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Ávila,Marizangela Rizzatti; Braccini,Alessandro de Lucca e; Souza,Cristina Giatti Marques de; Mandarino,José Marcos Gontijo; Bazo,Gabriel Loli; Cabral,Yara Camila Fabrin. |
The objective of this study was to evaluate physiological quality, content, and activity of antioxidants, in soybean seeds subjected to accelerated aging during different periods. Seeds of cultivars BRS 258, BRS 262 and BRS 268, subjected to accelerated aging during 12, 24, 36 and 48 hours and non-aged seeds were used. After each aging period, the seed were evaluated by tests of: germination; first count and tetrazolium. The total of phenolic compounds, total flavonoides, total of isoflavones, and activity for eliminating ABTS●+ radicals were quantified. There were differences among cultivars according to vigor and viability only after seeds were aged. Cultivars BRS 158 and BRS 268 have shown better seed physiological quality in each aging period; however,... |
Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Isoflavones; Glycine max; Phenolic compounds; Viability; Vigor. |
Ano: 2012 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0101-31222012000300006 |
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Moreira,Fabiana Guillen; Lima,Francieli Arrias de; Pedrinho,Sophia Renata Fazzano; Lenartovicz,Veridiana; Souza,Cristina Giatti Marques de; Peralta,Rosane Marina. |
A strain of Aspergillus tamarii, a filamentous fungus isolated from soil, was able to produce both <FONT FACE="Symbol">a</FONT>-amylase and glucoamylase activities in mineral media supplemented with 1% (w/v) starch or maltose as the carbon source. Static cultivation led to significantly higher yields than those obtained using shaking culture. The production of amylases was tolerant to a wide range of initial culture pH values (from 4 to 10) and temperature (from 25 to 42oC). Two amylases, one <FONT FACE="Symbol">a</FONT>-amylase and one glucoamylase, were separated by ion exchange chromatography. Both partially purified enzymes had optimal activities at pH values between 4.5 and 6.0 and were stable under acid conditions (pH... |
Tipo: Info:eu-repo/semantics/article |
Palavras-chave: < FONT FACE=Symbol> A< /FONT> -amylase Aspergillus tamarii glucoamylase. |
Ano: 1999 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0001-37141999000200014 |
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