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Registro Completo |
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Biblioteca(s): |
Embrapa Hortaliças. |
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Data corrente: |
23/06/2009 |
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Data da última atualização: |
23/06/2009 |
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Autoria: |
OLIVEIRA, A. B. de; HERNANDEZ, F. F. F. |
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Título: |
Adsorção de nutrientes em mudas de berinjela cultivadas em substratos alternativos. |
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Ano de publicação: |
2008 |
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Fonte/Imprenta: |
Revista Ciência Agronômica, Fortaleza, v. 39, n. 4, p. 583-589, out./dez. 2008 |
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Idioma: |
Português |
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Palavras-Chave: |
Coco verde; Cultivar Florida Market; Nutrição mineral; Substrato. |
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Thesagro: |
Análise Química; Berinjela; Irrigação; Muda; Nutriente; Solanum Melongena. |
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Categoria do assunto: |
-- |
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Marc: |
LEADER 00710naa a2200241 a 4500
001 1781553
005 2009-06-23
008 2008 bl uuuu u00u1 u #d
100 1 $aOLIVEIRA, A. B. de
245 $aAdsorção de nutrientes em mudas de berinjela cultivadas em substratos alternativos.
260 $c2008
650 $aAnálise Química
650 $aBerinjela
650 $aIrrigação
650 $aMuda
650 $aNutriente
650 $aSolanum Melongena
653 $aCoco verde
653 $aCultivar Florida Market
653 $aNutrição mineral
653 $aSubstrato
700 1 $aHERNANDEZ, F. F. F.
773 $tRevista Ciência Agronômica, Fortaleza$gv. 39, n. 4, p. 583-589, out./dez. 2008
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Embrapa Hortaliças (CNPH) |
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 | Acesso ao texto completo restrito à biblioteca da Embrapa Soja. Para informações adicionais entre em contato com valeria.cardoso@embrapa.br. |
Registro Completo
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Biblioteca(s): |
Embrapa Soja. |
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Data corrente: |
10/07/2012 |
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Data da última atualização: |
03/08/2017 |
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Tipo da produção científica: |
Artigo em Periódico Indexado |
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Circulação/Nível: |
B - 2 |
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Autoria: |
YOSHIARA, L. Y.; MADEIRA, T. B.; RIBEIRO, M. L. L.; MANDARINO, J. M. G.; CARRÃO-PANIZZI, M. C.; IDA, E. I. |
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Afiliação: |
L.Y. YOSHIARA, UEL; T.B. MADEIRA, UEL; M.L.L. RIBEIRO, UEL; JOSE MARCOS GONTIJO MANDARINO, CNPSO; MERCEDES CONCORDIA CARRAO PANIZZI, CNPT; ELZA IOUKO IDA, UEL. |
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Título: |
B-glucosidase activity of soybean (Glycine max) embryonic axis germinated in the presence or absence of light. |
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Ano de publicação: |
2012 |
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Fonte/Imprenta: |
Journal of Food Biochemistry, v. 36, n. 6, p. 699-705, Dec. 2012. |
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DOI: |
doi:10.1111/j.1745-4514.2011.00585.x |
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Idioma: |
Inglês |
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Conteúdo: |
The aim of this study was to investigate the b-glucosidase activity of radicles, hypocotyls, cotyledons and epicotyls of soybeans (Glycine max) grown in the presence and absence of light and to obtain an alternative source of b-glucosidase. Seeds were germinated in the presence and absence of light at various time points, and the radicles, epicotyls, hypocotyls and cotyledons were separated. The enzymatic activity in the epicotyls presented the highest activity at 144 h in the presence of light. Specifically, the enzymatic activity of the epicotyls was sixfold higher than that of radicles and 12-fold higher than that of cotyledons. Interestingly, the specific activity of hypocotyls and cotyledons was 4.02-fold and 5.17-fold lower than that of epicotyls after 144 h of germination under light. The high specific activity of lightgerminated epicotyls suggested that the purity of b-glucosidase from epicotyls is greater than b-glucosidase obtained fromother parts of the plant. PRACTICAL APPLICATIONS: Isoflavones are beneficial to human health. Specifically, isoflavones and estrogen have similar positive effects on the symptoms of menopause and osteoporosis. Moreover, isoflavones possess antioxidant and antitumoral properties against certain cancers. In nature, the most common form of the isoflavone is the glycosylated form. Studies on the bioavailability of isoflavones indicate that these compounds behave similarly to estrogen in most biological systems and the aglycone forms aremore bioavailable than their glycoside forms. b-glucosidase is produced from the metabolism of fungi, bacteria or soybeans, and is the only enzyme capable of hydrolyzing isoflavone glycosides to aglycones. Therefore, safe and effective methods for the synthesis of b-glucosidase must be developed to produce soy-based foods with high concentrations of aglycone isoflavones. Thus, the objective of the present study is to investigate the best conditions under which the greatest amount of b-glucosidase could be isolated from soybean. MenosThe aim of this study was to investigate the b-glucosidase activity of radicles, hypocotyls, cotyledons and epicotyls of soybeans (Glycine max) grown in the presence and absence of light and to obtain an alternative source of b-glucosidase. Seeds were germinated in the presence and absence of light at various time points, and the radicles, epicotyls, hypocotyls and cotyledons were separated. The enzymatic activity in the epicotyls presented the highest activity at 144 h in the presence of light. Specifically, the enzymatic activity of the epicotyls was sixfold higher than that of radicles and 12-fold higher than that of cotyledons. Interestingly, the specific activity of hypocotyls and cotyledons was 4.02-fold and 5.17-fold lower than that of epicotyls after 144 h of germination under light. The high specific activity of lightgerminated epicotyls suggested that the purity of b-glucosidase from epicotyls is greater than b-glucosidase obtained fromother parts of the plant. PRACTICAL APPLICATIONS: Isoflavones are beneficial to human health. Specifically, isoflavones and estrogen have similar positive effects on the symptoms of menopause and osteoporosis. Moreover, isoflavones possess antioxidant and antitumoral properties against certain cancers. In nature, the most common form of the isoflavone is the glycosylated form. Studies on the bioavailability of isoflavones indicate that these compounds behave similarly to estrogen in most biological systems and the aglycone forms arem... Mostrar Tudo |
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Palavras-Chave: |
Isoflavona. |
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Categoria do assunto: |
-- |
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Marc: |
LEADER 02707naa a2200205 a 4500
001 1927991
005 2017-08-03
008 2012 bl uuuu u00u1 u #d
024 7 $adoi:10.1111/j.1745-4514.2011.00585.x$2DOI
100 1 $aYOSHIARA, L. Y.
245 $aB-glucosidase activity of soybean (Glycine max) embryonic axis germinated in the presence or absence of light.$h[electronic resource]
260 $c2012
520 $aThe aim of this study was to investigate the b-glucosidase activity of radicles, hypocotyls, cotyledons and epicotyls of soybeans (Glycine max) grown in the presence and absence of light and to obtain an alternative source of b-glucosidase. Seeds were germinated in the presence and absence of light at various time points, and the radicles, epicotyls, hypocotyls and cotyledons were separated. The enzymatic activity in the epicotyls presented the highest activity at 144 h in the presence of light. Specifically, the enzymatic activity of the epicotyls was sixfold higher than that of radicles and 12-fold higher than that of cotyledons. Interestingly, the specific activity of hypocotyls and cotyledons was 4.02-fold and 5.17-fold lower than that of epicotyls after 144 h of germination under light. The high specific activity of lightgerminated epicotyls suggested that the purity of b-glucosidase from epicotyls is greater than b-glucosidase obtained fromother parts of the plant. PRACTICAL APPLICATIONS: Isoflavones are beneficial to human health. Specifically, isoflavones and estrogen have similar positive effects on the symptoms of menopause and osteoporosis. Moreover, isoflavones possess antioxidant and antitumoral properties against certain cancers. In nature, the most common form of the isoflavone is the glycosylated form. Studies on the bioavailability of isoflavones indicate that these compounds behave similarly to estrogen in most biological systems and the aglycone forms aremore bioavailable than their glycoside forms. b-glucosidase is produced from the metabolism of fungi, bacteria or soybeans, and is the only enzyme capable of hydrolyzing isoflavone glycosides to aglycones. Therefore, safe and effective methods for the synthesis of b-glucosidase must be developed to produce soy-based foods with high concentrations of aglycone isoflavones. Thus, the objective of the present study is to investigate the best conditions under which the greatest amount of b-glucosidase could be isolated from soybean.
653 $aIsoflavona
700 1 $aMADEIRA, T. B.
700 1 $aRIBEIRO, M. L. L.
700 1 $aMANDARINO, J. M. G.
700 1 $aCARRÃO-PANIZZI, M. C.
700 1 $aIDA, E. I.
773 $tJournal of Food Biochemistry$gv. 36, n. 6, p. 699-705, Dec. 2012.
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