867 resultados para biochemical ecology


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In Southern Brazil, Aegla parana Schmitt, 1942 is characterized by a broad distribution throughout the Iguacu River basin, particularly between the southern state of Parana and the northern state of Santa Catarina, preferentially inhabiting streams with rocky substrates. Although there has been an increase in the number of studies about the population biology of Aeglidae, many aspects about the reproductive biology of A. parana are still unknown. Therefore, the present study aimed to investigate the size at sexual maturity, reproductive seasonality and recruitment of A. parana from November, 2008 to December, 2009, in a tributary of the Iguacu River located in Uniao da Vitoria, Parana, Brazil. Basic environmental factors were investigated to determine their influence on the reproductive cycle of this species. Gonadal stages were characterized macroscopically, and the presence or absence of embryos in females (ovigerous females) from monthly samples was recorded. The entire sample was composed of 436 males and 211 females. Although the smallest ovigerous female was 16.2 mm, the average size (carapace length, CL) at sexual maturity (CL50%) was calculated at 17.4 mm. The greatest percentage of females with developed (mature, near spawning) gonads stage was observed from January to June, 2009, while ovigerous females were recorded from April to July, 2009, after which the reproductive period ended. Recruitment occurred from October to December, 2009. The presence of ovigerous females was negatively correlated with temperature (Spearman, p < 0.05). Females carrying embryos were generally collected during periods of lower temperatures, whereas recruits entered the population during periods of higher temperatures, when food for them is more abundant in the region studied.

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Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)

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Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

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Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

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An extracellular pectin lyase secreted by Fusarium decemcellulare MTCC 2079 under solid state fermentation condition has been purified to electrophoretic homogeniety by using ammonium sulfate fractionation, carboxymethyl cellulose and gel filtration (Sephadex G-100) column chromatographies. The purified enzyme showed single protein band corresponding to molecular mass 45 +/- 01 kDa on sodium dodecyl sulfate polyacrylamide gel electrophoresis. The enzyme had maximum activity at pH 9.0 and showed maximum stability in the pH range of 9.0-12.0. The optimum temperature of the purified enzyme was 50 degrees C and it showed maximum stability upto 40 degrees C. The energy of activation for the thermal denaturation (Ea) was 59.06 kJ mol(-1) K-1. The K-m and k(cat) values using citrus pectin as the substrate were 0.125mgml(-1) and 72.9 s(-1) in 100mM sodium carbonate buffer pH 9.0 at 50 degrees C. The biophysical studies on pectin lyase showed that its secondary structure belongs to alpha+beta class of protein with comparatively less of beta-sheets. Purified pectin lyase showed efficient retting of Crotolaria juncea fibers.

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Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

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Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

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Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)

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Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)

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Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)

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Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

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Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)