 55°C. The kinetic parameters for the hydrolysis of sodium phytate were determined to be KM = 54 µmol l-1 and kcat = 190 sec-1 at pH 5.0 and 37°C. The purified enzyme was rather specific for phytate dephosphorylation. It was shown that the phytase preferably dephosphorylates myo-inositol hexakisphosphate in a stereospecific way by sequential removal of phosphate groups via D-Ins(1,2,4,5,6)P5, D-Ins(1,2,5,6)P4, D-Ins(1,2,6)P3, D-Ins(1,2)P2 to finally Ins(2)P. |
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Palavras-Chave: |
Fitase. |
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Thesagro: |
Aspergillus Niger. |
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Categoria do assunto: |
X Pesquisa, Tecnologia e Engenharia |
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URL: |
https://www.scielo.br/pdf/bjm/v40n4/v40n4a10.pdf
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Marc: |
LEADER 01527naa a2200181 a 4500
001 1658932
005 2010-02-26
008 2009 bl --- 0-- u #d
024 7 $a10.1590/S1517-83822009000400010$2DOI
100 1 $aGREINER, R.
245 $aPurification and characterisation of an extracellular phytase from Aspergillus niger 11T53A9.
260 $c2009
520 $aAn extracellular phytase from Aspergillus niger 11T53A9 was purified about 51-fold to apparent homogeneity with a recovery of 20.3% referred to the phytase activity in the crude extract. Purification was achieved by ammonium sulphate precipitation, ion chromataography and gel filtration. The purified enzyme behaved as a monomeric protein with a molecular mass of about 85 kDa and exhibited maximal phytate-degrading activity at pH 5.0. Optimum temperature for the degradation of phytate was 55°C. The kinetic parameters for the hydrolysis of sodium phytate were determined to be KM = 54 µmol l-1 and kcat = 190 sec-1 at pH 5.0 and 37°C. The purified enzyme was rather specific for phytate dephosphorylation. It was shown that the phytase preferably dephosphorylates myo-inositol hexakisphosphate in a stereospecific way by sequential removal of phosphate groups via D-Ins(1,2,4,5,6)P5, D-Ins(1,2,5,6)P4, D-Ins(1,2,6)P3, D-Ins(1,2)P2 to finally Ins(2)P.
650 $aAspergillus Niger
653 $aFitase
700 1 $aSILVA, L. G. da
700 1 $aCOURI, S.
773 $tBrazilian Journal of Microbiology, São Paulo$gv. 40, n. 4, p. 795-807, oct./dec. 2009.
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Embrapa Agroindústria de Alimentos (CTAA) |
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